Flavins and Flavoproteins 1993 : : Proceedings of the Eleventh International Symposium, Nagoya, Japan, July 27–31, 1993 / / ed. by Kunio Yagi.

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Superior document:Title is part of eBook package: De Gruyter DGBA Reference Works 1990 - 1999
MitwirkendeR:
Abell, C.,
Abu-Soud, H. M.,
Aki, Kenji,
Akker, F. van den,
Aliverti, A.,
Amaya, Yoshihiro,
Anderson, R.F.,
Arscott, L. David,
Arunachalam, Usha,
Ashby, G.A.,
Babbitt, Patricia C.,
Bacher, A.,
Balasubramanian, S.,
Baldwin, T. O.,
Ballou, D.,
Ballou, David P.,
Balme, Alexis,
Bando, S.,
Bannister, J. V.,
Bartsch, R. G.,
Bashir, Asam,
Batie, C.,
Belmouden, Ahmed,
Bendrat, K.,
Bennett, D.W.,
Berg, A.,
Berkel, W. van,
Berkel, W.J.H. van,
Berry, Alan,
Bes, M.T.,
Blow, David,
Boeren, J.A.,
Boersma, M.G.,
Bolt, F.J.T. van der,
Bont, J.A.M. de,
Bornemann, S.,
Brandsch, R.,
Brandt, J.,
Brick, Peter,
Bross, P.,
Brosst, P.,
Brown, Bette Jo,
Bruns, C.M.,
Buckel, W.,
Buckel, Wolfgang,
Böhme, H.,
Bückmann, A. F.,
Calzi, M. Li,
Campbell, Wilbur H.,
Cazzaniga, G.,
Ceciliani, F.,
Ceciliani, Fabrizio,
Chae, Y.K.,
Chaffotte, A.-F.,
Chapman, Stephen K.,
Chen, Shiuan,
Cheng, H.,
Chlumsky, Lawrence J.,
Claiborne, Al,
Clark, A. C.,
Cnubben, N.H.P.,
Cockerill, Matthew J.,
Coggins, J. R.,
Correll, C. C.,
Crane, Edward J.,
Cummings, J.G.,
Curti, B.,
Curti, Bruno,
Cusanovich, M. A.,
Cusanovich, M.A.,
Cushman, M.,
Daff, Simon,
Danno, M.,
Davies, G. M.,
Davis, B.A.,
Denu, J.M.,
Deonarain, Mahendra P.,
Dixon, M.M.,
Djordjevic, S.,
Dolata, M. M.,
Doolittle, W. F.,
Drummond, M.H.,
Dunham, W. R.,
Dwivedi, U.N.,
Eady, R.R.,
Eberhardt, S.,
Edmondson, Dale E.,
Eger, B. T.,
Eikmanns, U.,
Eikmanns, Ulrich,
Emanuele, J.J.,
Engst, S.,
Entsch, Barrie,
Eppink, M.H.M.,
Erdmann, H.,
Ernster, L.,
Esaki, Nobuyoshi,
Fabisz-Kijowska, A.,
Falciani, F.,
Faotto, L.,
Fernández, V.M.,
Fillat, M.F.,
Fitch, J.,
Fitch, J.C.,
Fitzpatrick, P.F.,
Fontecilla-Camps, J.,
Ford, G.,
Fox, Kristin M.,
Fraaije, M.W.,
Francisco, W. A.,
Frey, M.,
Fujii, S.,
Fukui, Kiyoshi,
Fukumori, Y.,
Fumagalli, P.,
Gadda, G.,
Galbiati, F.,
Garattini, E.,
García-Ramírez, J.J.,
Gassen, H.G.,
Gassner, G.,
Gatti, A.,
Gatti, D.,
Gatti, D.L.,
Gatti, Domenico,
Gerlt, John A.,
Ghisla, S.,
Ghisla, Sandro,
Goldwurm, S.,
Gomez-Moreno, C.,
Gondry, Muriel,
Gómez-Moreno, C.,
Hall, J. M.,
Harris, Christopher M.,
Harrison, P.M.,
Hawkes, T. R.,
Hazekawa, I.,
Higashiyama, M.,
