Flavins and Flavoproteins 1987 : : Proceedings of the Ninth International Symposium, Atlanta, Georgia, USA, June 7–12, 1987 / / ed. by D. E. Edmondson, D. B. McCormick.

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Superior document:Title is part of eBook package: De Gruyter DGBA Physical Sciences <1990
MitwirkendeR:
Ackrell, Brian A. C.,
Aliverti, A.,
Anderson, Robert F.,
Aral, Ryohachi,
Armstrong, D. A.,
Arscott, L. David,
Astorga, Adrienne M.,
Bacher, Adelbert,
Bakx, Edwin J.,
Baldwin, T. O.,
Baldwin, Thomas O.,
Ballou, D. P.,
Ballou, David P.,
Ballou, David,
Barber, M. J.,
Bartsch, R. G.,
Bastiaens, Phil,
Batie, Christopher J.,
Becker, K.,
Beintema, Jaap J.,
Bellamy, H. D.,
Berkel, Willem J. H. van,
Berkel, Willem J.H. van,
Berry, A.,
Blanchard, J. S.,
Bohmont, Craig,
Bonants, Peter,
Bowers-Komro, D. M.,
Bowers-Komro, Delores M.,
Brandsch, Roderich,
Breakefield, Xandra O.,
Brissette, Pierre,
Brown, Kathleen,
Bryant, Christopher,
Byron, Colleen M.,
Casalin, P.,
Cecchini, Gary,
Chastain, J. L.,
Cheddar, Glen,
Chen, L. H.,
Chen, Shiuan,
Chikako, Chikako,
Chlumsky, L. J.,
Churchich, Jorge E.,
Claiborne, Al,
Cochran, Bruce,
Corey, David P.,
Curti, B.,
Cusanovich, M. A.,
Cusanovich, Michael A.,
Daubner, Susan Colette,
De Francesco, R.,
De Francesco, Raffaele,
De la Rosa, M . A .,
DeLuca, Marlene,
Decker, Karl,
Devine, J. H.,
Distefano, M.,
Distefano, Mark D.,
Drake, Donna M.,
Drenth, Jan,
Dutta, P.,
Eckstein, Jens,
Edmondson, D. E.,
Edmondson, Dale E.,
Einarsdottir, G. H.,
Eisenreich, Wolfgang,
Ellison, Patricia A.,
Engel, Paul C.,
Engelke, David R.,
Ermler, Ulrich,
Fauque, G.,
Fillat, M. F.,
Fillat, M.,
Fish, Kenneth M.,
Florence, Lederer,
Floss, Heinz G.,
Fukui, Kiyoshi,
Galliano, N.,
Ghisla, Sandra,
Ghisla, Sandro,
Ghislat, Sandro,
Giegel, David A.,
Gomez-Moreno, C.,
Grandori, R.,
Green, Jacalyn M.,
Gustafson, William G.,
Gómez-Moreno, C.,
Gückel, F.,
Hall, Carole L.,
Hall, D. O.,
Hazzard, James T.,
Hederstedt, L.,
Heelis, P. F.,
Hille, Russ,
Hinkkanen, Ari E.,
Hoek, Arie van,
Hoi, Wim G. J.,
Hol, Win G. J.,
Holden, H. M.,
Horiike, Kihachiro,
Hsu, Yun-Pung P.,
Hubera, Robert,
Husain, Mazhar,
Ichihara, Chikako,
Inagaki, Taisuke,
Innis, W. S. A.,
Innis-Whitehouse, W. S. A.,
Ishii, Yasuhiko,
Jekel, Peter A.,
Johnston, T. C.,
Jorns, Marilyn Schuman,
Jörns, Marilyn Schuman,
Kaiczyk, G. B.,
Kalk, Kor H.,
Karplus, P. A.,
Kasai, Sabu,
Kawamura-Konishi, Y.,
Kawamura-Konishi, Yasuko,
Kay, C. J.,
Kearney, Edna B.,
Keller, Paul J.,
Kim, J. J. P.,
Klapper, Michael H.,
Kodo, Keiun,
Koerber, Steven C.,
Kok, Arie de,
Koshizaka, Takuya,
Koyama, H.,
Kozioł, J.,
Krauth-Siegel, R. L.,
Krey, Grigorios D.,
Kvalnes-Krick, Kalla,
Kwok, Francis,
König, Astrid,
Laan, Jan M. van der,
Labeyrie, F.,
Ladensteina, Rudolf,
Lau, S-M.,
Laudenbach, David E.,
Le Vana, Quang,
LeGall, J.,
Lederer, F.,
Lee, J.,
Lee, James S.,
Lee, John,
Leisman, Gary,
Lim, L. W.,
Lin, J.-W.,
Lindskog, S.,
Lively, Chris R.,
Ludwig, Martha L.,
Macheroux, Peter,
Maeda, Toshihiro,
Mager, Humphrey I. X.,
Manstein, D. J.,
Manstein, Dietmar J.,
Markley, John L.,
Martin, Tracy,
Massey, V.,
Massey, Vincent,
Mathews, F. S.,
Matsuara, Hiroshi,
Matsui, Kunio,
Matthews, Rowena G.,
Mauch, Ludwig,
Mayhew, Stephen G.,
Mayhew, Steve G.,
McCormick, D. B.,
McCormick, Donald B.,
McFarland, James T.,
McWhirter, Robert B.,
Mclntire, W. S.,
Mclntire, William S.,
Merrill, A. H.,
Meyer, T. E.,
Meyer, Terrance E.,
Mierlo, Carlo P.M. van,
Mierlo, Carlo van,
Miiller, Franz,
Miller, S. M.,
Miura, R.,
Miyake, Y.,
Miyake, Yoshihiro,
Momoi, Kyoko,
Moore, M.,
Moore, Melissa J.,
Moura, I.,
Moura, J. J. G.,
Muller, F.,
Murata, M.,
Müller, Franz,
Nagata, T.,
Nagursky, Heiner,
Nakamura, Makoto,
Nakamura, Takao,
Negri, Armando,
Neujahr, Haiina Y.,
Neujahr, Halina Y.,
Nishikimi, Morimitsu,
Nishina, Yasuzo,
Nishino, T.,
Nishino, Takeshi,
Nishino, Tomoko,
Nishiyama, Kyoko,
Nisimoto, Y.,
Nitta, Satoshi,
Nozaki, Mitsuhiro,
Ohishi, Nobuko,
Ohnishi, Norihiro,
Oka, M.,
Ozawa, Takayuki,
O’Kane, D. J.,
O’Kane, Dennis J.,
O’Nuallain, Eoin M.,
Pai, E. F.,
Pai, Emil F.,
Pattridge, Katherine A.,
Peck, H. D.,
Perham, R. N.,
Pinto, J. T.,
Pollegioni, L.,
Poole, Leslie B.,
Poulsen, L. L.,
Powell, John,
Powell, P. J.,
Powlowski, Justin,
Prongay, Andrew J.,
Pueyo, J. J.,
Pust, Stefan,
Ramsay, Rona R.,
Rao, K. K.,
Ratti, S.,
Rayment, I.,
Rivlin, R. S.,
Ronchi, S.,
Sahlman, Lena,
Saint-Martin, P.,
Saito, T.,
Sancho, J.,
Sandström, A.,
Schirmer, R. H.,
Schneider, Monika,
Schopfer, Lawrence M.,
Schott, Karin,
Schreuder, Herman A.,
Schulz, G. E.,
Schulz, Georg E.,
Schwarzkopf, Bruno,
Schweitzer, D.,
Schöllhammer, T.,
Scrutton, N. S.,
Sejlitz, Torsten,
Shibata, Toshihiro,
Shiga, Kiyoshi,
Simonetta, M. Pilone,
Singer, T. P.,
Singer, Thomas P.,
Solomonson, L. P.,
Staab, H. A.,
Stankovich, M. T.,
Stankovich, Marian T.,
Steenkamp, D. J.,
Stewart, D. E.,
Stockman, Brian J.,
Straus, Neil A.,
Sugihara, J.,
Surdhar, P. S.,
Suzuki, H.,
Suzuki, Haruo,
Swarte, Myra B. A.,
Swenson, Richard P.,
Szafran, M. M.,
Takeshima, Katsuhito,
Taylor, K. L.,
Taylor, M. G.,
Tegoni, M.,
Thorpe, C.,
Thorpe, Colin,
Thunnissen, Marjolein M. G. M.,
Titlow, Christian,
Tojo, Hiroaasa,
Tojo, Hiromasa,
Tollin, Gordon,
Tsukagoshi, Norihiro,
Tsushima, K.,
Tsushima, Keizo,
Tu, S.-C.,
Tu, Shiao-Chun,
Udaka, Shigezo,
Urban, Philippe,
Ushijiaa, Hidetaka,
Utterback, Margot,
Van Beeumen, J.,
Vanin, Elio F.,
Vanoni, M. A.,
Vervoort, J.,
Vervoort, Jacques,
Visser, Antonie J. W. G.,
Visser, Antonie J.W.,
Visser, Ton,
Volka, Rainer,
Waddle, J. J.,
Walker, Mark C.,
Walsh, C. T.,
Walsh, Christopher T.,
Wampler, J. E.,
Wang, L.-H.,
Wang, Lee-Ho,
Watanabe, Fusao,
Weiner, P. K.,
Westphal, Adrie H.,
Weyer, Wicher J.,
Weyler, Walter,
Wierenga, Rik K.,
Williams, C. H.,
Williams, Charles H.,
Wong, K. K.,
Wu, J.,
Xavier, A. V.,
Xia, Z. -x.,
Yagi, Kunio,
Yamano, Toshio,
Yamazaki, K.,
Yoshikawa, Shinya,
Yu, Yimin,
Zanetti, G.,
Zeller, Hans-Dieter,
Zhou, Jing-Zhi,
Ziegler, M. M.,
Zipplies, M. F.,
HerausgeberIn:
Place / Publishing House:Berlin ;, Boston : : De Gruyter, , [2019]
©1987
Year of Publication:2019
Edition:Reprint 2019
Language:English
Online Access:
Physical Description:1 online resource (XXIII, 775 p.) :; Num. figs.
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spelling Flavins and Flavoproteins 1987 : Proceedings of the Ninth International Symposium, Atlanta, Georgia, USA, June 7–12, 1987 / ed. by D. E. Edmondson, D. B. McCormick.
Reprint 2019
Berlin ; Boston : De Gruyter, [2019]
©1987
1 online resource (XXIII, 775 p.) : Num. figs.
text txt rdacontent
computer c rdamedia
online resource cr rdacarrier
text file PDF rda
Frontmatter -- Preface -- Organizing committee -- Acknowledgements -- Contents -- STRUCTURE AND MECHANISMS OF FLAVOENZYMES -- Absolute stereochemistry of flavins in enzyme - catalyzed reactions -- Conserved cysteine pairs of mercuric ion reductase: an investigation of function via site-directed mutagenesis -- Reduced forms of native mercuric reductase and their reactions with mercuric compounds - activity vs inhibition -- Rapid-scan stopped-flow studies of the flavoenzyme mercuric reductase during catalytic turnover -- The penultimate cysteines in mercuric reductase aid in the reduction of mercury -- The active center of glutathione reductase at 1.54 A resolution -- Kinetic isotope effect studies on yeast, spinach and human erythrocyte glutathione reductases -- Excited electronic states of flavin-containing coenzyme models -- Trypanothione reductase from Trypanosoma cruzi -- Inactivation of two-electron reduced Escherichia coll glutathione reductase by NADPH and NADH -- Studies on the active site of human erythrocyte glutathione reductase using 6-SCN-FAD and 6-mercapto - FAD -- Protein engineering of glutathione reductase from Escherichia coli -- Studies on the active sites of lipoamide dehydrogenase and glutathione reductase -- Cloning, organisation and nucleotide sequence of the Azotobacter vinelandii gene for lipoamide dehydrogenase -- Reaction of pig heart lipoamide dehydrogenase with monobromoacetone and 1,3-dibromoacetone -- Site-directed mutagenesis of thioredoxin reductase -- Effects of urea on redox properties of streptococcal NADH peroxidase -- Three dimensional structure of baker's yeast flavocytochrome b2 -- Mechanism of L-lactate dehydrogenation catalyzed by flavocytochrome b.2 from baker's yeast -- Inactivation of yeast flavocytochrone b.2 with fluoropyruvate. Modification of the active site histidine -- Evidence for an alteration of the flavin behavior induced by 2-methyl - 2,4 - pentandiol in cerevis iae flavocytochrome b2 -- Medium chain acyl-CoA dehydrogenase from pig kidney: Aspects of the reductive half - reaction -- Crystal structure of the general acyl-CoA dehydrogenase -- Inactivation of general acyl-CoA dehydrogenase from pig k i dney by the suicide substrate methylenecyclopropylacetyl - CoA. Stucture of one of the covalent flavin-inhibitor adducts -- 2 - Bromo-octanoyl CoA: Apseudo-substrateforgeneral acyl-CoA dehydrogenase -- Reaction of pig kidney medium chain acyl-CoA dehydrogenase with ^ - oxidation intermediates -- Medium chain acyl-CoA dehydrogenase from pig kidney: I n activation of the reduced enzyme by 2-octynoy1-CoA -- Oxidation - reduction of general acyl-CoA dehydrogenase by the butyryl-CoA / crotonyl-CoA couple. A new investigation of the rapid reaction kinetics -- Catalytic versatility of butyryl-CoA dehydrogenase from M. elsdenii -- Oxidation-reduction potential of glutaryl-CoA dehydrogenase from Paracoccus denitrifleans -- 13C NMR studies on the complexes and reaction intermediates of D-amino acid oxidase -- 13C-,15N-, and 31P- NMR studies on 6-hydroxy-L-nicotine oxidase from Arthrobacter oxidans -- A study on the interaction between reduced D-amino acid oxidase and ligands -- D-Amino acid oxidase from the yeast Rhodotorula gracilis -- Purification and properties of D-aspartate oxidase from beef kidney -- Spectral and kinetic studies on Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating) -- Time - resolved flavin fluorescence of pyridoxine-5-P oxidase from sheep brain -- An active site thiol in lactate oxidase -- Can methylenetetrahydrofolate reductase be used to evade the methyl trap? -- The catalytic mechanism of DNA photolyase -- FLAVOENZYME STRUCTURE AND ELECTRON TRANSFER MECHANISMS -- Sequence and structure of Anacvstis nidulans flavodoxin: Comparisons with flavodoxins from other species -- C-13, N-15, and two-dimensional NMR techniques in flavoprotein research -- Two dimensional NMR studies on Megasphaera elsdenii -- Flavodoxin from Anabaena 7120: Uniform N-15 enrichment and nitrogen-15 and phosphorus - 31 NMR investigations of the FMN binding site in the reduced and oxidized states -- Pulse radiolysis studies on flavodoxin -- Resonance raman investigations of flavins and flavoproteins -- Spectral studies on hydrogen bonded alloxazines -- Use of flavin and flavodoxin semiquinones as kinetic probes to elucidate the factors which determine reaction rate constants and biological specificity for electron transfer proteins -- Factors influencing the rate of electron transfer from flavodoxin to cytochrome c. -- A computer graphics model of the complex formed between flavodoxin and the tetraheme cytochrome c.3 -- Cloning and nucleotide sequence of a bacterial flavodoxin gene: Towards the site-directed mutagenesis of the flavin binding site -- Flavin binding site differences between Photobacterium phosphoreum lumazine protein and Megasphaera elsdenii flavodoxin. An investigation using circular dichroism and fluorescence -- Ferredoxin and ferredoxin-NADP+oxidoreductase interactions: Mapping of their binding sites -- Complex formation between ferredoxin-NADP+-oxidoreductase and flavodoxin -- Mechanism of ferredoxin-NADP+ reductase reaction NADP radical, semiquinone and fully reduced enzyme-NADP+ charge transfer complex as the reaction intermediates -- In vivo deactivation/activation of ferredoxin-NADP+- oxidoreductase from the cyanobacteria Anabaena variabills -- Isolation from Desulfovibrio desulfuricans of a flavoprotein with NADH-H+ oxidoreductase activity towards a protein containing a rubredoxin-like center -- Microsomal electron transport system focused on NADPH-cytochrome P-450 reductase -- Time - resolved fluorescence spectroscopy on NADPH-cytochrome P-450 reductase -- Studies on the reactions of flavin- and nicotinamide nucleotide analogues with a bacterial electron-transferring flavoprotein -- Kinetics of ligand binding, amino acid sequence, and crystallization of Chlorobium and Chromatium flavocytochrome c. -- Redox properties of flavocytochrome c.
