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 |
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Place / Publishing House: | Berlin ;, Boston : : De Gruyter, , [2019] ©1987 |
Year of Publication: | 2019 |
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Language: | English |
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Physical Description: | 1 online resource (XXIII, 775 p.) :; Num. figs. |
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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. In English. 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 Ellison, Patricia A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Engel, Paul C., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Engelke, David R., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ermler, Ulrich, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Fauque, G., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Fillat, M. F., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Fillat, M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Fish, Kenneth M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Florence, Lederer, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Floss, Heinz G., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Fukui, Kiyoshi, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Galliano, N., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ghisla, Sandra, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ghisla, Sandro, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ghislat, Sandro, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Giegel, David A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Gomez-Moreno, C., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Grandori, R., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Green, Jacalyn M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Gustafson, William G., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Gómez-Moreno, C., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Gückel, F., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hall, Carole L., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hall, D. O., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hazzard, James T., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hederstedt, L., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Heelis, P. F., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hille, Russ, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hinkkanen, Ari E., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hoek, Arie van, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hoi, Wim G. J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hol, Win G. J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Holden, H. M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Horiike, Kihachiro, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hsu, Yun-Pung P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hubera, Robert, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Husain, Mazhar, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ichihara, Chikako, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Inagaki, Taisuke, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Innis, W. S. A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Innis-Whitehouse, W. S. A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ishii, Yasuhiko, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Jekel, Peter A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Johnston, T. C., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Jorns, Marilyn Schuman, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Jörns, Marilyn Schuman, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kaiczyk, G. B., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kalk, Kor H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Karplus, P. A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kasai, Sabu, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kawamura-Konishi, Y., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kawamura-Konishi, Yasuko, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kay, C. J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kearney, Edna B., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Keller, Paul J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kim, J. J. P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Klapper, Michael H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kodo, Keiun, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Koerber, Steven C., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kok, Arie de, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Koshizaka, Takuya, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Koyama, H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kozioł, J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Krauth-Siegel, R. L., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Krey, Grigorios D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kvalnes-Krick, Kalla, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kwok, Francis, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb König, Astrid, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Laan, Jan M. van der, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Labeyrie, F., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ladensteina, Rudolf, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lau, S-M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Laudenbach, David E., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Le Vana, Quang, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb LeGall, J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lederer, F., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lee, J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lee, James S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lee, John, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Leisman, Gary, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lim, L. W., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lin, J.-W., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lindskog, S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lively, Chris R., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ludwig, Martha L., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Macheroux, Peter, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Maeda, Toshihiro, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Mager, Humphrey I. X., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Manstein, D. J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Manstein, Dietmar J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Markley, John L., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Martin, Tracy, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Massey, V., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Massey, Vincent, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Mathews, F. S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Matsuara, Hiroshi, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Matsui, Kunio, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Matthews, Rowena G., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Mauch, Ludwig, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Mayhew, Stephen G., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Mayhew, Steve G., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb McCormick, D. B., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb McCormick, D. B., editor. edt http://id.loc.gov/vocabulary/relators/edt McCormick, Donald B., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb McFarland, James T., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb McWhirter, Robert B., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Mclntire, W. S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Mclntire, William S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Merrill, A. H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Meyer, T. E., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Meyer, Terrance E., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Mierlo, Carlo P.M. van, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Mierlo, Carlo van, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Miiller, Franz, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Miller, S. M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Miura, R., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Miyake, Y., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Miyake, Yoshihiro, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Momoi, Kyoko, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Moore, M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Moore, Melissa J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Moura, I., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Moura, J. J. G., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Muller, F., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Murata, M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Müller, Franz, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nagata, T., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nagursky, Heiner, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nakamura, Makoto, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nakamura, Takao, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Negri, Armando, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Neujahr, Haiina Y., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Neujahr, Halina Y., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nishikimi, Morimitsu, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nishina, Yasuzo, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nishino, T., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nishino, Takeshi, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nishino, Tomoko, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nishiyama, Kyoko, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nisimoto, Y., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nitta, Satoshi, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nozaki, Mitsuhiro, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ohishi, Nobuko, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ohnishi, Norihiro, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Oka, M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ozawa, Takayuki, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb O’Kane, D. J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb O’Kane, Dennis J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb O’Nuallain, Eoin M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Pai, E. F., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Pai, Emil F., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Pattridge, Katherine A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Peck, H. D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Perham, R. N., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Pinto, J. T., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Pollegioni, L., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Poole, Leslie B., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Poulsen, L. L., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Powell, John, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Powell, P. J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Powlowski, Justin, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Prongay, Andrew J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Pueyo, J. J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Pust, Stefan, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ramsay, Rona R., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Rao, K. K., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ratti, S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Rayment, I., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Rivlin, R. 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F., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb 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 |
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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. 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W., Lin, J.-W., Lin, J.-W., Lindskog, S., Lindskog, S., Lively, Chris R., Lively, Chris R., Ludwig, Martha L., Ludwig, Martha L., Macheroux, Peter, Macheroux, Peter, Maeda, Toshihiro, 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., Markley, John L., Martin, Tracy, Martin, Tracy, Massey, V., Massey, V., Massey, Vincent, Massey, Vincent, Mathews, F. S., Mathews, F. S., Matsuara, Hiroshi, Matsuara, Hiroshi, Matsui, Kunio, Matsui, Kunio, Matthews, Rowena G., Matthews, Rowena G., Mauch, Ludwig, Mauch, Ludwig, Mayhew, Stephen G., Mayhew, Stephen G., Mayhew, Steve G., Mayhew, Steve G., McCormick, D. B., McCormick, D. B., McCormick, D. B., McCormick, D. B., McCormick, Donald B., McCormick, Donald B., McFarland, James T., McFarland, James T., McWhirter, Robert B., McWhirter, Robert B., Mclntire, W. S., Mclntire, W. S., Mclntire, William S., Mclntire, William S., Merrill, A. 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jmvdl j m v d l jmvd jmvdl f l fl f l fl r l rl r l rl s m l sml s m l sml d e l de del d e l de del v q l vq vql v q l vq vql j l jl j l jl f l fl f l fl j l jl j l jl j s l js jsl j s l js jsl j l jl j l jl g l gl g l gl l w l lw lwl l w l lw lwl j w l jwl j w l jwl s l sl s l sl c r l cr crl c r l cr crl m l l ml mll m l l ml mll p m pm p m pm t m tm t m tm h i x m hix hixm h i x m hix hixm d j m dj djm d j m dj djm d j m dj djm d j m dj djm j l m jl jlm j l m jl jlm t m tm t m tm v m vm v m vm v m vm v m vm f s m fs fsm f s m fs fsm h m hm h m hm k m km k m km r g m rg rgm r g m rg rgm l m lm l m lm s g m sg sgm s g m sg sgm s g m sg sgm s g m sg sgm d b m db dbm d b m db dbm d b m db dbm d b m db dbm d b m db dbm d b m db dbm j t m jt jtm j t m jt jtm r b m rb rbm r b m rb rbm w s m ws wsm w s m ws wsm w s m ws wsm w s m ws wsm a h m ah ahm a h m ah ahm t e m te tem t e m te tem t e m te tem t e m te tem c p v m cpv cpvm c p v m cpv cpvm c v m cv cvm c v m cv cvm f m fm f m fm s m m sm smm s m m sm smm r m rm r m rm y m ym y m ym y m ym y m ym k m km k m km m m mm m m mm m j m mj mjm m j m mj mjm i m im i m im j j g m jjg jjgm j j g m jjg jjgm f m fm f m fm m m mm m m mm f m fm f m fm t n tn t n tn h n hn h n hn m n mn m n mn t n tn t n tn a n an a n an h y n hy hyn h y n hy hyn h y n hy hyn h y n hy hyn m n mn m n mn y n yn y n yn t n tn t n tn t n tn t n tn t n tn t n tn k n kn k n kn y n yn y n yn s n sn s n sn m n mn m n mn n o no n o no n o no n o no m o mo m o mo t o to t o to d j o dj djo d j o dj djo d j o dj djo d j o dj djo e m o em emo e m o em emo e f p ef efp e f p ef efp e f p ef efp e f p ef efp k a p ka kap k a p ka kap h d p hd hdp h d p hd hdp r n p rn rnp r n p rn rnp j t p jt jtp j t p jt jtp l p lp l p lp l b p lb lbp l b p lb lbp l l p ll llp l l p ll llp j p jp j p jp p j p pj pjp p j p pj pjp j p jp j p jp a j p aj ajp a j p aj ajp j j p jj jjp j j p jj jjp s p sp s p sp r r r rr rrr r r r rr rrr k k r kk kkr k k r kk kkr s r sr s r sr i r ir i r ir r s r rs rsr r s r rs rsr s r sr s r sr l s ls l s ls p s m psm p s m psm t s ts t s ts j s js j s js a s as a s as r h s rh rhs r h s rh rhs m s ms m s ms l m s lm lms l m s lm lms k s ks k s ks h a s ha has h a s ha has g e s ge ges g e s ge ges g e s ge ges g e s ge ges b s bs b s bs d s ds