Hikichi, S.,
Hill, H.A.O.,
Hille, Russ,
Hirasiki, I.,
Hoi, W.G.J.,
Hong, Yeong-Man,
Hoover, D. M.,
Hopkins, Nancy,
Horii, C.,
Horiike, Kihachiro,
Horowitz, P. M.,
Hosoya, Tatsuo,
Huber, R.,
Hughes, D.L.,
Hunt, Jennifer,
Hurley, J.K.,
Härtel, Ulrich,
Ichida, Kimiyoshi,
Ichikawa, Y.,
Ichikawa, Yoshiyuki,
Ikemi, Yoshiaki,
Ishida, N.,
Ishida, Tetsuo,
Itagaki, Eiji,
Ito, A.,
Iwamoto, Takeshi,
Iwasaki, Toshio,
Jacoby, E.,
Johnson, Bruce D.,
Jong, E. de,
Jonsson, Thoriakur,
Jorns, Marilyn S.,
Joseph, Diane,
Kadode, Michiaki,
Karplus, P. Andrew,
Karplus, P.A.,
Kasai, S.,
Katsuya, Y.,
Kawamoto, Susumu,
Kazlauskaite, J.,
Kenyon, George L.,
Kieweg, V.,
Kim, J.J.P.,
Kimoto, Masumi,
Kis, K.,
Klees, A.-G.,
Klinman, Judith P.,
Kobayashi, J.,
Kobayashi, K.,
Koerts, J.,
Koike, Kichiko,
Koike, Masahiko,
Kok, A. de,
Komura, S.,
Koyama, Hirokazu,
Krauth-Siegel, R.L.,
Krishna, Talluru S. R.,
Kräutle, F.,
Kurihara, Tatsuo,
Kuriyan, John,
Kuroda, K.,
Ladenstein, R.,
Lah, Myoung S.,
Langkau, B.,
Lantwin, C.B.,
Lederer, Florence,
Lee, J.,
Lei, Benfang,
Lennon, Brett W.,
Li, Jiayao,
Lindqvist, Ylva,
Lowe, D. J.,
Ludwig, M. L.,
Ludwig, M.L.,
Ludwig, Martha L.,
Lumberg, Michael S.,
López, A.,
Macheroux, Peter,
Mack, M.,
Maeda-Yorita, Kazuko,
Mager, Humphrey I. X.,
Manson, Forbes D. C.,
Manson, Forbes D.C.,
Markley, J.L.,
Massey, V.,
Massey, Vincent,
Masters, B. S. S.,
Mathews, F. Scott,
Matsui, K.,
Matsuo, Yoshinori,
Matsushita, Hiroyuki,
Matsuura, Katsumi,
Mattevi, A.,
Matthews, R. G.,
Mazzoni, A.,
McMillan, Kirk,
Medina, M.,
Menon, V.,
Meyer, T. E.,
Meyer, T.E.,
Miki, M.,
Miller, S.M.,
Minoia, C.,
Minoshima, Shinsei,
Mitoma, J.,
Mitra, Bharati,
Mitsui, K.,
Miura, R.,
Miura, S.,
Miura, Shigetoshi,
Mortarino, M.,
Mukouyama, Etsuko B.,
Mulrooney, Scott B.,
Murakami, H.O.,
Murthy, Yerramilli V.S.N.,
Müh, U.,
Müller, U.,
Nabeshima, T.,
Nakashima, M.,
Nandy, A.,
Narayanasami, R.,
Natori, Yasuo,
Negri, A.,
Nichols, W. W.,
Nicoletti, Aileen,
Niimura, Youichi,
Nishikawa, Toyohiro,
Nishikimi, M.,
Nishina, Y.,
Nishina, Yasuzo,
Nishino, T.,
Nishino, Takeshi,
Nishino, Tomoko,
Nisimoto, Y.,
Noda, Kumi,
Obata, Shigehiro,
Ogata, F.,
Ogawa, K.,
Ogawa, Tadashi,
Ohishi, N.,
Ohishi, Nobuko,
Ohnishi, Kenji,
Ohsawa, Y.,
Oka, Tatsuzo,
Okamoto, K.,
Okamoto, Ken,
Oschkinat, H.,
Oshima, Tairo,
Otvos, J. D.,
Pacheco, M.C.,
Packman, Leonard C.,
Page, Theodore,
Pai, E. F.,
Pai, Emil F.,
Palfey, Bruce A.,
Parsonage, Derek,
Paschke, R.,