-- Electron transfer kinetics of phthalate oxygenase reductase, an iron sulfur center containing flavoprotein -- CD and potentiometry of the FAD of nitrate reductase -- Kinetic studies on glutamate synthase from Azospirillum bras ilense -- Redox interactions of the FAD in xanthine oxidase with other centers of the protein -- Laser flash photolysis studies of intramolecular electron transfer between the FAD and Fe/S II centers in xanthine oxidase -- Mechanism of action of chicken liver xanthine dehydrogenase -- Interconversion between O-dependent and NAD - dependent types of rat liver xanthine dehydrogenase -- Reactivity of chicken liver xanthine dehydrogenase containing artificial flavins -- The molybdenum cofactor of milk xanthine oxidase -- Isolation of a cDNA sequence coding for a part of xanthine dehydrogenase from rat liver -- FLAVIN BIOSYNTHESIS/ METABOLISM/ AND MEDICAL ASPECTS -- Biosynthesis of flavins and deazaflavins -- The icosahedral ß60 capsid of heavy riboflavin synthase (6,7- dimethyl-8-ribityllumazine synthase/riboflavin synthase) -- Characterization of human riboflavin-binding immunoglobulins -- Riboflavin uptake by isolated rat kidney cells -- Purification and characterization of the bifunctional enzyme FAD synthetase from Brevibacterium ammoniapenes -- An update on flavin metabolism in rats and humans -- Effects of quinacrine, tetracycline, adriamycin and chloroquine upon flavin metabolism in rats -- Role of flavoproteins in the neurotoxic action of MPTP -- Biosynthesis of flavoproteins -- Biological and Medical Aspects of D-Amino Acid Oxidase — Biogenesis and in vivo reaction with D-propargylglycine — -- Molecular and cellular biology of D-amino acid oxidase -- Localization of D-amino acid oxidase in rat cerebellum -- Biosynthesis of D-amino acid oxidase and molecular cloning of the cDNA -- Characterization of a partially purified nitroaryl reductase -- FLAVOENZYME HYDROXYLASES -- Crystallographic studies on the mechanism of hydroxybenzoate hydroxylase from Psudomonas fluorescens -- Applications of deuterium and tritium isotope effects to the elucidation of kinetic mechanisms of flavoprotein hydroxylases -- Chemical modification of tyrosine-38 in j>.-hydroxybenzoate hydroxylase from Pseudomonas fluorescens by 5'-Pfluorosulfonylbenzoyladenosine: A probe for the elucidation of the NADPH binding site? -- Phenol Complexes of Phenol Hydroxylase -- The involvement of SH-groups in cooperativity of phenol binding sites in phenol hydroxylase -- 6-Thiocyanate-FAD and 6-mercapto-FAD as active site probes of phenol hydroxylase -- Hysteretic behavior of anthranilate hydroxylase -- Redox potentials of salicylate hydroxylase -- The oxidative half-reaction of 2-methyl-3-hydroxypyridine-5 - carboxylic acid oxygenase from Pseudomonas sp. MA-1 -- Lipid stabilization of the flavin hydroperoxide in the microsomal flavin-containing monooxygenase -- FLAVIN-DEPENDENT BIOLUMINESCENCE -- One-electron transfers in flavin systems: Relevance to the postulated C1EEL mechanism in bacterial bioluminescence -- Characterization of new "bleached" products obtained on treating flavins and flavoproteins with dithionite -- Flavin-mediated hydrogen peroxide production by biological and chemical photosystems -- On the chemical mechanisms of bacterial luciferase, an updating -- Studies on the mechanism of bacterial bioluminescence. Evidence compatible with a one electron transfer process and a CIEEL mechanism in the luciferase reaction -- Structural analysis of bacterial luciferase -- Sequence similarity between the a subunit of luciferase from Vibrio harvevl and clostridial flavodoxin -- Isolation and characterization of a yellow fluorescent protein from Vibrio fischeri strain Y-1 -- Purification and characterization of an unusual nonfluores cent flavoprotein from Photobacterium leiognathi -- Purification and some properties of FP390 from P. phosphoreum -- STRUCTURE, MECHANISM, AND BIOSYNTHESIS OF FLAVOENZYMES CONTAINING COVALENTLY-BOUND FLAVINS -- 8α-Imidazolylflavins: Application of their redox and spectral properties to flavoenzyme systems -- X-ray study of flavoenzymes containing covalently bound flavins -- Structural studies of P-cresol methylhydroxylase -- The chemical and stereochemical course of oxidation of 4- ethylphenol and other 4-alkylphenols by ^-cresol methylhydroxylase -- Redox properties of trimethylamine dehydrogenase -- Redox properties of Escherichia coll fumarate reductase -- Reactions of lumiflavin with aminyl and a-amino radicals of piperazine -- Kinetic probes of the proposed radical mechanism of monoamine oxidase -- Stopped-flow studies on the mechanism of the oxidation of N—methyl - 4 - phenyl - 1 , 2 , 3 , 6 - tetrahydropyridine (HPTP) by monoamine oxidase -- Methoxatin containing methylamine dehydrogenase: Enzyme reduction by primary amines -- Interaction of bacterial sarcosine oxidase with folate derivatives -- Sulfhydryl groups and the binding site of noncovalently bound FAD ofCorvnebacterlum sarcosine oxidase -- Dimethylglycine dehydrogenase from pig liver mitochondria: Purification and properties -- Comparison of partial amino acid sequences deduced from the nucleotide sequence of a bovine adrenal monoamine oxidase cDNA clone to amino acid sequences obtained from bovine liver monoamine oxidase type B -- Covalent binding of FAD to Bacillus subtllis succinate dehydrogenase -- 6 - Hydroxy-D-nicotine oxidase: Expression of the flavoenzyme as a covalently flavinylated polypeptide -- The flavin-binding sites of 6-hydroxy-D- and 6-hydroxy-Lnicotine oxidase -- LIST OF PARTICIPANTS -- AUTHOR INDEX -- SUBJECT INDEX -- Backmatter
restricted access http://purl.org/coar/access_right/c_16ec online access with authorization star
Mode of access: Internet via World Wide Web.
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Description based on online resource; title from PDF title page (publisher's Web site, viewed 30. Aug 2021)
Flavine.
Flavoenzym.
SCIENCE / General. bisacsh
Ackrell, Brian A. C., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Aliverti, A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Anderson, Robert F., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Aral, Ryohachi, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Armstrong, D. A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Arscott, L. David, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Astorga, Adrienne M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Bacher, Adelbert, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Bakx, Edwin J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Baldwin, T. O., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Baldwin, Thomas O., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Ballou, D. P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Ballou, David P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Ballou, David, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Barber, M. J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Bartsch, R. G., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Bastiaens, Phil, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Batie, Christopher J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Becker, K., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Beintema, Jaap J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Bellamy, H. D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Berkel, Willem J. H. van, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Berkel, Willem J.H. van, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Berry, A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Blanchard, J. S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Bohmont, Craig, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Bonants, Peter, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Bowers-Komro, D. M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Bowers-Komro, Delores M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Brandsch, Roderich, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Breakefield, Xandra O., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Brissette, Pierre, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Brown, Kathleen, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Bryant, Christopher, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Byron, Colleen M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Casalin, P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Cecchini, Gary, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Chastain, J. L., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Cheddar, Glen, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Chen, L. H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Chen, Shiuan, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Chikako, Chikako, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Chlumsky, L. J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Churchich, Jorge E., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Claiborne, Al, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Cochran, Bruce, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Corey, David P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Curti, B., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Cusanovich, M. A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Cusanovich, Michael A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Daubner, Susan Colette, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
De Francesco, R., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
De Francesco, Raffaele, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
De la Rosa, M . A ., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
DeLuca, Marlene, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Decker, Karl, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Devine, J. H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Distefano, M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Distefano, Mark D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Drake, Donna M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Drenth, Jan, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Dutta, P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Eckstein, Jens, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Edmondson, D. E., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Edmondson, D. E., editor. edt http://id.loc.gov/vocabulary/relators/edt
Edmondson, Dale E., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Einarsdottir, G. H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Eisenreich, Wolfgang, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
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Title is part of eBook package: De Gruyter DGBA Physical Sciences <1990 9783110637243 ZDB-23-GPS
print 9783110109504
https://doi.org/10.1515/9783110884715
https://www.degruyter.com/isbn/9783110884715
Cover https://www.degruyter.com/cover/covers/9783110884715.jpg
language English
format eBook
author2 Ackrell, Brian A. C.,
Ackrell, Brian A. C.,
Aliverti, A.,
Aliverti, A.,
Anderson, Robert F.,
Anderson, Robert F.,
Aral, Ryohachi,
Aral, Ryohachi,
Armstrong, D. A.,
Armstrong, D. A.,
Arscott, L. David,
Arscott, L. David,
Astorga, Adrienne M.,
Astorga, Adrienne M.,
Bacher, Adelbert,
Bacher, Adelbert,
Bakx, Edwin J.,
Bakx, Edwin J.,
Baldwin, T. O.,
Baldwin, T. O.,
Baldwin, Thomas O.,
Baldwin, Thomas O.,
Ballou, D. P.,
Ballou, D. P.,
Ballou, David P.,
Ballou, David P.,
Ballou, David,
Ballou, David,
Barber, M. J.,
Barber, M. J.,
Bartsch, R. G.,
Bartsch, R. G.,
Bastiaens, Phil,
Bastiaens, Phil,
Batie, Christopher J.,
Batie, Christopher J.,
Becker, K.,
Becker, K.,
Beintema, Jaap J.,
Beintema, Jaap J.,
Bellamy, H. D.,
Bellamy, H. D.,
Berkel, Willem J. H. van,
Berkel, Willem J. H. van,
Berkel, Willem J.H. van,
Berkel, Willem J.H. van,
Berry, A.,
Berry, A.,
Blanchard, J. S.,
Blanchard, J. S.,
Bohmont, Craig,
Bohmont, Craig,
Bonants, Peter,
Bonants, Peter,
Bowers-Komro, D. M.,
Bowers-Komro, D. M.,
Bowers-Komro, Delores M.,
Bowers-Komro, Delores M.,
Brandsch, Roderich,
Brandsch, Roderich,
Breakefield, Xandra O.,
Breakefield, Xandra O.,
Brissette, Pierre,
Brissette, Pierre,
Brown, Kathleen,
Brown, Kathleen,
Bryant, Christopher,
Bryant, Christopher,
Byron, Colleen M.,
Byron, Colleen M.,
Casalin, P.,
Casalin, P.,
Cecchini, Gary,
Cecchini, Gary,
Chastain, J. L.,
Chastain, J. L.,
Cheddar, Glen,
Cheddar, Glen,
Chen, L. H.,
Chen, L. H.,
Chen, Shiuan,
Chen, Shiuan,
Chikako, Chikako,
Chikako, Chikako,
Chlumsky, L. J.,
Chlumsky, L. J.,
Churchich, Jorge E.,
Churchich, Jorge E.,
Claiborne, Al,
Claiborne, Al,
Cochran, Bruce,
Cochran, Bruce,
Corey, David P.,
Corey, David P.,