d s ds t s ts t s ts n s s ns nss n s s ns nss t s ts t s ts t s ts t s ts k s ks k s ks m p s mp mps m p s mp mps t p s tp tps t p s tp tps t p s tp tps t p s tp tps l p s lp lps l p s lp lps h a s ha has h a s ha has m t s mt mts m t s mt mts m t s mt mts m t s mt mts d j s dj djs d j s dj djs d e s de des d e s de des b j s bj bjs b j s bj bjs n a s na nas n a s na nas j s js j s js p s s ps pss p s s ps pss h s hs h s hs h s hs h s hs m b a s mba mbas m b a s mba mbas r p s rp rps r p s rp rps m m s mm mms m m s mm mms k t kt k t kt k l t kl klt k l t kl klt m g t mg mgt m g t mg mgt m t mt m t mt c t ct c t ct c t ct c t ct m m g m t mmgm mmgmt m m g m t mmgm mmgmt c t ct c t ct h t ht h t ht h t ht h t ht g t gt g t gt n t nt n t nt k t kt k t kt k t kt k t kt s c t sct s c t sct s c t sct s c t sct s u su s u su p u pu p u pu h u hu h u hu m u mu m u mu b j v bj bjv b j v bj bjv e f v ef efv e f v ef efv m a v ma mav m a v ma mav j v jv j v jv j v jv j v jv a j w g v ajwg ajwgv a j w g v ajwg ajwgv a j v aj ajv a j v aj ajv t v tv t v tv r v rv r v rv j j w jj jjw j j w jj jjw m c w mc mcw m c w mc mcw c t w ct ctw c t w ct ctw c t w ct ctw c t w ct ctw j e w je jew j e w je jew l h w lhw l h w lhw l h w lhw l h w lhw f w fw f w fw p k w pk pkw p k w pk pkw a h w ah ahw a h w ah ahw w j w wj wjw w j w wj wjw w w ww w w ww r k w rk rkw r k w rk rkw c h w ch chw c h w ch chw c h w ch chw c h w ch chw k k w kk kkw k k w kk kkw j w jw j w jw a v x av avx a v x av avx z - x z- z-x z - x z- z-x k y ky k y ky t y ty t y ty k y ky k y ky s y sy s y sy y y yy y y yy g z gz g z gz h d z hdz h d z hdz j z z jzz j z z jzz m m z mm mmz m m z mm mmz m f z mf mfz m f z mf mfz |
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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 |
work_keys_str_mv |
AT ackrellbrianac flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT alivertia flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT andersonrobertf flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT aralryohachi flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT armstrongda flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT arscottldavid flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT astorgaadriennem flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT bacheradelbert flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT bakxedwinj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT baldwinto flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT baldwinthomaso flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT balloudp flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT balloudavidp flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT balloudavid flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT barbermj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT bartschrg flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT bastiaensphil flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT batiechristopherj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT beckerk flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT beintemajaapj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT bellamyhd flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT berkelwillemjhvan flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT berrya flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT blanchardjs flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT bohmontcraig 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flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT byroncolleenm flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT casalinp flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT cecchinigary flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT chastainjl flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT cheddarglen flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT chenlh flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT chenshiuan flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT chikakochikako flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT chlumskylj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT churchichjorgee flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT claiborneal flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT cochranbruce flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT coreydavidp flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT curtib flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT cusanovichma flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT cusanovichmichaela flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT daubnersusancolette flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT defrancescor flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT defrancescoraffaele flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT delarosama flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 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 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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 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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 AT visserantoniejw flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT visserton flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT volkarainer flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT waddlejj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT walkermarkc flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT walshct flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT walshchristophert flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT wamplerje flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT wanglh flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT wangleeho flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT watanabefusao flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT weinerpk flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT westphaladrieh flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT weyerwicherj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT weylerwalter flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT wierengarikk flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT williamsch flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT williamscharlesh flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT wongkk flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT wuj flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT xavierav flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT xiazx flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT yagikunio flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT yamanotoshio flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT yamazakik flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT yoshikawashinya flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT yuyimin flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT zanettig flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT zellerhansdieter flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT zhoujingzhi flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT zieglermm flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 AT zippliesmf flavinsandflavoproteins1987proceedingsoftheninthinternationalsymposiumatlantageorgiausajune7121987 |
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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 / |
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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>.-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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