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

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Superior document:Title is part of eBook package: De Gruyter DGBA Physical Sciences <1990
MitwirkendeR:
Ackrell, Brian A. C.,
Aliverti, A.,
Anderson, Robert F.,
Aral, Ryohachi,
Armstrong, D. A.,
Arscott, L. David,
Astorga, Adrienne M.,
Bacher, Adelbert,
Bakx, Edwin J.,
Baldwin, T. O.,
Baldwin, Thomas O.,
Ballou, D. P.,
Ballou, David P.,
Ballou, David,
Barber, M. J.,
Bartsch, R. G.,
Bastiaens, Phil,
Batie, Christopher J.,
Becker, K.,
Beintema, Jaap J.,
Bellamy, H. D.,
Berkel, Willem J. H. van,
Berkel, Willem J.H. van,
Berry, A.,
Blanchard, J. S.,
Bohmont, Craig,
Bonants, Peter,
Bowers-Komro, D. M.,
Bowers-Komro, Delores M.,
Brandsch, Roderich,
Breakefield, Xandra O.,
Brissette, Pierre,
Brown, Kathleen,
Bryant, Christopher,
Byron, Colleen M.,
Casalin, P.,
Cecchini, Gary,
Chastain, J. L.,
Cheddar, Glen,
Chen, L. H.,
Chen, Shiuan,
Chikako, Chikako,
Chlumsky, L. J.,
Churchich, Jorge E.,
Claiborne, Al,
Cochran, Bruce,
Corey, David P.,
Curti, B.,
Cusanovich, M. A.,
Cusanovich, Michael A.,
Daubner, Susan Colette,
De Francesco, R.,
De Francesco, Raffaele,
De la Rosa, M . A .,
DeLuca, Marlene,
Decker, Karl,
Devine, J. H.,
Distefano, M.,
Distefano, Mark D.,
Drake, Donna M.,
Drenth, Jan,
Dutta, P.,
Eckstein, Jens,
Edmondson, D. E.,
Edmondson, Dale E.,
Einarsdottir, G. H.,
Eisenreich, Wolfgang,
Ellison, Patricia A.,
Engel, Paul C.,
Engelke, David R.,
Ermler, Ulrich,
Fauque, G.,
Fillat, M. F.,
Fillat, M.,
Fish, Kenneth M.,
Florence, Lederer,
Floss, Heinz G.,
Fukui, Kiyoshi,
Galliano, N.,
Ghisla, Sandra,
Ghisla, Sandro,
Ghislat, Sandro,
Giegel, David A.,
Gomez-Moreno, C.,
Grandori, R.,
Green, Jacalyn M.,
Gustafson, William G.,
Gómez-Moreno, C.,
Gückel, F.,
Hall, Carole L.,
Hall, D. O.,
Hazzard, James T.,
Hederstedt, L.,
Heelis, P. F.,
Hille, Russ,
Hinkkanen, Ari E.,
Hoek, Arie van,
Hoi, Wim G. J.,
Hol, Win G. J.,
Holden, H. M.,
Horiike, Kihachiro,
Hsu, Yun-Pung P.,
Hubera, Robert,
Husain, Mazhar,
Ichihara, Chikako,
Inagaki, Taisuke,
Innis, W. S. A.,
Innis-Whitehouse, W. S. A.,
Ishii, Yasuhiko,
Jekel, Peter A.,
Johnston, T. C.,
Jorns, Marilyn Schuman,
Jörns, Marilyn Schuman,
Kaiczyk, G. B.,
Kalk, Kor H.,
Karplus, P. A.,
Kasai, Sabu,
Kawamura-Konishi, Y.,
Kawamura-Konishi, Yasuko,
Kay, C. J.,
Kearney, Edna B.,
Keller, Paul J.,
Kim, J. J. P.,
Klapper, Michael H.,
Kodo, Keiun,
Koerber, Steven C.,
Kok, Arie de,
Koshizaka, Takuya,
Koyama, H.,
Kozioł, J.,
Krauth-Siegel, R. L.,
Krey, Grigorios D.,
Kvalnes-Krick, Kalla,
Kwok, Francis,
König, Astrid,
Laan, Jan M. van der,
Labeyrie, F.,
Ladensteina, Rudolf,
Lau, S-M.,
Laudenbach, David E.,
Le Vana, Quang,
LeGall, J.,
Lederer, F.,
Lee, J.,
Lee, James S.,
Lee, John,
Leisman, Gary,
Lim, L. W.,
Lin, J.-W.,
Lindskog, S.,
Lively, Chris R.,
Ludwig, Martha L.,
Macheroux, Peter,
Maeda, Toshihiro,
Mager, Humphrey I. X.,
Manstein, D. J.,
Manstein, Dietmar J.,
Markley, John L.,
Martin, Tracy,
Massey, V.,
Massey, Vincent,
Mathews, F. S.,
Matsuara, Hiroshi,
Matsui, Kunio,
Matthews, Rowena G.,
Mauch, Ludwig,
Mayhew, Stephen G.,
Mayhew, Steve G.,
McCormick, D. B.,
McCormick, Donald B.,
McFarland, James T.,
McWhirter, Robert B.,