Curti, B.,
Curti, B.,
Cusanovich, M. A.,
Cusanovich, M. A.,
Cusanovich, Michael A.,
Cusanovich, Michael A.,
Daubner, Susan Colette,
Daubner, Susan Colette,
De Francesco, R.,
De Francesco, R.,
De Francesco, Raffaele,
De Francesco, Raffaele,
De la Rosa, M . A .,
De la Rosa, M . A .,
DeLuca, Marlene,
DeLuca, Marlene,
Decker, Karl,
Decker, Karl,
Devine, J. H.,
Devine, J. H.,
Distefano, M.,
Distefano, M.,
Distefano, Mark D.,
Distefano, Mark D.,
Drake, Donna M.,
Drake, Donna M.,
Drenth, Jan,
Drenth, Jan,
Dutta, P.,
Dutta, P.,
Eckstein, Jens,
Eckstein, Jens,
Edmondson, D. E.,
Edmondson, D. E.,
Edmondson, D. E.,
Edmondson, D. E.,
Edmondson, Dale E.,
Edmondson, Dale E.,
Einarsdottir, G. H.,
Einarsdottir, G. H.,
Eisenreich, Wolfgang,
Eisenreich, Wolfgang,
Ellison, Patricia A.,
Ellison, Patricia A.,
Engel, Paul C.,
Engel, Paul C.,
Engelke, David R.,
Engelke, David R.,
Ermler, Ulrich,
Ermler, Ulrich,
Fauque, G.,
Fauque, G.,
Fillat, M. F.,
Fillat, M. F.,
Fillat, M.,
Fillat, M.,
Fish, Kenneth M.,
Fish, Kenneth M.,
Florence, Lederer,
Florence, Lederer,
Floss, Heinz G.,
Floss, Heinz G.,
Fukui, Kiyoshi,
Fukui, Kiyoshi,
Galliano, N.,
Galliano, N.,
Ghisla, Sandra,
Ghisla, Sandra,
Ghisla, Sandro,
Ghisla, Sandro,
Ghislat, Sandro,
Ghislat, Sandro,
Giegel, David A.,
Giegel, David A.,
Gomez-Moreno, C.,
Gomez-Moreno, C.,
Grandori, R.,
Grandori, R.,
Green, Jacalyn M.,
Green, Jacalyn M.,
Gustafson, William G.,
Gustafson, William G.,
Gómez-Moreno, C.,
Gómez-Moreno, C.,
Gückel, F.,
Gückel, F.,
Hall, Carole L.,
Hall, Carole L.,
Hall, D. O.,
Hall, D. O.,
Hazzard, James T.,
Hazzard, James T.,
Hederstedt, L.,
Hederstedt, L.,
Heelis, P. F.,
Heelis, P. F.,
Hille, Russ,
Hille, Russ,
Hinkkanen, Ari E.,
Hinkkanen, Ari E.,
Hoek, Arie van,
Hoek, Arie van,
Hoi, Wim G. J.,
Hoi, Wim G. J.,
Hol, Win G. J.,
Hol, Win G. J.,
Holden, H. M.,
Holden, H. M.,
Horiike, Kihachiro,
Horiike, Kihachiro,
Hsu, Yun-Pung P.,
Hsu, Yun-Pung P.,
Hubera, Robert,
Hubera, Robert,
Husain, Mazhar,
Husain, Mazhar,
Ichihara, Chikako,
Ichihara, Chikako,
Inagaki, Taisuke,
Inagaki, Taisuke,
Innis, W. S. A.,
Innis, W. S. A.,
Innis-Whitehouse, W. S. A.,
Innis-Whitehouse, W. S. A.,
Ishii, Yasuhiko,
Ishii, Yasuhiko,
Jekel, Peter A.,
Jekel, Peter A.,
Johnston, T. C.,
Johnston, T. C.,
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Jorns, Marilyn Schuman,
Jörns, Marilyn Schuman,
Jörns, Marilyn Schuman,
Kaiczyk, G. B.,
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Kalk, Kor H.,
Kalk, Kor H.,
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Kasai, Sabu,
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Kawamura-Konishi, Y.,
Kawamura-Konishi, Yasuko,
Kawamura-Konishi, Yasuko,
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Maeda, Toshihiro,
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Manstein, D. J.,
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Manstein, Dietmar J.,
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Martin, Tracy,
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McCormick, D. B.,
McCormick, D. B.,
McCormick, D. B.,
McCormick, Donald B.,
McCormick, Donald B.,
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McFarland, James T.,
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McWhirter, Robert B.,
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Mclntire, W. S.,
Mclntire, William S.,
Mclntire, William S.,
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Moore, Melissa J.,
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Moura, I.,
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O’Kane, Dennis J.,
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Pai, E. F.,
Pai, Emil F.,
Pai, Emil F.,
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Pattridge, Katherine A.,
Peck, H. D.,
Peck, H. D.,
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Perham, R. N.,
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Pinto, J. T.,
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Poole, Leslie B.,
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Schreuder, Herman A.,
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Schwarzkopf, Bruno,
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Schweitzer, D.,
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Simonetta, M. Pilone,
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Singer, T. P.,
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Solomonson, L. P.,
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Staab, H. A.,
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Stankovich, M. T.,
Stankovich, Marian T.,
Stankovich, Marian T.,
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Steenkamp, D. J.,
Stewart, D. E.,
Stewart, D. E.,
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Stockman, Brian J.,
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Straus, Neil A.,
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Sugihara, J.,
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Surdhar, P. S.,
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Suzuki, H.,
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Suzuki, Haruo,
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Swarte, Myra B. A.,
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Swenson, Richard P.,
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Szafran, M. M.,
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Takeshima, Katsuhito,
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Taylor, K. L.,
Taylor, M. G.,
Taylor, M. G.,
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Tegoni, M.,
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Thorpe, C.,
Thorpe, Colin,
Thorpe, Colin,
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Thunnissen, Marjolein M. G. M.,
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Titlow, Christian,
Tojo, Hiroaasa,
Tojo, Hiroaasa,
Tojo, Hiromasa,
Tojo, Hiromasa,
Tollin, Gordon,
Tollin, Gordon,
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Tsukagoshi, Norihiro,
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Tsushima, K.,
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Tsushima, Keizo,
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Tu, S.-C.,
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Tu, Shiao-Chun,
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Udaka, Shigezo,
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Urban, Philippe,
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Ushijiaa, Hidetaka,
Utterback, Margot,
Utterback, Margot,
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Vanin, Elio F.,
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Vervoort, Jacques,
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Visser, Antonie J. W. G.,
Visser, Antonie J.W.,
Visser, Antonie J.W.,
Visser, Ton,
Visser, Ton,
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Volka, Rainer,
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Waddle, J. J.,
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Walker, Mark C.,
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Walsh, C. T.,
Walsh, Christopher T.,
Walsh, Christopher T.,
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Wampler, J. E.,
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Wang, L.-H.,
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Watanabe, Fusao,
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Westphal, Adrie H.,
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Weyler, Walter,
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Williams, C. H.,
Williams, Charles H.,
Williams, Charles H.,
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Wong, K. K.,
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Xavier, A. V.,
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Yoshikawa, Shinya,
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Yu, Yimin,
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Zanetti, G.,
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Zeller, Hans-Dieter,
Zhou, Jing-Zhi,
Zhou, Jing-Zhi,
Ziegler, M. M.,
Ziegler, M. M.,
Zipplies, M. F.,
Zipplies, M. F.,
author_facet Ackrell, Brian A. C.,
Ackrell, Brian A. C.,
Aliverti, A.,
Aliverti, A.,
Anderson, Robert F.,
Anderson, Robert F.,
Aral, Ryohachi,
Aral, Ryohachi,
Armstrong, D. A.,
Armstrong, D. A.,
Arscott, L. David,
Arscott, L. David,
Astorga, Adrienne M.,
Astorga, Adrienne M.,
Bacher, Adelbert,
Bacher, Adelbert,
Bakx, Edwin J.,
Bakx, Edwin J.,
Baldwin, T. O.,
Baldwin, T. O.,
Baldwin, Thomas O.,
Baldwin, Thomas O.,
Ballou, D. P.,
Ballou, D. P.,
Ballou, David P.,
Ballou, David P.,
Ballou, David,
Ballou, David,
Barber, M. J.,
Barber, M. J.,
Bartsch, R. G.,
Bartsch, R. G.,
Bastiaens, Phil,
Bastiaens, Phil,
Batie, Christopher J.,
Batie, Christopher J.,
Becker, K.,
Becker, K.,
Beintema, Jaap J.,
Beintema, Jaap J.,
Bellamy, H. D.,
Bellamy, H. D.,
Berkel, Willem J. H. van,
Berkel, Willem J. H. van,
Berkel, Willem J.H. van,
Berkel, Willem J.H. van,
Berry, A.,
Berry, A.,
Blanchard, J. S.,
Blanchard, J. S.,
Bohmont, Craig,
Bohmont, Craig,
Bonants, Peter,
Bonants, Peter,
Bowers-Komro, D. M.,
Bowers-Komro, D. M.,
Bowers-Komro, Delores M.,
Bowers-Komro, Delores M.,
Brandsch, Roderich,
Brandsch, Roderich,
Breakefield, Xandra O.,
Breakefield, Xandra O.,
Brissette, Pierre,
Brissette, Pierre,
Brown, Kathleen,
Brown, Kathleen,
Bryant, Christopher,
Bryant, Christopher,
Byron, Colleen M.,
Byron, Colleen M.,
Casalin, P.,
Casalin, P.,
Cecchini, Gary,
Cecchini, Gary,
Chastain, J. L.,
Chastain, J. L.,
Cheddar, Glen,
Cheddar, Glen,
Chen, L. H.,
Chen, L. H.,
Chen, Shiuan,
Chen, Shiuan,
Chikako, Chikako,
Chikako, Chikako,
Chlumsky, L. J.,
Chlumsky, L. J.,
Churchich, Jorge E.,
Churchich, Jorge E.,
Claiborne, Al,
Claiborne, Al,
Cochran, Bruce,
Cochran, Bruce,
Corey, David P.,
Corey, David P.,
Curti, B.,
Curti, B.,
Cusanovich, M. A.,
Cusanovich, M. A.,
Cusanovich, Michael A.,
Cusanovich, Michael A.,
Daubner, Susan Colette,
Daubner, Susan Colette,
De Francesco, R.,
De Francesco, R.,
De Francesco, Raffaele,
De Francesco, Raffaele,
De la Rosa, M . A .,
De la Rosa, M . A .,
DeLuca, Marlene,
DeLuca, Marlene,
Decker, Karl,
Decker, Karl,
Devine, J. H.,
Devine, J. H.,
Distefano, M.,
Distefano, M.,
Distefano, Mark D.,
Distefano, Mark D.,
Drake, Donna M.,
Drake, Donna M.,
Drenth, Jan,
Drenth, Jan,
Dutta, P.,
Dutta, P.,
Eckstein, Jens,
Eckstein, Jens,
Edmondson, D. E.,
Edmondson, D. E.,
Edmondson, D. E.,
Edmondson, D. E.,
Edmondson, Dale E.,
Edmondson, Dale E.,
Einarsdottir, G. H.,
Einarsdottir, G. H.,
Eisenreich, Wolfgang,
Eisenreich, Wolfgang,
Ellison, Patricia A.,
Ellison, Patricia A.,
Engel, Paul C.,
Engel, Paul C.,
Engelke, David R.,
Engelke, David R.,
Ermler, Ulrich,
Ermler, Ulrich,
Fauque, G.,
Fauque, G.,
Fillat, M. F.,
Fillat, M. F.,
Fillat, M.,
Fillat, M.,
Fish, Kenneth M.,
Fish, Kenneth M.,
Florence, Lederer,
Florence, Lederer,
Floss, Heinz G.,
Floss, Heinz G.,
Fukui, Kiyoshi,
Fukui, Kiyoshi,
Galliano, N.,
Galliano, N.,
Ghisla, Sandra,
Ghisla, Sandra,
Ghisla, Sandro,
Ghisla, Sandro,
Ghislat, Sandro,
Ghislat, Sandro,
Giegel, David A.,
Giegel, David A.,
Gomez-Moreno, C.,
Gomez-Moreno, C.,
Grandori, R.,
Grandori, R.,
Green, Jacalyn M.,
Green, Jacalyn M.,
Gustafson, William G.,
Gustafson, William G.,
Gómez-Moreno, C.,
Gómez-Moreno, C.,
Gückel, F.,
Gückel, F.,
Hall, Carole L.,
Hall, Carole L.,
Hall, D. O.,
Hall, D. O.,
Hazzard, James T.,
Hazzard, James T.,
Hederstedt, L.,
Hederstedt, L.,
Heelis, P. F.,
Heelis, P. F.,
Hille, Russ,
Hille, Russ,
Hinkkanen, Ari E.,
Hinkkanen, Ari E.,
Hoek, Arie van,
Hoek, Arie van,
Hoi, Wim G. J.,
Hoi, Wim G. J.,
Hol, Win G. J.,
Hol, Win G. J.,
Holden, H. M.,
Holden, H. M.,
Horiike, Kihachiro,
Horiike, Kihachiro,
Hsu, Yun-Pung P.,
Hsu, Yun-Pung P.,
Hubera, Robert,
Hubera, Robert,
Husain, Mazhar,
Husain, Mazhar,
Ichihara, Chikako,
Ichihara, Chikako,
Inagaki, Taisuke,
Inagaki, Taisuke,
Innis, W. S. A.,
Innis, W. S. A.,
Innis-Whitehouse, W. S. A.,
Innis-Whitehouse, W. S. A.,
Ishii, Yasuhiko,
Ishii, Yasuhiko,
Jekel, Peter A.,
Jekel, Peter A.,
Johnston, T. C.,
Johnston, T. C.,
Jorns, Marilyn Schuman,
Jorns, Marilyn Schuman,
Jörns, Marilyn Schuman,
Jörns, Marilyn Schuman,
Kaiczyk, G. B.,
Kaiczyk, G. B.,
Kalk, Kor H.,
Kalk, Kor H.,
Karplus, P. A.,
Karplus, P. A.,
Kasai, Sabu,
Kasai, Sabu,
Kawamura-Konishi, Y.,
Kawamura-Konishi, Y.,
Kawamura-Konishi, Yasuko,
Kawamura-Konishi, Yasuko,
Kay, C. J.,
Kay, C. J.,
Kearney, Edna B.,
Kearney, Edna B.,
Keller, Paul J.,
Keller, Paul J.,
Kim, J. J. P.,
Kim, J. J. P.,
Klapper, Michael H.,
Klapper, Michael H.,
Kodo, Keiun,
Kodo, Keiun,
Koerber, Steven C.,
Koerber, Steven C.,
Kok, Arie de,
Kok, Arie de,
Koshizaka, Takuya,
Koshizaka, Takuya,
Koyama, H.,
Koyama, H.,
Kozioł, J.,
Kozioł, J.,
Krauth-Siegel, R. L.,
Krauth-Siegel, R. L.,
Krey, Grigorios D.,