Pattridge, K.A.,
Pealing, Sara L.,
Peelen, S.,
Peiham, Richard N.,
Pelanda, R.,
Peleato, M.L.,
Perham, Richard N.,
Petsko, Gregory A.,
Pietzsch, M.,
Pilone, M.S.,
Pilone, Mirella S.,
Piubelli, L.,
Pollegioni, L.,
Pollegioni, Loredano,
Poole, Leslie B.,
Ramjee, M. N.,
Ramsay, Rona R.,
Ramsey, Andrew J.,
Rasched, I.,
Raushel, F. M.,
Razquin, P.,
Reid, Graeme A,
Reid, Graeme A.,
Rescigno, Maria,
Revuelta, J.L.,
Richter, G.,
Rietjens, I.M.C.M.,
Rietveld, Patrick,
Ritsert, K.,
Ritz, H.,
Robson, R.L.,
Rohlfs, Ronald J.,
Ronchi, A.,
Ronchi, S.,
Ronchi, Severino,
Ross, R. Paul,
Sablin, Sergey O.,
Saito, Tatsuya,
Sakai, Osamu,
Sakihama, Naoko,
Salamon, Z.,
Salmona, M.,
Sands, R.H.,
Santos, M.A.,
Sasaki, Toshihide,
Sato, Akira,
Sato, K.,
Sato, Kyosuke,
Sato, M.,
Schaffner, Myriam,
Schalkwyk, L. C.,
Scherf, Uwe,
Scheuring, J.,
Schiavo, P. Lo,
Schmidt-Base, K.,
Schmitz, S.,
Schreuder, Herman A.,
Scrutton, Nigel S.,
Segalla, F.,
Sekido, Toshihiro,
Serre, L.,
Sharp, R. Eryl,
Shaw, A.,
Sheta, Essam,
Shiga, K.,
Shiga, Kiyoshi,
Shimizu, Nobuyoshi,
Shin, Masateru,
Shirabe, K.,
Shirabe, Komei,
Siler Masters, Bettie Sue,
Simonie, T.,
Sinclair, J. F.,
Singer, Thomas P.,
Smekal, Otto,
Soda, Kenji,
Soffers, A.E.M.F.,
Stankovich, Marian T.,
Stevenson, Kj.,
StraussH, A.W.,
Suzuki, Haruo,
Suzuki, Kenzi,
Swenson, R.P.,
Szymusiak, Henryk,
Takano, T.,
Takenaka, Akio,
Takeshita, M.,
Takeshita, Masazumi,
Tanaka, F.,
Tchorzewski, Marek,
Tedeschi, G.,
Tedeschi, Gabriella,
Terao, M.,
Thorneley, R. N. F.,
Thorneley, R.N.F.,
Thorpe, C.,
Tollin, G.,
Tomita, Shuhei,
Tsugeno, Y.,
Tsuji, Hideaki,
Tsujita, Maki,
Tu, Shiao-Chun,
Van Beeumen, J.,
Vanoni, M A.,
Vanoni, Maria A.,
Varga, E.,
Veeger, C.,
Veine, Donna M.,
Vellieux, F.,
Vervoort, J.,
Verzotti, E.,
Vettakkorumakankav, N.N.,
Vock, P.,
Vockley, J.,
Vrielink, Alice,
Wakagi, Takayoshi,
Waksman, Gabriel,
Walker, Mark C.,
Wang, L.,
Wang, M.,
Ward, Don,
Ward, F. Bruce,
Weinkauf, S.,
Westphal, A.,
White, Patricia,
Williams, C. H.,
Williams, Charles H.,
Woodland Hastings, J.,
Wu, Ru-Feng,
Xia, B.,
Yagi, K.,
Yamanaka, T.,
Yano, Y.,
Yokoyama, Kazunori,
Yu, P. H.,
Yubisui, T.,
Yubisui, Toshitsugu,
Yuvaniyama, Jirundon,
Zanetti, G.,
Zhang, Lening,
Ziegler, M. M.,
HerausgeberIn:
Place / Publishing House:Berlin ;, Boston : : De Gruyter, , [2020]
©1994
Year of Publication:2020
Edition:Reprint 2020
Language:English
Online Access:
Physical Description:1 online resource (889 p.)