Mclntire, W. S.,
Mclntire, William S.,
Merrill, A. H.,
Meyer, T. E.,
Meyer, Terrance E.,
Mierlo, Carlo P.M. van,
Mierlo, Carlo van,
Miiller, Franz,
Miller, S. M.,
Miura, R.,
Miyake, Y.,
Miyake, Yoshihiro,
Momoi, Kyoko,
Moore, M.,
Moore, Melissa J.,
Moura, I.,
Moura, J. J. G.,
Muller, F.,
Murata, M.,
Müller, Franz,
Nagata, T.,
Nagursky, Heiner,
Nakamura, Makoto,
Nakamura, Takao,
Negri, Armando,
Neujahr, Haiina Y.,
Neujahr, Halina Y.,
Nishikimi, Morimitsu,
Nishina, Yasuzo,
Nishino, T.,
Nishino, Takeshi,
Nishino, Tomoko,
Nishiyama, Kyoko,
Nisimoto, Y.,
Nitta, Satoshi,
Nozaki, Mitsuhiro,
Ohishi, Nobuko,
Ohnishi, Norihiro,
Oka, M.,
Ozawa, Takayuki,
O’Kane, D. J.,
O’Kane, Dennis J.,
O’Nuallain, Eoin M.,
Pai, E. F.,
Pai, Emil F.,
Pattridge, Katherine A.,
Peck, H. D.,
Perham, R. N.,
Pinto, J. T.,
Pollegioni, L.,
Poole, Leslie B.,
Poulsen, L. L.,
Powell, John,
Powell, P. J.,
Powlowski, Justin,
Prongay, Andrew J.,
Pueyo, J. J.,
Pust, Stefan,
Ramsay, Rona R.,
Rao, K. K.,
Ratti, S.,
Rayment, I.,
Rivlin, R. S.,
Ronchi, S.,
Sahlman, Lena,
Saint-Martin, P.,
Saito, T.,
Sancho, J.,
Sandström, A.,
Schirmer, R. H.,
Schneider, Monika,
Schopfer, Lawrence M.,
Schott, Karin,
Schreuder, Herman A.,
Schulz, G. E.,
Schulz, Georg E.,
Schwarzkopf, Bruno,
Schweitzer, D.,
Schöllhammer, T.,
Scrutton, N. S.,
Sejlitz, Torsten,
Shibata, Toshihiro,
Shiga, Kiyoshi,
Simonetta, M. Pilone,
Singer, T. P.,
Singer, Thomas P.,
Solomonson, L. P.,
Staab, H. A.,
Stankovich, M. T.,
Stankovich, Marian T.,
Steenkamp, D. J.,
Stewart, D. E.,
Stockman, Brian J.,
Straus, Neil A.,
Sugihara, J.,
Surdhar, P. S.,
Suzuki, H.,
Suzuki, Haruo,
Swarte, Myra B. A.,
Swenson, Richard P.,
Szafran, M. M.,
Takeshima, Katsuhito,
Taylor, K. L.,
Taylor, M. G.,
Tegoni, M.,
Thorpe, C.,
Thorpe, Colin,
Thunnissen, Marjolein M. G. M.,
Titlow, Christian,
Tojo, Hiroaasa,
Tojo, Hiromasa,
Tollin, Gordon,
Tsukagoshi, Norihiro,
Tsushima, K.,
Tsushima, Keizo,
Tu, S.-C.,
Tu, Shiao-Chun,
Udaka, Shigezo,
Urban, Philippe,
Ushijiaa, Hidetaka,
Utterback, Margot,
Van Beeumen, J.,
Vanin, Elio F.,
Vanoni, M. A.,
Vervoort, J.,
Vervoort, Jacques,
Visser, Antonie J. W. G.,
Visser, Antonie J.W.,
Visser, Ton,
Volka, Rainer,
Waddle, J. J.,
Walker, Mark C.,
Walsh, C. T.,
Walsh, Christopher T.,
Wampler, J. E.,
Wang, L.-H.,
Wang, Lee-Ho,
Watanabe, Fusao,
Weiner, P. K.,
Westphal, Adrie H.,
Weyer, Wicher J.,
Weyler, Walter,
Wierenga, Rik K.,
Williams, C. H.,
Williams, Charles H.,
Wong, K. K.,
Wu, J.,
Xavier, A. V.,
Xia, Z. -x.,
Yagi, Kunio,
Yamano, Toshio,
Yamazaki, K.,
Yoshikawa, Shinya,
Yu, Yimin,
Zanetti, G.,
Zeller, Hans-Dieter,
Zhou, Jing-Zhi,
Ziegler, M. M.,
Zipplies, M. F.,
HerausgeberIn:
Place / Publishing House:Berlin ;, Boston : : De Gruyter, , [2019]
©1987
Year of Publication:2019
Edition:Reprint 2019
Language:English
Online Access:
Physical Description:1 online resource (XXIII, 775 p.) :; Num. figs.
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Other title: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
Format:Mode of access: Internet via World Wide Web.
ISBN:9783110884715
9783110637243
DOI:10.1515/9783110884715
Access:restricted access
Hierarchical level:Monograph
Statement of Responsibility: ed. by D. E. Edmondson, D. B. McCormick.