Krey, Grigorios D.,
Kvalnes-Krick, Kalla,
Kvalnes-Krick, Kalla,
Kwok, Francis,
Kwok, Francis,
König, Astrid,
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Labeyrie, F.,
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Lin, J.-W.,
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Macheroux, Peter,
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Maeda, Toshihiro,
Mager, Humphrey I. X.,
Mager, Humphrey I. X.,
Manstein, D. J.,
Manstein, D. J.,
Manstein, Dietmar J.,
Manstein, Dietmar J.,
Markley, John L.,
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Massey, V.,
Massey, Vincent,
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Matsuara, Hiroshi,
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Mayhew, Steve G.,
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McCormick, D. B.,
McCormick, Donald B.,
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McFarland, James T.,
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McWhirter, Robert B.,
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Mclntire, William S.,
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Merrill, A. H.,
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Meyer, T. E.,
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Mierlo, Carlo P.M. van,
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Mierlo, Carlo van,
Mierlo, Carlo van,
Miiller, Franz,
Miiller, Franz,
Miller, S. M.,
Miller, S. M.,
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Miura, R.,
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Moore, M.,
Moore, Melissa J.,
Moore, Melissa J.,
Moura, I.,
Moura, I.,
Moura, J. J. G.,
Moura, J. J. G.,
Muller, F.,
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Murata, M.,
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Müller, Franz,
Müller, Franz,
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Nagata, T.,
Nagursky, Heiner,
Nagursky, Heiner,
Nakamura, Makoto,
Nakamura, Makoto,
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Negri, Armando,
Negri, Armando,
Neujahr, Haiina Y.,
Neujahr, Haiina Y.,
Neujahr, Halina Y.,
Neujahr, Halina Y.,
Nishikimi, Morimitsu,
Nishikimi, Morimitsu,
Nishina, Yasuzo,
Nishina, Yasuzo,
Nishino, T.,
Nishino, T.,
Nishino, Takeshi,
Nishino, Takeshi,
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Nishino, Tomoko,
Nishiyama, Kyoko,
Nishiyama, Kyoko,
Nisimoto, Y.,
Nisimoto, Y.,
Nitta, Satoshi,
Nitta, Satoshi,
Nozaki, Mitsuhiro,
Nozaki, Mitsuhiro,
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Ohishi, Nobuko,
Ohnishi, Norihiro,
Ohnishi, Norihiro,
Oka, M.,
Oka, M.,
Ozawa, Takayuki,
Ozawa, Takayuki,
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O’Kane, D. J.,
O’Kane, Dennis J.,
O’Kane, Dennis J.,
O’Nuallain, Eoin M.,
O’Nuallain, Eoin M.,
Pai, E. F.,
Pai, E. F.,
Pai, Emil F.,
Pai, Emil F.,
Pattridge, Katherine A.,
Pattridge, Katherine A.,
Peck, H. D.,
Peck, H. D.,
Perham, R. N.,
Perham, R. N.,
Pinto, J. T.,
Pinto, J. T.,
Pollegioni, L.,
Pollegioni, L.,
Poole, Leslie B.,
Poole, Leslie B.,
Poulsen, L. L.,
Poulsen, L. L.,
Powell, John,
Powell, John,
Powell, P. J.,
Powell, P. J.,
Powlowski, Justin,
Powlowski, Justin,
Prongay, Andrew J.,
Prongay, Andrew J.,
Pueyo, J. J.,
Pueyo, J. J.,
Pust, Stefan,
Pust, Stefan,
Ramsay, Rona R.,
Ramsay, Rona R.,
Rao, K. K.,
Rao, K. K.,
Ratti, S.,
Ratti, S.,
Rayment, I.,
Rayment, I.,
Rivlin, R. S.,
Rivlin, R. S.,
Ronchi, S.,
Ronchi, S.,
Sahlman, Lena,
Sahlman, Lena,
Saint-Martin, P.,
Saint-Martin, P.,
Saito, T.,
Saito, T.,
Sancho, J.,
Sancho, J.,
Sandström, A.,
Sandström, A.,
Schirmer, R. H.,
Schirmer, R. H.,
Schneider, Monika,
Schneider, Monika,
Schopfer, Lawrence M.,
Schopfer, Lawrence M.,
Schott, Karin,
Schott, Karin,
Schreuder, Herman A.,
Schreuder, Herman A.,
Schulz, G. E.,
Schulz, G. E.,
Schulz, Georg E.,
Schulz, Georg E.,
Schwarzkopf, Bruno,
Schwarzkopf, Bruno,
Schweitzer, D.,
Schweitzer, D.,
Schöllhammer, T.,
Schöllhammer, T.,
Scrutton, N. S.,
Scrutton, N. S.,
Sejlitz, Torsten,
Sejlitz, Torsten,
Shibata, Toshihiro,
Shibata, Toshihiro,
Shiga, Kiyoshi,
Shiga, Kiyoshi,
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Simonetta, M. Pilone,
Singer, T. P.,
Singer, T. P.,
Singer, Thomas P.,
Singer, Thomas P.,
Solomonson, L. P.,
Solomonson, L. P.,
Staab, H. A.,
Staab, H. A.,
Stankovich, M. T.,
Stankovich, M. T.,
Stankovich, Marian T.,
Stankovich, Marian T.,
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Steenkamp, D. J.,
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Stewart, D. E.,
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Stockman, Brian J.,
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Straus, Neil A.,
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Swarte, Myra B. A.,
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Swenson, Richard P.,
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Szafran, M. M.,
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Taylor, K. L.,
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Thorpe, C.,
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Thorpe, Colin,
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Thunnissen, Marjolein M. G. M.,
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Titlow, Christian,
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Tojo, Hiroaasa,
Tojo, Hiromasa,
Tojo, Hiromasa,
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Tollin, Gordon,
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Tsukagoshi, Norihiro,
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Tsushima, K.,
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Tsushima, Keizo,
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Walsh, C. T.,
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Weiner, P. K.,
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Westphal, Adrie H.,
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Weyer, Wicher J.,
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Wierenga, Rik K.,
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Yamazaki, K.,
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Yoshikawa, Shinya,
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Zanetti, G.,
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Zeller, Hans-Dieter,
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a j w g v ajwg ajwgv
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a j v aj ajv
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author_sort Ackrell, Brian A. C.,
title Flavins and Flavoproteins 1987 : Proceedings of the Ninth International Symposium, Atlanta, Georgia, USA, June 7–12, 1987 /
spellingShingle Flavins and Flavoproteins 1987 : Proceedings of the Ninth International Symposium, Atlanta, Georgia, USA, June 7–12, 1987 /
Frontmatter --
Preface --
Organizing committee --
Acknowledgements --
Contents --
STRUCTURE AND MECHANISMS OF FLAVOENZYMES --
Absolute stereochemistry of flavins in enzyme - catalyzed reactions --
Conserved cysteine pairs of mercuric ion reductase: an investigation of function via site-directed mutagenesis --
Reduced forms of native mercuric reductase and their reactions with mercuric compounds - activity vs inhibition --
Rapid-scan stopped-flow studies of the flavoenzyme mercuric reductase during catalytic turnover --
The penultimate cysteines in mercuric reductase aid in the reduction of mercury --
The active center of glutathione reductase at 1.54 A resolution --
Kinetic isotope effect studies on yeast, spinach and human erythrocyte glutathione reductases --
Excited electronic states of flavin-containing coenzyme models --
Trypanothione reductase from Trypanosoma cruzi --
Inactivation of two-electron reduced Escherichia coll glutathione reductase by NADPH and NADH --
Studies on the active site of human erythrocyte glutathione reductase using 6-SCN-FAD and 6-mercapto - FAD --
Protein engineering of glutathione reductase from Escherichia coli --
Studies on the active sites of lipoamide dehydrogenase and glutathione reductase --
Cloning, organisation and nucleotide sequence of the Azotobacter vinelandii gene for lipoamide dehydrogenase --
Reaction of pig heart lipoamide dehydrogenase with monobromoacetone and 1,3-dibromoacetone --
Site-directed mutagenesis of thioredoxin reductase --
Effects of urea on redox properties of streptococcal NADH peroxidase --
Three dimensional structure of baker's yeast flavocytochrome b2 --
Mechanism of L-lactate dehydrogenation catalyzed by flavocytochrome b.2 from baker's yeast --
Inactivation of yeast flavocytochrone b.2 with fluoropyruvate. Modification of the active site histidine --
Evidence for an alteration of the flavin behavior induced by 2-methyl - 2,4 - pentandiol in cerevis iae flavocytochrome b2 --
Medium chain acyl-CoA dehydrogenase from pig kidney: Aspects of the reductive half - reaction --
Crystal structure of the general acyl-CoA dehydrogenase --
Inactivation of general acyl-CoA dehydrogenase from pig k i dney by the suicide substrate methylenecyclopropylacetyl - CoA. Stucture of one of the covalent flavin-inhibitor adducts --
2 - Bromo-octanoyl CoA: Apseudo-substrateforgeneral acyl-CoA dehydrogenase --
Reaction of pig kidney medium chain acyl-CoA dehydrogenase with ^ - oxidation intermediates --
Medium chain acyl-CoA dehydrogenase from pig kidney: I n activation of the reduced enzyme by 2-octynoy1-CoA --
Oxidation - reduction of general acyl-CoA dehydrogenase by the butyryl-CoA / crotonyl-CoA couple. A new investigation of the rapid reaction kinetics --
Catalytic versatility of butyryl-CoA dehydrogenase from M. elsdenii --
Oxidation-reduction potential of glutaryl-CoA dehydrogenase from Paracoccus denitrifleans --
13C NMR studies on the complexes and reaction intermediates of D-amino acid oxidase --
13C-,15N-, and 31P- NMR studies on 6-hydroxy-L-nicotine oxidase from Arthrobacter oxidans --
A study on the interaction between reduced D-amino acid oxidase and ligands --
D-Amino acid oxidase from the yeast Rhodotorula gracilis --
Purification and properties of D-aspartate oxidase from beef kidney --
Spectral and kinetic studies on Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating) --
Time - resolved flavin fluorescence of pyridoxine-5-P oxidase from sheep brain --
An active site thiol in lactate oxidase --
Can methylenetetrahydrofolate reductase be used to evade the methyl trap? --
The catalytic mechanism of DNA photolyase --
FLAVOENZYME STRUCTURE AND ELECTRON TRANSFER MECHANISMS --
Sequence and structure of Anacvstis nidulans flavodoxin: Comparisons with flavodoxins from other species --
C-13, N-15, and two-dimensional NMR techniques in flavoprotein research --
Two dimensional NMR studies on Megasphaera elsdenii --
Flavodoxin from Anabaena 7120: Uniform N-15 enrichment and nitrogen-15 and phosphorus - 31 NMR investigations of the FMN binding site in the reduced and oxidized states --
Pulse radiolysis studies on flavodoxin --
Resonance raman investigations of flavins and flavoproteins --
Spectral studies on hydrogen bonded alloxazines --
Use of flavin and flavodoxin semiquinones as kinetic probes to elucidate the factors which determine reaction rate constants and biological specificity for electron transfer proteins --
Factors influencing the rate of electron transfer from flavodoxin to cytochrome c. --
A computer graphics model of the complex formed between flavodoxin and the tetraheme cytochrome c.3 --
Cloning and nucleotide sequence of a bacterial flavodoxin gene: Towards the site-directed mutagenesis of the flavin binding site --
Flavin binding site differences between Photobacterium phosphoreum lumazine protein and Megasphaera elsdenii flavodoxin. An investigation using circular dichroism and fluorescence --
Ferredoxin and ferredoxin-NADP+oxidoreductase interactions: Mapping of their binding sites --
Complex formation between ferredoxin-NADP+-oxidoreductase and flavodoxin --
Mechanism of ferredoxin-NADP+ reductase reaction NADP radical, semiquinone and fully reduced enzyme-NADP+ charge transfer complex as the reaction intermediates --
In vivo deactivation/activation of ferredoxin-NADP+- oxidoreductase from the cyanobacteria Anabaena variabills --
Isolation from Desulfovibrio desulfuricans of a flavoprotein with NADH-H+ oxidoreductase activity towards a protein containing a rubredoxin-like center --
Microsomal electron transport system focused on NADPH-cytochrome P-450 reductase --
Time - resolved fluorescence spectroscopy on NADPH-cytochrome P-450 reductase --
Studies on the reactions of flavin- and nicotinamide nucleotide analogues with a bacterial electron-transferring flavoprotein --
Kinetics of ligand binding, amino acid sequence, and crystallization of Chlorobium and Chromatium flavocytochrome c. --
Redox properties of flavocytochrome c.