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Other title:Frontmatter --
PREFACE --
Committees --
CONTENTS --
THEORETICAL AND CHEMICAL APPROACH --
Use of Molecular Orbital Calculations in Studies on Mechanisms of Enzyme Catalysis --
A theoretical approach of the mechanism of C(4a)-peroxyflavin catalyzed reactions --
Semiempirical calculations on properties of (iso)alloxazines in ground and excited states --
Pathways for a 4a-hydroxy-4a,5-dihydroflavin radical in the hydroxylation of aromatics --
CHEMICAL SYNTHESIS OF NEKOFLAVIN --
NOVEL 5 - SUBSTITUTED 5 - DEAZAFLAVINS : SYNTHESIS AND APPLICATIONS AS ACTIVE SITE PROBES FOR FLAVOPROTEINS --
D-Lactate Dehydrogenase Model. Oxidation of a-Hydroxy Acid by Functionalized Oxidation Active flavin Mimic in the Presence of Zn2+ and Base in t-Butanol --
Mechanism of Flavin Reduction By Cu(I)-EDTA Complex --
SELF-ASSOCIATION OF FLAVIN: INTERACTION OF FMN WITH ALBUMIN --
BIOSYNTHESIS OF FLAVINS --
STUDIES ON THE BIOSYNTHESIS OF FLAVINS. STRUCTURE AND MECHANISM OF 6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE --
BIOSYNTHESIS OF RIBOFLAVIN. CLONING, SEQUENCING, MAPPING, AND HYPEREXPRESSION OF THE GENES ribA CODING FOR GTP CYCLOHYDROLASE II AND ribC CODING FOR RIBOFLAVIN SYNTHASE OF ESCHERICHIA COLL --
BIOSYNTHESIS OF RIBOFLAVIN: ENZYMATIC FORMATION OF 6,7-DIMETHYL-8-RIBITYLLUMAZINE IN Saccharomyces cerevisiae --
ELECTRON MICROSCOPIC STUDIES ON THE LUMAZINE SYNTHASE/ RIBOFLAVIN SYNTHASE COMPLEX OF BACILLUS SUBTILIS --
19F NMR STUDIES ON LUMAZINE PROTEIN FROM PHOTOBACTERIUM PHOSPHOREUM --
19F NMR STUDIES ON THE MECHANISM OF RIBOFLAVIN SYNTHASE --
OXIDASES --
STUDIES ON ACTIVE SITE MUTANTS OF SPINACH GLYCOLATE OXIDASE --
HIGH-LEVEL EXPRESSION OF RAT KIDNEY HYDROXY ACID OXIDASE IN ESCHERICHIA COLI: PURIFICATION AND CHARACTERIZATION OF THE RECOMBINANT PROTEIN --
The Influence of Substrate Structure on the Redox Reactions of Monoamine Oxidases --
QUANTITATIVE STRUCTURE-ACTIVITY RELATIONSHIPS IN THE OXIDATION OF BENZYLAMINE ANALOGUES BY BOVINE LIVER MONOAMINE OXIDASE B --
Experimental Probes of Hydrogen Tunneling in Bovine Liver Monoamine Oxidase B --
Stereospecificity and Deuterium Isotope Effect in the Oxidative Deamination Catalyzed by Flavine and Non-flavine Amine Oxidases --
CHARACTERIZATION OF L-ASPARTATE OXIDASE OVEREXPRESSED IN E. COLI --
IDENTIFICATION OF ANOTHER SUBUNIT IN L-PHENYLALANINE OXIDASE FROM PSEUDOMONAS SP. P-501 AND THE PRIMARY STRUCTURE OF THE SUBUNIT --
Kinetic Isotope Effects on Reductive Half-Reactions of Flavoprotein Oxidases --
Effects of Ligands on the Reactivities of Reduced and Semiquinoid Forms of D-Amino Acid Oxidase --
Thermodynamic Study of FAD Binding in D-Amino Acid Oxidase --
Structure of Human D- Amino Acid Oxidase Gene --
AMINO ACID SEQUENCE OF D-AMINO ACID OXIDASE FROM THE YEAST Rhodotorula gracilis --
CHEMICAL MODIFICATION OF ARGEVINE GROUPS IN D-AMINO ACID OXIDASE FROM Rhodotorula gracilis Involvement in catalysis and assignment in the sequence --
FUNCTIONAL AND STRUCTURAL ASPECTS OF D-AMINO ACID OXIDASE FROM Rhodotorula gracilis PROBED BY LIMITED PROTEOLYSIS --
THE CRYSTAL STRUCTURE OF CHOLESTEROL OXIDASE. MECHANISTIC IMPLICATIONS FOR FAD DEPENDENT ALCOHOL OXIDATION --
Nitroalkane-Oxidizing Flavoenzymes --
A 340-nm Chromophore of Nitroalkane Oxidase from Fusarium oxysporum --
OXYGENASES --
LACTATE MONOOXYGENASE: STUDIES OF ACTIVE SITE MUTATIONS --
The Mobile Flavin of Parahydroxybenzoate Hydroxylase - A Case for Major Structural Dynamics in Catalysis --
Structures of Mutant p-Hydroxybenzoate Hydroxylases: Evidence for an Alternative Mode of Flavin Binding --
Substrate and Effector Specificity of Two Active-Site Mutants of p-Hydroxybenzoate Hydroxylase from Pseudomonas fluorescens --
Solvent Isotope Effects on p-Hydroxybenzoate Hydroxylase --
IMMUNOLOGICAL STUDIES ON THE STRUCTURE OF 4-AMINOBENZOATE HYDROXYLASE FROM AGARICUS BISPORUS --
STUDIES ON p-HYDROXYPHENYLACETATE-3-HYDROXYLASE --
Fluorescent Intermediates and the Reaction Mechanism of Phenol Hydroxylase --
Application of pulse radiolysis to produce absorbing species of substrates for flavoprotein hydroxylases --
Mammalian Flavin-Containing Monooxygenase Catalyzed Conversion of 4-Halo-NMethylanilines --
2-AMINOBENZOYL-CoA-MONOOXYGENASE/REDUCTASE, AN ENZYME WITH TWO DISTINCT FUNCTIONS AND ONE ACTIVE CENTER --
Characteristic Properties and Kinetic Analysis of Neurotoxins for Porcine FAD-containing Monooxygenase --
Genomic DNA Structure of a Unique Flavoprotein, 2-Nitropropane Dioxygenase from Hansenula rnrakii --
DEHYDROGENASES AND ELECTRON TRANSFER --
THREE DIMENSIONAL STRUCTURES OF ACYL-CoA DEHYDROGENASES: STRUCTURAL BASIS OF SUBSTRATE SPECIFICITY --
MECHANISM OF a,ß-DEHYDROGENATION BY ACYL-COA DEHYDROGENASES --
13C- and 15N-NMR Studies of Medium-Chain Acyl-CoA Dehydrogenase from Porcine Kidney --
Resonance Raman Studies on Acyl-CoA Dehydrogenases --
Two New Mechanism-Based Inhibitors of the Acyl-CoA Dehydrogenases --
STÜDES OF THE THERMODYNAMIC REGULATION OF MEDIUM CHAIN ACYL-CoA DEHYDROGENASE --
LONG-CHAIN SPECIFIC ENZYME FROM MEDIUM-CHAIN ACYL-COA DEHYDROGENASE --
Glutaryl-CoA dehydrogenase from anaerobic, benzoate degrading Pseudomonas sp.: An FAD-dependent glutaconyl-CoA decarboxylase --
CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDY OF THE BIFUNCTIONAL FLAVOENZYME 5-HYDROXYVALERYL-COA DEHYDRATASE/DEHYDROGENASE FROM CLOSTRIDIUM AMINOVALERICUM --