--
Electron transfer kinetics of phthalate oxygenase reductase, an iron sulfur center containing flavoprotein --
CD and potentiometry of the FAD of nitrate reductase --
Kinetic studies on glutamate synthase from Azospirillum bras ilense --
Redox interactions of the FAD in xanthine oxidase with other centers of the protein --
Laser flash photolysis studies of intramolecular electron transfer between the FAD and Fe/S II centers in xanthine oxidase --
Mechanism of action of chicken liver xanthine dehydrogenase --
Interconversion between O-dependent and NAD - dependent types of rat liver xanthine dehydrogenase --
Reactivity of chicken liver xanthine dehydrogenase containing artificial flavins --
The molybdenum cofactor of milk xanthine oxidase --
Isolation of a cDNA sequence coding for a part of xanthine dehydrogenase from rat liver --
FLAVIN BIOSYNTHESIS/ METABOLISM/ AND MEDICAL ASPECTS --
Biosynthesis of flavins and deazaflavins --
The icosahedral ß60 capsid of heavy riboflavin synthase (6,7- dimethyl-8-ribityllumazine synthase/riboflavin synthase) --
Characterization of human riboflavin-binding immunoglobulins --
Riboflavin uptake by isolated rat kidney cells --
Purification and characterization of the bifunctional enzyme FAD synthetase from Brevibacterium ammoniapenes --
An update on flavin metabolism in rats and humans --
Effects of quinacrine, tetracycline, adriamycin and chloroquine upon flavin metabolism in rats --
Role of flavoproteins in the neurotoxic action of MPTP --
Biosynthesis of flavoproteins --
Biological and Medical Aspects of D-Amino Acid Oxidase — Biogenesis and in vivo reaction with D-propargylglycine — --
Molecular and cellular biology of D-amino acid oxidase --
Localization of D-amino acid oxidase in rat cerebellum --
Biosynthesis of D-amino acid oxidase and molecular cloning of the cDNA --
Characterization of a partially purified nitroaryl reductase --
FLAVOENZYME HYDROXYLASES --
Crystallographic studies on the mechanism of hydroxybenzoate hydroxylase from Psudomonas fluorescens --
Applications of deuterium and tritium isotope effects to the elucidation of kinetic mechanisms of flavoprotein hydroxylases --
Chemical modification of tyrosine-38 in j>.-hydroxybenzoate hydroxylase from Pseudomonas fluorescens by 5'-Pfluorosulfonylbenzoyladenosine: A probe for the elucidation of the NADPH binding site? --
Phenol Complexes of Phenol Hydroxylase --
The involvement of SH-groups in cooperativity of phenol binding sites in phenol hydroxylase --
6-Thiocyanate-FAD and 6-mercapto-FAD as active site probes of phenol hydroxylase --
Hysteretic behavior of anthranilate hydroxylase --
Redox potentials of salicylate hydroxylase --
The oxidative half-reaction of 2-methyl-3-hydroxypyridine-5 - carboxylic acid oxygenase from Pseudomonas sp. MA-1 --
Lipid stabilization of the flavin hydroperoxide in the microsomal flavin-containing monooxygenase --
FLAVIN-DEPENDENT BIOLUMINESCENCE --
One-electron transfers in flavin systems: Relevance to the postulated C1EEL mechanism in bacterial bioluminescence --
Characterization of new "bleached" products obtained on treating flavins and flavoproteins with dithionite --
Flavin-mediated hydrogen peroxide production by biological and chemical photosystems --
On the chemical mechanisms of bacterial luciferase, an updating --
Studies on the mechanism of bacterial bioluminescence. Evidence compatible with a one electron transfer process and a CIEEL mechanism in the luciferase reaction --
Structural analysis of bacterial luciferase --
Sequence similarity between the a subunit of luciferase from Vibrio harvevl and clostridial flavodoxin --
Isolation and characterization of a yellow fluorescent protein from Vibrio fischeri strain Y-1 --
Purification and characterization of an unusual nonfluores cent flavoprotein from Photobacterium leiognathi --
Purification and some properties of FP390 from P. phosphoreum --
STRUCTURE, MECHANISM, AND BIOSYNTHESIS OF FLAVOENZYMES CONTAINING COVALENTLY-BOUND FLAVINS --
8α-Imidazolylflavins: Application of their redox and spectral properties to flavoenzyme systems --
X-ray study of flavoenzymes containing covalently bound flavins --
Structural studies of P-cresol methylhydroxylase --
The chemical and stereochemical course of oxidation of 4- ethylphenol and other 4-alkylphenols by ^-cresol methylhydroxylase --
Redox properties of trimethylamine dehydrogenase --
Redox properties of Escherichia coll fumarate reductase --
Reactions of lumiflavin with aminyl and a-amino radicals of piperazine --
Kinetic probes of the proposed radical mechanism of monoamine oxidase --
Stopped-flow studies on the mechanism of the oxidation of N—methyl - 4 - phenyl - 1 , 2 , 3 , 6 - tetrahydropyridine (HPTP) by monoamine oxidase --
Methoxatin containing methylamine dehydrogenase: Enzyme reduction by primary amines --
Interaction of bacterial sarcosine oxidase with folate derivatives --
Sulfhydryl groups and the binding site of noncovalently bound FAD ofCorvnebacterlum sarcosine oxidase --
Dimethylglycine dehydrogenase from pig liver mitochondria: Purification and properties --
Comparison of partial amino acid sequences deduced from the nucleotide sequence of a bovine adrenal monoamine oxidase cDNA clone to amino acid sequences obtained from bovine liver monoamine oxidase type B --
Covalent binding of FAD to Bacillus subtllis succinate dehydrogenase --
6 - Hydroxy-D-nicotine oxidase: Expression of the flavoenzyme as a covalently flavinylated polypeptide --
The flavin-binding sites of 6-hydroxy-D- and 6-hydroxy-Lnicotine oxidase --
LIST OF PARTICIPANTS --
AUTHOR INDEX --
SUBJECT INDEX --
Backmatter
title_sub Proceedings of the Ninth International Symposium, Atlanta, Georgia, USA, June 7–12, 1987 /
title_full Flavins and Flavoproteins 1987 : Proceedings of the Ninth International Symposium, Atlanta, Georgia, USA, June 7–12, 1987 / ed. by D. E. Edmondson, D. B. McCormick.
title_fullStr Flavins and Flavoproteins 1987 : Proceedings of the Ninth International Symposium, Atlanta, Georgia, USA, June 7–12, 1987 / ed. by D. E. Edmondson, D. B. McCormick.
title_full_unstemmed Flavins and Flavoproteins 1987 : Proceedings of the Ninth International Symposium, Atlanta, Georgia, USA, June 7–12, 1987 / ed. by D. E. Edmondson, D. B. McCormick.
title_auth Flavins and Flavoproteins 1987 : Proceedings of the Ninth International Symposium, Atlanta, Georgia, USA, June 7–12, 1987 /
title_alt Frontmatter --
Preface --
Organizing committee --
Acknowledgements --
Contents --
STRUCTURE AND MECHANISMS OF FLAVOENZYMES --
Absolute stereochemistry of flavins in enzyme - catalyzed reactions --
Conserved cysteine pairs of mercuric ion reductase: an investigation of function via site-directed mutagenesis --
Reduced forms of native mercuric reductase and their reactions with mercuric compounds - activity vs inhibition --
Rapid-scan stopped-flow studies of the flavoenzyme mercuric reductase during catalytic turnover --
The penultimate cysteines in mercuric reductase aid in the reduction of mercury --
The active center of glutathione reductase at 1.54 A resolution --
Kinetic isotope effect studies on yeast, spinach and human erythrocyte glutathione reductases --
Excited electronic states of flavin-containing coenzyme models --
Trypanothione reductase from Trypanosoma cruzi --
Inactivation of two-electron reduced Escherichia coll glutathione reductase by NADPH and NADH --
Studies on the active site of human erythrocyte glutathione reductase using 6-SCN-FAD and 6-mercapto - FAD --
Protein engineering of glutathione reductase from Escherichia coli --
Studies on the active sites of lipoamide dehydrogenase and glutathione reductase --
Cloning, organisation and nucleotide sequence of the Azotobacter vinelandii gene for lipoamide dehydrogenase --
Reaction of pig heart lipoamide dehydrogenase with monobromoacetone and 1,3-dibromoacetone --
Site-directed mutagenesis of thioredoxin reductase --
Effects of urea on redox properties of streptococcal NADH peroxidase --
Three dimensional structure of baker's yeast flavocytochrome b2 --
Mechanism of L-lactate dehydrogenation catalyzed by flavocytochrome b.2 from baker's yeast --
Inactivation of yeast flavocytochrone b.2 with fluoropyruvate. Modification of the active site histidine --
Evidence for an alteration of the flavin behavior induced by 2-methyl - 2,4 - pentandiol in cerevis iae flavocytochrome b2 --
Medium chain acyl-CoA dehydrogenase from pig kidney: Aspects of the reductive half - reaction --
Crystal structure of the general acyl-CoA dehydrogenase --
Inactivation of general acyl-CoA dehydrogenase from pig k i dney by the suicide substrate methylenecyclopropylacetyl - CoA. Stucture of one of the covalent flavin-inhibitor adducts --
2 - Bromo-octanoyl CoA: Apseudo-substrateforgeneral acyl-CoA dehydrogenase --
Reaction of pig kidney medium chain acyl-CoA dehydrogenase with ^ - oxidation intermediates --
Medium chain acyl-CoA dehydrogenase from pig kidney: I n activation of the reduced enzyme by 2-octynoy1-CoA --
Oxidation - reduction of general acyl-CoA dehydrogenase by the butyryl-CoA / crotonyl-CoA couple. A new investigation of the rapid reaction kinetics --
Catalytic versatility of butyryl-CoA dehydrogenase from M. elsdenii --
Oxidation-reduction potential of glutaryl-CoA dehydrogenase from Paracoccus denitrifleans --
13C NMR studies on the complexes and reaction intermediates of D-amino acid oxidase --
13C-,15N-, and 31P- NMR studies on 6-hydroxy-L-nicotine oxidase from Arthrobacter oxidans --
A study on the interaction between reduced D-amino acid oxidase and ligands --
D-Amino acid oxidase from the yeast Rhodotorula gracilis --
Purification and properties of D-aspartate oxidase from beef kidney --
Spectral and kinetic studies on Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating) --
Time - resolved flavin fluorescence of pyridoxine-5-P oxidase from sheep brain --
An active site thiol in lactate oxidase --
Can methylenetetrahydrofolate reductase be used to evade the methyl trap? --
The catalytic mechanism of DNA photolyase --
FLAVOENZYME STRUCTURE AND ELECTRON TRANSFER MECHANISMS --
Sequence and structure of Anacvstis nidulans flavodoxin: Comparisons with flavodoxins from other species --
C-13, N-15, and two-dimensional NMR techniques in flavoprotein research --
Two dimensional NMR studies on Megasphaera elsdenii --
Flavodoxin from Anabaena 7120: Uniform N-15 enrichment and nitrogen-15 and phosphorus - 31 NMR investigations of the FMN binding site in the reduced and oxidized states --
Pulse radiolysis studies on flavodoxin --
Resonance raman investigations of flavins and flavoproteins --
Spectral studies on hydrogen bonded alloxazines --
Use of flavin and flavodoxin semiquinones as kinetic probes to elucidate the factors which determine reaction rate constants and biological specificity for electron transfer proteins --
Factors influencing the rate of electron transfer from flavodoxin to cytochrome c. --
A computer graphics model of the complex formed between flavodoxin and the tetraheme cytochrome c.3 --
Cloning and nucleotide sequence of a bacterial flavodoxin gene: Towards the site-directed mutagenesis of the flavin binding site --
Flavin binding site differences between Photobacterium phosphoreum lumazine protein and Megasphaera elsdenii flavodoxin. An investigation using circular dichroism and fluorescence --
Ferredoxin and ferredoxin-NADP+oxidoreductase interactions: Mapping of their binding sites --
Complex formation between ferredoxin-NADP+-oxidoreductase and flavodoxin --
Mechanism of ferredoxin-NADP+ reductase reaction NADP radical, semiquinone and fully reduced enzyme-NADP+ charge transfer complex as the reaction intermediates --
In vivo deactivation/activation of ferredoxin-NADP+- oxidoreductase from the cyanobacteria Anabaena variabills --
Isolation from Desulfovibrio desulfuricans of a flavoprotein with NADH-H+ oxidoreductase activity towards a protein containing a rubredoxin-like center --
Microsomal electron transport system focused on NADPH-cytochrome P-450 reductase --
Time - resolved fluorescence spectroscopy on NADPH-cytochrome P-450 reductase --
Studies on the reactions of flavin- and nicotinamide nucleotide analogues with a bacterial electron-transferring flavoprotein --
Kinetics of ligand binding, amino acid sequence, and crystallization of Chlorobium and Chromatium flavocytochrome c. --
Redox properties of flavocytochrome c.
--
Electron transfer kinetics of phthalate oxygenase reductase, an iron sulfur center containing flavoprotein --
CD and potentiometry of the FAD of nitrate reductase --
Kinetic studies on glutamate synthase from Azospirillum bras ilense --
Redox interactions of the FAD in xanthine oxidase with other centers of the protein --
Laser flash photolysis studies of intramolecular electron transfer between the FAD and Fe/S II centers in xanthine oxidase --
Mechanism of action of chicken liver xanthine dehydrogenase --
Interconversion between O-dependent and NAD - dependent types of rat liver xanthine dehydrogenase --
Reactivity of chicken liver xanthine dehydrogenase containing artificial flavins --
The molybdenum cofactor of milk xanthine oxidase --
Isolation of a cDNA sequence coding for a part of xanthine dehydrogenase from rat liver --
FLAVIN BIOSYNTHESIS/ METABOLISM/ AND MEDICAL ASPECTS --
Biosynthesis of flavins and deazaflavins --
The icosahedral ß60 capsid of heavy riboflavin synthase (6,7- dimethyl-8-ribityllumazine synthase/riboflavin synthase) --
Characterization of human riboflavin-binding immunoglobulins --
Riboflavin uptake by isolated rat kidney cells --
Purification and characterization of the bifunctional enzyme FAD synthetase from Brevibacterium ammoniapenes --
An update on flavin metabolism in rats and humans --
Effects of quinacrine, tetracycline, adriamycin and chloroquine upon flavin metabolism in rats --
Role of flavoproteins in the neurotoxic action of MPTP --
Biosynthesis of flavoproteins --
Biological and Medical Aspects of D-Amino Acid Oxidase — Biogenesis and in vivo reaction with D-propargylglycine — --
Molecular and cellular biology of D-amino acid oxidase --
Localization of D-amino acid oxidase in rat cerebellum --
Biosynthesis of D-amino acid oxidase and molecular cloning of the cDNA --
Characterization of a partially purified nitroaryl reductase --
FLAVOENZYME HYDROXYLASES --
Crystallographic studies on the mechanism of hydroxybenzoate hydroxylase from Psudomonas fluorescens --
Applications of deuterium and tritium isotope effects to the elucidation of kinetic mechanisms of flavoprotein hydroxylases --
Chemical modification of tyrosine-38 in j>.-hydroxybenzoate hydroxylase from Pseudomonas fluorescens by 5'-Pfluorosulfonylbenzoyladenosine: A probe for the elucidation of the NADPH binding site? --
Phenol Complexes of Phenol Hydroxylase --
The involvement of SH-groups in cooperativity of phenol binding sites in phenol hydroxylase --
6-Thiocyanate-FAD and 6-mercapto-FAD as active site probes of phenol hydroxylase --
Hysteretic behavior of anthranilate hydroxylase --
Redox potentials of salicylate hydroxylase --
The oxidative half-reaction of 2-methyl-3-hydroxypyridine-5 - carboxylic acid oxygenase from Pseudomonas sp. MA-1 --
Lipid stabilization of the flavin hydroperoxide in the microsomal flavin-containing monooxygenase --
FLAVIN-DEPENDENT BIOLUMINESCENCE --
One-electron transfers in flavin systems: Relevance to the postulated C1EEL mechanism in bacterial bioluminescence --
Characterization of new "bleached" products obtained on treating flavins and flavoproteins with dithionite --
Flavin-mediated hydrogen peroxide production by biological and chemical photosystems --
On the chemical mechanisms of bacterial luciferase, an updating --
Studies on the mechanism of bacterial bioluminescence. Evidence compatible with a one electron transfer process and a CIEEL mechanism in the luciferase reaction --
Structural analysis of bacterial luciferase --
Sequence similarity between the a subunit of luciferase from Vibrio harvevl and clostridial flavodoxin --
Isolation and characterization of a yellow fluorescent protein from Vibrio fischeri strain Y-1 --
Purification and characterization of an unusual nonfluores cent flavoprotein from Photobacterium leiognathi --
Purification and some properties of FP390 from P. phosphoreum --
STRUCTURE, MECHANISM, AND BIOSYNTHESIS OF FLAVOENZYMES CONTAINING COVALENTLY-BOUND FLAVINS --
8α-Imidazolylflavins: Application of their redox and spectral properties to flavoenzyme systems --
X-ray study of flavoenzymes containing covalently bound flavins --
Structural studies of P-cresol methylhydroxylase --
The chemical and stereochemical course of oxidation of 4- ethylphenol and other 4-alkylphenols by ^-cresol methylhydroxylase --
Redox properties of trimethylamine dehydrogenase --
Redox properties of Escherichia coll fumarate reductase --
Reactions of lumiflavin with aminyl and a-amino radicals of piperazine --
Kinetic probes of the proposed radical mechanism of monoamine oxidase --
Stopped-flow studies on the mechanism of the oxidation of N—methyl - 4 - phenyl - 1 , 2 , 3 , 6 - tetrahydropyridine (HPTP) by monoamine oxidase --
Methoxatin containing methylamine dehydrogenase: Enzyme reduction by primary amines --
Interaction of bacterial sarcosine oxidase with folate derivatives --
Sulfhydryl groups and the binding site of noncovalently bound FAD ofCorvnebacterlum sarcosine oxidase --
Dimethylglycine dehydrogenase from pig liver mitochondria: Purification and properties --
Comparison of partial amino acid sequences deduced from the nucleotide sequence of a bovine adrenal monoamine oxidase cDNA clone to amino acid sequences obtained from bovine liver monoamine oxidase type B --
Covalent binding of FAD to Bacillus subtllis succinate dehydrogenase --
6 - Hydroxy-D-nicotine oxidase: Expression of the flavoenzyme as a covalently flavinylated polypeptide --
The flavin-binding sites of 6-hydroxy-D- and 6-hydroxy-Lnicotine oxidase --
LIST OF PARTICIPANTS --
AUTHOR INDEX --
SUBJECT INDEX --
Backmatter
title_new Flavins and Flavoproteins 1987 :
title_sort flavins and flavoproteins 1987 : proceedings of the ninth international symposium, atlanta, georgia, usa, june 7–12, 1987 /
publisher De Gruyter,
publishDate 2019
physical 1 online resource (XXIII, 775 p.) : Num. figs.
edition Reprint 2019
contents Frontmatter --
Preface --
Organizing committee --
Acknowledgements --
Contents --
STRUCTURE AND MECHANISMS OF FLAVOENZYMES --
Absolute stereochemistry of flavins in enzyme - catalyzed reactions --
Conserved cysteine pairs of mercuric ion reductase: an investigation of function via site-directed mutagenesis --
Reduced forms of native mercuric reductase and their reactions with mercuric compounds - activity vs inhibition --
Rapid-scan stopped-flow studies of the flavoenzyme mercuric reductase during catalytic turnover --
The penultimate cysteines in mercuric reductase aid in the reduction of mercury --
The active center of glutathione reductase at 1.54 A resolution --
Kinetic isotope effect studies on yeast, spinach and human erythrocyte glutathione reductases --
Excited electronic states of flavin-containing coenzyme models --
Trypanothione reductase from Trypanosoma cruzi --
Inactivation of two-electron reduced Escherichia coll glutathione reductase by NADPH and NADH --
Studies on the active site of human erythrocyte glutathione reductase using 6-SCN-FAD and 6-mercapto - FAD --
Protein engineering of glutathione reductase from Escherichia coli --
Studies on the active sites of lipoamide dehydrogenase and glutathione reductase --
Cloning, organisation and nucleotide sequence of the Azotobacter vinelandii gene for lipoamide dehydrogenase --
Reaction of pig heart lipoamide dehydrogenase with monobromoacetone and 1,3-dibromoacetone --
Site-directed mutagenesis of thioredoxin reductase --
Effects of urea on redox properties of streptococcal NADH peroxidase --
Three dimensional structure of baker's yeast flavocytochrome b2 --
Mechanism of L-lactate dehydrogenation catalyzed by flavocytochrome b.2 from baker's yeast --
Inactivation of yeast flavocytochrone b.2 with fluoropyruvate. Modification of the active site histidine --
Evidence for an alteration of the flavin behavior induced by 2-methyl - 2,4 - pentandiol in cerevis iae flavocytochrome b2 --
Medium chain acyl-CoA dehydrogenase from pig kidney: Aspects of the reductive half - reaction --
Crystal structure of the general acyl-CoA dehydrogenase --
Inactivation of general acyl-CoA dehydrogenase from pig k i dney by the suicide substrate methylenecyclopropylacetyl - CoA. Stucture of one of the covalent flavin-inhibitor adducts --
2 - Bromo-octanoyl CoA: Apseudo-substrateforgeneral acyl-CoA dehydrogenase --
Reaction of pig kidney medium chain acyl-CoA dehydrogenase with ^ - oxidation intermediates --
Medium chain acyl-CoA dehydrogenase from pig kidney: I n activation of the reduced enzyme by 2-octynoy1-CoA --
Oxidation - reduction of general acyl-CoA dehydrogenase by the butyryl-CoA / crotonyl-CoA couple. A new investigation of the rapid reaction kinetics --
Catalytic versatility of butyryl-CoA dehydrogenase from M. elsdenii --
Oxidation-reduction potential of glutaryl-CoA dehydrogenase from Paracoccus denitrifleans --
13C NMR studies on the complexes and reaction intermediates of D-amino acid oxidase --
13C-,15N-, and 31P- NMR studies on 6-hydroxy-L-nicotine oxidase from Arthrobacter oxidans --
A study on the interaction between reduced D-amino acid oxidase and ligands --
D-Amino acid oxidase from the yeast Rhodotorula gracilis --
Purification and properties of D-aspartate oxidase from beef kidney --
Spectral and kinetic studies on Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating) --
Time - resolved flavin fluorescence of pyridoxine-5-P oxidase from sheep brain --
An active site thiol in lactate oxidase --
Can methylenetetrahydrofolate reductase be used to evade the methyl trap? --
The catalytic mechanism of DNA photolyase --
FLAVOENZYME STRUCTURE AND ELECTRON TRANSFER MECHANISMS --
Sequence and structure of Anacvstis nidulans flavodoxin: Comparisons with flavodoxins from other species --
C-13, N-15, and two-dimensional NMR techniques in flavoprotein research --
Two dimensional NMR studies on Megasphaera elsdenii --
Flavodoxin from Anabaena 7120: Uniform N-15 enrichment and nitrogen-15 and phosphorus - 31 NMR investigations of the FMN binding site in the reduced and oxidized states --
Pulse radiolysis studies on flavodoxin --
Resonance raman investigations of flavins and flavoproteins --
Spectral studies on hydrogen bonded alloxazines --
Use of flavin and flavodoxin semiquinones as kinetic probes to elucidate the factors which determine reaction rate constants and biological specificity for electron transfer proteins --
Factors influencing the rate of electron transfer from flavodoxin to cytochrome c. --
A computer graphics model of the complex formed between flavodoxin and the tetraheme cytochrome c.3 --
Cloning and nucleotide sequence of a bacterial flavodoxin gene: Towards the site-directed mutagenesis of the flavin binding site --
Flavin binding site differences between Photobacterium phosphoreum lumazine protein and Megasphaera elsdenii flavodoxin. An investigation using circular dichroism and fluorescence --
Ferredoxin and ferredoxin-NADP+oxidoreductase interactions: Mapping of their binding sites --
Complex formation between ferredoxin-NADP+-oxidoreductase and flavodoxin --
Mechanism of ferredoxin-NADP+ reductase reaction NADP radical, semiquinone and fully reduced enzyme-NADP+ charge transfer complex as the reaction intermediates --
In vivo deactivation/activation of ferredoxin-NADP+- oxidoreductase from the cyanobacteria Anabaena variabills --
Isolation from Desulfovibrio desulfuricans of a flavoprotein with NADH-H+ oxidoreductase activity towards a protein containing a rubredoxin-like center --
Microsomal electron transport system focused on NADPH-cytochrome P-450 reductase --
Time - resolved fluorescence spectroscopy on NADPH-cytochrome P-450 reductase --
Studies on the reactions of flavin- and nicotinamide nucleotide analogues with a bacterial electron-transferring flavoprotein --
Kinetics of ligand binding, amino acid sequence, and crystallization of Chlorobium and Chromatium flavocytochrome c. --
Redox properties of flavocytochrome c.