ESSENTIAL ARGININE RESIDUE(S) OF 3-KETOSTEROID-Δ1- DEHYDROGENASE --
Flavodoxins and Nitrogen Fixation - Structure, Electrochemistry and Post-translational Modification by Coenzyme A --
REGULATION OF THE EXPRESSION OF FLAVODOXIN AND FERREDOXIN IN Anabaena PCC 7120 UNDER IRON AND NITROGEN LIMITING CONDITIONS --
Crystallization and X-ray Structure Determination of E. coli Flavodoxin --
Cis-trans Isomerization of the 57-58 Peptide in Crystalline Flavodoxins from C. beijerinckii --
Electron-Transferring Flavoprotein from Pig Kidney Contains an AMP --
The Enigma of Old Yellow Enzyme. II --
STIRRING NEW INTEREST IN AN OLD ENZYME: CRYSTAL STRUCTURE OF OLD YELLOW ENZYME --
EFFECT OF DELETION AND MUTATION OF OLD YELLOW ENZYME GENE FROM SACCHAROMYCES CEREVISIAE --
STRUCTURE AND FUNCTION OF NADH-CYTOCHROME b5 REDUCTASE IN RELATION TO HEREDITARY METHEMOGLOBINEMIA --
ROLE OF FLAVIN BINDING MOTIF, RxY(T/S), OF NADH-CYTOCHROME b5 REDUCTASE IN ELECTRON TRANSFER REACTION --
THE STRUCTURE OF HUMAN ERYTHROCYTE NADH-CYTOCHROME b5 REDUCTASE AT 2.5Â RESOLUTION --
Two Bound Forms of Ferredoxin-NADP Reductase in Chloroplast Thylakoids --
CHARACTERIZATION OF ACTIVE-SITE MUTANTS OF FERREDOXIN-NADP+ REDUCTASE --
Structural Study of Ferredoxin-NADP+ Reductase from Anabaena PCC 7119 and of Its Complex with NADP+ --
Structure-Function Relationships in Ferredoxin: Site-Directed Mutagenesis and Time-Resolved Absorption Spectroscopy Applied to the Ferredoxin:Ferredoxin NADP+ Reductase Interaction --
N-Terminal Structure of Mature Ferredoxin-NADP Reductase --
Refined Crystal Structures of Native, Complexed and Reduced Forms of Spinach Ferredoxin Reductase --
Overexpression of ferredoxin-NADP+ reductase from Anabaena sp. PCC7119 in E.coli --
THE REDUCTASE ACTIVITY OP A FLAVOPROTEIN IS CHANGED INTO A SUPEROXIDE-FORMING OXIDASE BY CHEMICAL MODIFICATION --
FNR -LIKE FLAVOPROTEINS OF CHEMOAUTOTROPHIC BACTERIA AND PHOTOSYNTHETIC BACTERIA --
1H NMR investigation of NADPH-adrenoferredoxin reductase with NADP+ and adrenoferredoxin --
One electron reduction of adrenodoxin reductase as studied by pulse radiolysis --
STRUCTURE-FUNCTION STUDIES ON NADPH-CYTOCHROME P450 REDUCTASE USING UREA-PERTURBATION AND 19F NMR SPECTROSCOPY --
Cerebellar Nitric Oxide Synthase Behaves as a Bi-Domain Structure --
STUDIES ON NAD(P)H-QUINONE OXIDOREDUCTASE --
EFFECT OF RIBOFLAVIN DEFICIENCY ON DT-DIAPHORASE --
DISULFIDE REDUCTASES --
Hybrid Molecules of Glutathione Reductase: Tools for Investigating Protein Interactions at the Dimer Interface --
THE REDUCTIVE HALF REACTION OF ESCHERICHIA COLI GLUTATHIONE REDUCTASE --
DETERMINATION OF THE REDOX POTENTIAL OF E.