--
Electron transfer kinetics of phthalate oxygenase reductase, an iron sulfur center containing flavoprotein --
CD and potentiometry of the FAD of nitrate reductase --
Kinetic studies on glutamate synthase from Azospirillum bras ilense --
Redox interactions of the FAD in xanthine oxidase with other centers of the protein --
Laser flash photolysis studies of intramolecular electron transfer between the FAD and Fe/S II centers in xanthine oxidase --
Mechanism of action of chicken liver xanthine dehydrogenase --
Interconversion between O-dependent and NAD - dependent types of rat liver xanthine dehydrogenase --
Reactivity of chicken liver xanthine dehydrogenase containing artificial flavins --
The molybdenum cofactor of milk xanthine oxidase --
Isolation of a cDNA sequence coding for a part of xanthine dehydrogenase from rat liver --
FLAVIN BIOSYNTHESIS/ METABOLISM/ AND MEDICAL ASPECTS --
Biosynthesis of flavins and deazaflavins --
The icosahedral ß60 capsid of heavy riboflavin synthase (6,7- dimethyl-8-ribityllumazine synthase/riboflavin synthase) --
Characterization of human riboflavin-binding immunoglobulins --
Riboflavin uptake by isolated rat kidney cells --
Purification and characterization of the bifunctional enzyme FAD synthetase from Brevibacterium ammoniapenes --
An update on flavin metabolism in rats and humans --
Effects of quinacrine, tetracycline, adriamycin and chloroquine upon flavin metabolism in rats --
Role of flavoproteins in the neurotoxic action of MPTP --
Biosynthesis of flavoproteins --
Biological and Medical Aspects of D-Amino Acid Oxidase — Biogenesis and in vivo reaction with D-propargylglycine — --
Molecular and cellular biology of D-amino acid oxidase --
Localization of D-amino acid oxidase in rat cerebellum --
Biosynthesis of D-amino acid oxidase and molecular cloning of the cDNA --
Characterization of a partially purified nitroaryl reductase --
FLAVOENZYME HYDROXYLASES --
Crystallographic studies on the mechanism of hydroxybenzoate hydroxylase from Psudomonas fluorescens --
Applications of deuterium and tritium isotope effects to the elucidation of kinetic mechanisms of flavoprotein hydroxylases --
Chemical modification of tyrosine-38 in j>.-hydroxybenzoate hydroxylase from Pseudomonas fluorescens by 5'-Pfluorosulfonylbenzoyladenosine: A probe for the elucidation of the NADPH binding site? --
Phenol Complexes of Phenol Hydroxylase --
The involvement of SH-groups in cooperativity of phenol binding sites in phenol hydroxylase --
6-Thiocyanate-FAD and 6-mercapto-FAD as active site probes of phenol hydroxylase --
Hysteretic behavior of anthranilate hydroxylase --
Redox potentials of salicylate hydroxylase --
The oxidative half-reaction of 2-methyl-3-hydroxypyridine-5 - carboxylic acid oxygenase from Pseudomonas sp. MA-1 --
Lipid stabilization of the flavin hydroperoxide in the microsomal flavin-containing monooxygenase --
FLAVIN-DEPENDENT BIOLUMINESCENCE --
One-electron transfers in flavin systems: Relevance to the postulated C1EEL mechanism in bacterial bioluminescence --
Characterization of new "bleached" products obtained on treating flavins and flavoproteins with dithionite --
Flavin-mediated hydrogen peroxide production by biological and chemical photosystems --
On the chemical mechanisms of bacterial luciferase, an updating --
Studies on the mechanism of bacterial bioluminescence. Evidence compatible with a one electron transfer process and a CIEEL mechanism in the luciferase reaction --
Structural analysis of bacterial luciferase --
Sequence similarity between the a subunit of luciferase from Vibrio harvevl and clostridial flavodoxin --
Isolation and characterization of a yellow fluorescent protein from Vibrio fischeri strain Y-1 --
Purification and characterization of an unusual nonfluores cent flavoprotein from Photobacterium leiognathi --
Purification and some properties of FP390 from P. phosphoreum --
STRUCTURE, MECHANISM, AND BIOSYNTHESIS OF FLAVOENZYMES CONTAINING COVALENTLY-BOUND FLAVINS --
8α-Imidazolylflavins: Application of their redox and spectral properties to flavoenzyme systems --
X-ray study of flavoenzymes containing covalently bound flavins --
Structural studies of P-cresol methylhydroxylase --
The chemical and stereochemical course of oxidation of 4- ethylphenol and other 4-alkylphenols by ^-cresol methylhydroxylase --
Redox properties of trimethylamine dehydrogenase --
Redox properties of Escherichia coll fumarate reductase --
Reactions of lumiflavin with aminyl and a-amino radicals of piperazine --
Kinetic probes of the proposed radical mechanism of monoamine oxidase --
Stopped-flow studies on the mechanism of the oxidation of N—methyl - 4 - phenyl - 1 , 2 , 3 , 6 - tetrahydropyridine (HPTP) by monoamine oxidase --
Methoxatin containing methylamine dehydrogenase: Enzyme reduction by primary amines --
Interaction of bacterial sarcosine oxidase with folate derivatives --
Sulfhydryl groups and the binding site of noncovalently bound FAD ofCorvnebacterlum sarcosine oxidase --
Dimethylglycine dehydrogenase from pig liver mitochondria: Purification and properties --
Comparison of partial amino acid sequences deduced from the nucleotide sequence of a bovine adrenal monoamine oxidase cDNA clone to amino acid sequences obtained from bovine liver monoamine oxidase type B --
Covalent binding of FAD to Bacillus subtllis succinate dehydrogenase --
6 - Hydroxy-D-nicotine oxidase: Expression of the flavoenzyme as a covalently flavinylated polypeptide --
The flavin-binding sites of 6-hydroxy-D- and 6-hydroxy-Lnicotine oxidase --
LIST OF PARTICIPANTS --
AUTHOR INDEX --
SUBJECT INDEX --
Backmatter
isbn 9783110884715
9783110637243
9783110109504
url https://doi.org/10.1515/9783110884715
https://www.degruyter.com/isbn/9783110884715
https://www.degruyter.com/cover/covers/9783110884715.jpg
illustrated Not Illustrated
doi_str_mv 10.1515/9783110884715
oclc_num 1105851472
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AT delucamarlene flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT deckerkarl flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT devinejh flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT distefanom flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT distefanomarkd flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT drakedonnam flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT drenthjan flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT duttap flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ecksteinjens flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT edmondsonde flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT edmondsondalee flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT einarsdottirgh flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT eisenreichwolfgang flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ellisonpatriciaa flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT engelpaulc flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT engelkedavidr flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ermlerulrich flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT fauqueg flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT fillatmf flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT fillatm flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT fishkennethm flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT florencelederer flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT flossheinzg flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT fukuikiyoshi flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT gallianon flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ghislasandra flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ghislasandro flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ghislatsandro flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT giegeldavida flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT gomezmorenoc flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT grandorir flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT greenjacalynm flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT gustafsonwilliamg flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT guckelf flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT hallcarolel flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT halldo flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT hazzardjamest flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT hederstedtl flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT heelispf flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT hilleruss flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT hinkkanenarie flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT hoekarievan flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT hoiwimgj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT holwingj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT holdenhm flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT horiikekihachiro flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT hsuyunpungp flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT huberarobert flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT husainmazhar flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ichiharachikako flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT inagakitaisuke flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT inniswsa flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT inniswhitehousewsa flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ishiiyasuhiko flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT jekelpetera flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT johnstontc flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT jornsmarilynschuman flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT kaiczykgb flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT kalkkorh flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT karpluspa flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT kasaisabu flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT kawamurakonishiy flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT kawamurakonishiyasuko flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT kaycj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT kearneyednab flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT kellerpaulj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT kimjjp flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT klappermichaelh flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT kodokeiun flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT koerberstevenc flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT kokariede flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT koshizakatakuya flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT koyamah flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT koziołj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT krauthsiegelrl flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT kreygrigoriosd flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT kvalneskrickkalla flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT kwokfrancis flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT konigastrid flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT laanjanmvander flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT labeyrief flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ladensteinarudolf flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT lausm flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT laudenbachdavide flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT levanaquang flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT legallj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ledererf flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT leej flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT leejamess flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT leejohn flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT leismangary flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT limlw flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT linjw flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT lindskogs flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT livelychrisr flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ludwigmarthal flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT macherouxpeter flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT maedatoshihiro flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT magerhumphreyix flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mansteindj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mansteindietmarj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT markleyjohnl flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT martintracy flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT masseyv flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT masseyvincent flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mathewsfs flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT matsuarahiroshi flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT matsuikunio flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT matthewsrowenag flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mauchludwig flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mayhewstepheng flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mayhewsteveg flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mccormickdb flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mccormickdonaldb flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mcfarlandjamest flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mcwhirterrobertb flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mclntirews flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mclntirewilliams flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT merrillah flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT meyerte flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT meyerterrancee flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mierlocarlopmvan flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mierlocarlovan flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT miillerfranz flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT millersm flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT miurar flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT miyakey flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT miyakeyoshihiro flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT momoikyoko flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT moorem flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mooremelissaj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mourai flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mourajjg flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mullerf flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT muratam flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT mullerfranz flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT nagatat flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT nagurskyheiner flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT nakamuramakoto flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT nakamuratakao flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT negriarmando flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT neujahrhaiinay flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT neujahrhalinay flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT nishikimimorimitsu flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT nishinayasuzo flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT nishinot flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT nishinotakeshi flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT nishinotomoko flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT nishiyamakyoko flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT nisimotoy flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT nittasatoshi flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT nozakimitsuhiro flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ohishinobuko flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ohnishinorihiro flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT okam flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ozawatakayuki flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT okanedj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT okanedennisj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT onuallaineoinm flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT paief flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT paiemilf flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT pattridgekatherinea flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT peckhd flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT perhamrn flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT pintojt flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT pollegionil flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT pooleleslieb flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT poulsenll flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT powelljohn flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT powellpj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT powlowskijustin flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT prongayandrewj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT pueyojj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT puststefan flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ramsayronar flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT raokk flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT rattis flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT raymenti flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT rivlinrs flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ronchis flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT sahlmanlena flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT saintmartinp flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT saitot flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT sanchoj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT sandstroma flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT schirmerrh flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT schneidermonika flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT schopferlawrencem flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT schottkarin flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT schreuderhermana flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT schulzge flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT schulzgeorge flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT schwarzkopfbruno flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT schweitzerd flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT schollhammert flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT scruttonns flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT sejlitztorsten flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT shibatatoshihiro flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT shigakiyoshi flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT simonettampilone flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT singertp flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT singerthomasp flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT solomonsonlp flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT staabha flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT stankovichmt flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT stankovichmariant flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT steenkampdj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT stewartde flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT stockmanbrianj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT strausneila flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT sugiharaj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT surdharps flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT suzukih flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT suzukiharuo flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT swartemyraba flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT swensonrichardp flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT szafranmm flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT takeshimakatsuhito flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT taylorkl flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT taylormg flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT tegonim flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT thorpec flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT thorpecolin flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT thunnissenmarjoleinmgm flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT titlowchristian flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT tojohiroaasa flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT tojohiromasa flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT tollingordon flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT tsukagoshinorihiro flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT tsushimak flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT tsushimakeizo flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT tusc flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT tushiaochun flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT udakashigezo flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT urbanphilippe flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT ushijiaahidetaka flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT utterbackmargot flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT vanbeeumenj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT vanineliof flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT vanonima flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT vervoortj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT vervoortjacques flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
AT visserantoniejwg flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987
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hierarchy_parent_title Title is part of eBook package: De Gruyter DGBA Physical Sciences <1990
is_hierarchy_title Flavins and Flavoproteins 1987 : Proceedings of the Ninth International Symposium, Atlanta, Georgia, USA, June 7–12, 1987 /
container_title Title is part of eBook package: De Gruyter DGBA Physical Sciences <1990
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E. Edmondson, D. B. McCormick.</subfield></datafield><datafield tag="250" ind1=" " ind2=" "><subfield code="a">Reprint 2019</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Berlin ;</subfield><subfield code="a">Boston : </subfield><subfield code="b">De Gruyter, </subfield><subfield code="c">[2019]</subfield></datafield><datafield tag="264" ind1=" " ind2="4"><subfield code="c">©1987</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">1 online resource (XXIII, 775 p.) :</subfield><subfield code="b">Num. figs.</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">computer</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">online resource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="347" ind1=" " ind2=" "><subfield code="a">text file</subfield><subfield code="b">PDF</subfield><subfield code="2">rda</subfield></datafield><datafield tag="505" ind1="0" ind2="0"><subfield code="t">Frontmatter -- </subfield><subfield code="t">Preface -- </subfield><subfield code="t">Organizing committee -- </subfield><subfield code="t">Acknowledgements -- </subfield><subfield code="t">Contents -- </subfield><subfield code="t">STRUCTURE AND MECHANISMS OF FLAVOENZYMES -- </subfield><subfield code="t">Absolute stereochemistry of flavins in enzyme - catalyzed reactions -- </subfield><subfield code="t">Conserved cysteine pairs of mercuric ion reductase: an investigation of function via site-directed mutagenesis -- </subfield><subfield code="t">Reduced forms of native mercuric reductase and their reactions with mercuric compounds - activity vs inhibition -- </subfield><subfield code="t">Rapid-scan stopped-flow studies of the flavoenzyme mercuric reductase during catalytic turnover -- </subfield><subfield code="t">The penultimate cysteines in mercuric reductase aid in the reduction of mercury -- </subfield><subfield code="t">The active center of glutathione reductase at 1.54 A resolution -- </subfield><subfield code="t">Kinetic isotope effect studies on yeast, spinach and human erythrocyte glutathione reductases -- </subfield><subfield code="t">Excited electronic states of flavin-containing coenzyme models -- </subfield><subfield code="t">Trypanothione reductase from Trypanosoma cruzi -- </subfield><subfield code="t">Inactivation of two-electron reduced Escherichia coll glutathione reductase by NADPH and NADH -- </subfield><subfield code="t">Studies on the active site of human erythrocyte glutathione reductase using 6-SCN-FAD and 6-mercapto - FAD -- </subfield><subfield code="t">Protein engineering of glutathione reductase from Escherichia coli -- </subfield><subfield code="t">Studies on the active sites of lipoamide dehydrogenase and glutathione reductase -- </subfield><subfield code="t">Cloning, organisation and nucleotide sequence of the Azotobacter vinelandii gene for lipoamide dehydrogenase -- </subfield><subfield code="t">Reaction of pig heart lipoamide dehydrogenase with monobromoacetone and 1,3-dibromoacetone -- </subfield><subfield code="t">Site-directed mutagenesis of thioredoxin reductase -- </subfield><subfield code="t">Effects of urea on redox properties of streptococcal NADH peroxidase -- </subfield><subfield code="t">Three dimensional structure of baker's yeast flavocytochrome b2 -- </subfield><subfield code="t">Mechanism of L-lactate dehydrogenation catalyzed by flavocytochrome b.2 from baker's yeast -- </subfield><subfield code="t">Inactivation of yeast flavocytochrone b.2 with fluoropyruvate. Modification of the active site histidine -- </subfield><subfield code="t">Evidence for an alteration of the flavin behavior induced by 2-methyl - 2,4 - pentandiol in cerevis iae flavocytochrome b2 -- </subfield><subfield code="t">Medium chain acyl-CoA dehydrogenase from pig kidney: Aspects of the reductive half - reaction -- </subfield><subfield code="t">Crystal structure of the general acyl-CoA dehydrogenase -- </subfield><subfield code="t">Inactivation of general acyl-CoA dehydrogenase from pig k i dney by the suicide substrate methylenecyclopropylacetyl - CoA. Stucture of one of the covalent flavin-inhibitor adducts -- </subfield><subfield code="t">2 - Bromo-octanoyl CoA: Apseudo-substrateforgeneral acyl-CoA dehydrogenase -- </subfield><subfield code="t">Reaction of pig kidney medium chain acyl-CoA dehydrogenase with ^ - oxidation intermediates -- </subfield><subfield code="t">Medium chain acyl-CoA dehydrogenase from pig kidney: I n activation of the reduced enzyme by 2-octynoy1-CoA -- </subfield><subfield code="t">Oxidation - reduction of general acyl-CoA dehydrogenase by the butyryl-CoA / crotonyl-CoA couple. A new investigation of the rapid reaction kinetics -- </subfield><subfield code="t">Catalytic versatility of butyryl-CoA dehydrogenase from M. elsdenii -- </subfield><subfield code="t">Oxidation-reduction potential of glutaryl-CoA dehydrogenase from Paracoccus denitrifleans -- </subfield><subfield code="t">13C NMR studies on the complexes and reaction intermediates of D-amino acid oxidase -- </subfield><subfield code="t">13C-,15N-, and 31P- NMR studies on 6-hydroxy-L-nicotine oxidase from Arthrobacter oxidans -- </subfield><subfield code="t">A study on the interaction between reduced D-amino acid oxidase and ligands -- </subfield><subfield code="t">D-Amino acid oxidase from the yeast Rhodotorula gracilis -- </subfield><subfield code="t">Purification and properties of D-aspartate oxidase from beef kidney -- </subfield><subfield code="t">Spectral and kinetic studies on Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating) -- </subfield><subfield code="t">Time - resolved flavin fluorescence of pyridoxine-5-P oxidase from sheep brain -- </subfield><subfield code="t">An active site thiol in lactate oxidase -- </subfield><subfield code="t">Can methylenetetrahydrofolate reductase be used to evade the methyl trap? -- </subfield><subfield code="t">The catalytic mechanism of DNA photolyase -- </subfield><subfield code="t">FLAVOENZYME STRUCTURE AND ELECTRON TRANSFER MECHANISMS -- </subfield><subfield code="t">Sequence and structure of Anacvstis nidulans flavodoxin: Comparisons with flavodoxins from other species -- </subfield><subfield code="t">C-13, N-15, and two-dimensional NMR techniques in flavoprotein research -- </subfield><subfield code="t">Two dimensional NMR studies on Megasphaera elsdenii -- </subfield><subfield code="t">Flavodoxin from Anabaena 7120: Uniform N-15 enrichment and nitrogen-15 and phosphorus - 31 NMR investigations of the FMN binding site in the reduced and oxidized states -- </subfield><subfield code="t">Pulse radiolysis studies on flavodoxin -- </subfield><subfield code="t">Resonance raman investigations of flavins and flavoproteins -- </subfield><subfield code="t">Spectral studies on hydrogen bonded alloxazines -- </subfield><subfield code="t">Use of flavin and flavodoxin semiquinones as kinetic probes to elucidate the factors which determine reaction rate constants and biological specificity for electron transfer proteins -- </subfield><subfield code="t">Factors influencing the rate of electron transfer from flavodoxin to cytochrome c. -- </subfield><subfield code="t">A computer graphics model of the complex formed between flavodoxin and the tetraheme cytochrome c.3 -- </subfield><subfield code="t">Cloning and nucleotide sequence of a bacterial flavodoxin gene: Towards the site-directed mutagenesis of the flavin binding site -- </subfield><subfield code="t">Flavin binding site differences between Photobacterium phosphoreum lumazine protein and Megasphaera elsdenii flavodoxin. An investigation using circular dichroism and fluorescence -- </subfield><subfield code="t">Ferredoxin and ferredoxin-NADP+oxidoreductase interactions: Mapping of their binding sites -- </subfield><subfield code="t">Complex formation between ferredoxin-NADP+-oxidoreductase and flavodoxin -- </subfield><subfield code="t">Mechanism of ferredoxin-NADP+ reductase reaction NADP radical, semiquinone and fully reduced enzyme-NADP+ charge transfer complex as the reaction intermediates -- </subfield><subfield code="t">In vivo deactivation/activation of ferredoxin-NADP+- oxidoreductase from the cyanobacteria Anabaena variabills -- </subfield><subfield code="t">Isolation from Desulfovibrio desulfuricans of a flavoprotein with NADH-H+ oxidoreductase activity towards a protein containing a rubredoxin-like center -- </subfield><subfield code="t">Microsomal electron transport system focused on NADPH-cytochrome P-450 reductase -- </subfield><subfield code="t">Time - resolved fluorescence spectroscopy on NADPH-cytochrome P-450 reductase -- </subfield><subfield code="t">Studies on the reactions of flavin- and nicotinamide nucleotide analogues with a bacterial electron-transferring flavoprotein -- </subfield><subfield code="t">Kinetics of ligand binding, amino acid sequence, and crystallization of Chlorobium and Chromatium flavocytochrome c. -- </subfield><subfield code="t">Redox properties of flavocytochrome c. </subfield></datafield><datafield tag="505" ind1="0" ind2="0"><subfield code="t">-- </subfield><subfield code="t">Electron transfer kinetics of phthalate oxygenase reductase, an iron sulfur center containing flavoprotein -- </subfield><subfield code="t">CD and potentiometry of the FAD of nitrate reductase -- </subfield><subfield code="t">Kinetic studies on glutamate synthase from Azospirillum bras ilense -- </subfield><subfield code="t">Redox interactions of the FAD in xanthine oxidase with other centers of the protein -- </subfield><subfield code="t">Laser flash photolysis studies of intramolecular electron transfer between the FAD and Fe/S II centers in xanthine oxidase -- </subfield><subfield code="t">Mechanism of action of chicken liver xanthine dehydrogenase -- </subfield><subfield code="t">Interconversion between O-dependent and NAD - dependent types of rat liver xanthine dehydrogenase -- </subfield><subfield code="t">Reactivity of chicken liver xanthine dehydrogenase containing artificial flavins -- </subfield><subfield code="t">The molybdenum cofactor of milk xanthine oxidase -- </subfield><subfield code="t">Isolation of a cDNA sequence coding for a part of xanthine dehydrogenase from rat liver -- </subfield><subfield code="t">FLAVIN BIOSYNTHESIS/ METABOLISM/ AND MEDICAL ASPECTS -- </subfield><subfield code="t">Biosynthesis of flavins and deazaflavins -- </subfield><subfield code="t">The icosahedral ß60 capsid of heavy riboflavin synthase (6,7- dimethyl-8-ribityllumazine synthase/riboflavin synthase) -- </subfield><subfield code="t">Characterization of human riboflavin-binding immunoglobulins -- </subfield><subfield code="t">Riboflavin uptake by isolated rat kidney cells -- </subfield><subfield code="t">Purification and characterization of the bifunctional enzyme FAD synthetase from Brevibacterium ammoniapenes -- </subfield><subfield code="t">An update on flavin metabolism in rats and humans -- </subfield><subfield code="t">Effects of quinacrine, tetracycline, adriamycin and chloroquine upon flavin metabolism in rats -- </subfield><subfield code="t">Role of flavoproteins in the neurotoxic action of MPTP -- </subfield><subfield code="t">Biosynthesis of flavoproteins -- </subfield><subfield code="t">Biological and Medical Aspects of D-Amino Acid Oxidase — Biogenesis and in vivo reaction with D-propargylglycine — -- </subfield><subfield code="t">Molecular and cellular biology of D-amino acid oxidase -- </subfield><subfield code="t">Localization of D-amino acid oxidase in rat cerebellum -- </subfield><subfield code="t">Biosynthesis of D-amino acid oxidase and molecular cloning of the cDNA -- </subfield><subfield code="t">Characterization of a partially purified nitroaryl reductase -- </subfield><subfield code="t">FLAVOENZYME HYDROXYLASES -- </subfield><subfield code="t">Crystallographic studies on the mechanism of hydroxybenzoate hydroxylase from Psudomonas fluorescens -- </subfield><subfield code="t">Applications of deuterium and tritium isotope effects to the elucidation of kinetic mechanisms of flavoprotein hydroxylases -- </subfield><subfield code="t">Chemical modification of tyrosine-38 in j&gt;.-hydroxybenzoate hydroxylase from Pseudomonas fluorescens by 5'-Pfluorosulfonylbenzoyladenosine: A probe for the elucidation of the NADPH binding site? -- </subfield><subfield code="t">Phenol Complexes of Phenol Hydroxylase -- </subfield><subfield code="t">The involvement of SH-groups in cooperativity of phenol binding sites in phenol hydroxylase -- </subfield><subfield code="t">6-Thiocyanate-FAD and 6-mercapto-FAD as active site probes of phenol hydroxylase -- </subfield><subfield code="t">Hysteretic behavior of anthranilate hydroxylase -- </subfield><subfield code="t">Redox potentials of salicylate hydroxylase -- </subfield><subfield code="t">The oxidative half-reaction of 2-methyl-3-hydroxypyridine-5 - carboxylic acid oxygenase from Pseudomonas sp. MA-1 -- </subfield><subfield code="t">Lipid stabilization of the flavin hydroperoxide in the microsomal flavin-containing monooxygenase -- </subfield><subfield code="t">FLAVIN-DEPENDENT BIOLUMINESCENCE -- </subfield><subfield code="t">One-electron transfers in flavin systems: Relevance to the postulated C1EEL mechanism in bacterial bioluminescence -- </subfield><subfield code="t">Characterization of new "bleached" products obtained on treating flavins and flavoproteins with dithionite -- </subfield><subfield code="t">Flavin-mediated hydrogen peroxide production by biological and chemical photosystems -- </subfield><subfield code="t">On the chemical mechanisms of bacterial luciferase, an updating -- </subfield><subfield code="t">Studies on the mechanism of bacterial bioluminescence. Evidence compatible with a one electron transfer process and a CIEEL mechanism in the luciferase reaction -- </subfield><subfield code="t">Structural analysis of bacterial luciferase -- </subfield><subfield code="t">Sequence similarity between the a subunit of luciferase from Vibrio harvevl and clostridial flavodoxin -- </subfield><subfield code="t">Isolation and characterization of a yellow fluorescent protein from Vibrio fischeri strain Y-1 -- </subfield><subfield code="t">Purification and characterization of an unusual nonfluores cent flavoprotein from Photobacterium leiognathi -- </subfield><subfield code="t">Purification and some properties of FP390 from P. phosphoreum -- </subfield><subfield code="t">STRUCTURE, MECHANISM, AND BIOSYNTHESIS OF FLAVOENZYMES CONTAINING COVALENTLY-BOUND FLAVINS -- </subfield><subfield code="t">8α-Imidazolylflavins: Application of their redox and spectral properties to flavoenzyme systems -- </subfield><subfield code="t">X-ray study of flavoenzymes containing covalently bound flavins -- </subfield><subfield code="t">Structural studies of P-cresol methylhydroxylase -- </subfield><subfield code="t">The chemical and stereochemical course of oxidation of 4- ethylphenol and other 4-alkylphenols by ^-cresol methylhydroxylase -- </subfield><subfield code="t">Redox properties of trimethylamine dehydrogenase -- </subfield><subfield code="t">Redox properties of Escherichia coll fumarate reductase -- </subfield><subfield code="t">Reactions of lumiflavin with aminyl and a-amino radicals of piperazine -- </subfield><subfield code="t">Kinetic probes of the proposed radical mechanism of monoamine oxidase -- </subfield><subfield code="t">Stopped-flow studies on the mechanism of the oxidation of N—methyl - 4 - phenyl - 1 , 2 , 3 , 6 - tetrahydropyridine (HPTP) by monoamine oxidase -- </subfield><subfield code="t">Methoxatin containing methylamine dehydrogenase: Enzyme reduction by primary amines -- </subfield><subfield code="t">Interaction of bacterial sarcosine oxidase with folate derivatives -- </subfield><subfield code="t">Sulfhydryl groups and the binding site of noncovalently bound FAD ofCorvnebacterlum sarcosine oxidase -- </subfield><subfield code="t">Dimethylglycine dehydrogenase from pig liver mitochondria: Purification and properties -- </subfield><subfield code="t">Comparison of partial amino acid sequences deduced from the nucleotide sequence of a bovine adrenal monoamine oxidase cDNA clone to amino acid sequences obtained from bovine liver monoamine oxidase type B -- </subfield><subfield code="t">Covalent binding of FAD to Bacillus subtllis succinate dehydrogenase -- </subfield><subfield code="t">6 - Hydroxy-D-nicotine oxidase: Expression of the flavoenzyme as a covalently flavinylated polypeptide -- </subfield><subfield code="t">The flavin-binding sites of 6-hydroxy-D- and 6-hydroxy-Lnicotine oxidase -- </subfield><subfield code="t">LIST OF PARTICIPANTS -- </subfield><subfield code="t">AUTHOR INDEX -- </subfield><subfield code="t">SUBJECT INDEX -- </subfield><subfield code="t">Backmatter</subfield></datafield><datafield tag="506" ind1="0" ind2=" "><subfield code="a">restricted access</subfield><subfield code="u">http://purl.org/coar/access_right/c_16ec</subfield><subfield code="f">online access with authorization</subfield><subfield code="2">star</subfield></datafield><datafield tag="538" ind1=" " ind2=" "><subfield code="a">Mode of access: Internet via World Wide Web.</subfield></datafield><datafield tag="546" ind1=" " ind2=" "><subfield code="a">In English.</subfield></datafield><datafield tag="588" ind1="0" ind2=" "><subfield code="a">Description based on online resource; title from PDF title page (publisher's Web site, viewed 30. Aug 2021)</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Flavine.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Flavoenzym.</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">SCIENCE / General.</subfield><subfield code="2">bisacsh</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ackrell, Brian A. C., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Aliverti, A., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Anderson, Robert F., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Aral, Ryohachi, </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Armstrong, D. A., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Arscott, L. David, </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Astorga, Adrienne M., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bacher, Adelbert, </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bakx, Edwin J., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Baldwin, T. O., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Baldwin, Thomas O., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ballou, D. P., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ballou, David P., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ballou, David, </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Barber, M. J., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bartsch, R. G., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bastiaens, Phil, </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Batie, Christopher J., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Becker, K., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Beintema, Jaap J., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bellamy, H. D., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Berkel, Willem J. H. van, </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Berkel, Willem J.H. van, </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Berry, A., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Blanchard, J. S., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bohmont, Craig, </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bonants, Peter, </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bowers-Komro, D. M., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bowers-Komro, Delores M., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Brandsch, Roderich, </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Breakefield, Xandra O., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Brissette, Pierre, </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Brown, Kathleen, </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bryant, Christopher, </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Byron, Colleen M., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Casalin, P., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Cecchini, Gary, </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Chastain, J. L., </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Cheddar, Glen, </subfield><subfield code="e">contributor.</subfield><subfield code="4">ctb</subfield><subfield code="4">https://id.loc.gov/vocabulary/relators/ctb</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Chen, L. 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