COLI GLUTATHIONE REDUCTASE USING NADH AND NAD+ --
AN INVESTIGATION OF ENGINEERED CO-OPERATIVITY IN INTERFACE MUTANTS OF ESCHERICHIA COU GLUTATHIONE REDUCTASE --
ROLE OF CONSERVED GLYCINE RESIDUES IN THE NADPH BINDING MOTIF OF GLUTATHIONE REDUCTASE --
Eukaryotic Lipoamide Dehydrogenase: Molecular Genetic and Structural Aspects --
Disruption of the Gene Coding for Dihydrolipoamide Dehydrogenase in Haloferax volcanii by Homologous Recombination --
Redox Properties of the FAD in the Active Site Mutants C44S and C49S of Escherichia coli Lipoamide Dehydrogenase --
R- AND S-DIHYDROLIPOIC ACID DERIVATIVES AS SUBSTRATES OF LIPO AMIDE DEHYDROGENASE --
Comparative Study on Flavin Radical Formation of Llipoamide Dehydrogenase and Glutathione Reductase by Photoreduction --
The Pyruvate Dehydrogenase Complex from Azotobacter vinelandii --
The 3-dimensional structure of trypanothione reductase from Trypanosoma cruzi as a basis for drug design against Chagas' disease --
MECHANISM AND STRUCTURE OF THIOREDOXIN REDUCTASE --
E. COLI THIOREDOXIN REDUCTASE - POTENTIAL ACID-BASE CATALYSTS - PROPERTIES OF HIS-245 AND ASP-139 MUTANTS --
RAPID REACTION KINETICS OF ESCHERICHIA COLI THIOREDOXIN REDUCTASE --
2'- Fluoro - 2'- Deoxy - Arabino - FAD: Effects On The Formation And Stability Of 2-Electron Reduced Mercuric Ion Reductase --
The Alkyl Hydroperoxide Reductase of Salmonella typhimurium: Redox Activity of the Cystine Disulfide of AhpC and Evidence for Involvement in Peroxide Reduction --
FLAVOPROTEIN PEROXIDE AND DISULFIDE REDUCTASES AND THEIR ROLES IN STREPTOCOCCAL OXIDATIVE METABOLISM --
N6-(2-AMINOETHYL)-FAD: SYNTHESIS AND COENZYME ACTIVITY WITH RESPECT TO APO-NADH OXIDASE FROM THERMUS THERMOPHILICS AND THERMUS AQUATICUS --
A FLAVOPROTEIN FUNCTIONAL AS NADH OXIDASE FROM Amphibacillus xylanus EpOl --
COMPLEX FLAVOPROTEINS --
Probing the Structure and Function of Flavocytochrome b2 Using Protein Engineering Methods --
The L-Mandelate Dehydrogenase from Rhodotorula gratninis is a Flavocytochrome b2 --
S-MANDEL ATE DEHYDROGENASE FROM PSEUDOMONAS PUTIDA: CONSTRUCTION OF A SOLUBLE CHIMERIC MUTANT OF A MEMBRANE-BOUND ENZYME --
The D282N and Y254L active-site mutants of flavocytochrome b2 are expressed in E. coli as a mixture of holoenzyme and flavin-free protein --
RECONSTITUTION OF FLAVIN-FREE FLAVOCYTOCHROME b2 WITH 5-DEAZAFMN : A CARBANION OR A HYDRIDE MECHANISM ? --
Physical Studies on Phthalate Dioxygenase Reductase (PDR) --
Structures of Oxidized, Reduced, and Liganded States of the Iron-Sulfur Flavoprotein, Phthalate Dioxygenase Reductase --
Flavin and iron-sulfur cluster containing hydroxyacyl-CoA dehydratases (I) (R)-2-Hydroxyglutaryl-CoA dehydratases from Acidaminococcus fermentans and Fusobacterium nucleatum --
Flavin and iron-sulfur containing hydroxyacyl-CoA dehydratases (II) 4-Hydroxybutyryl-CoA dehydratase from Clostridium aminobutyricum --
Glutamate synthase from AzospiriUum brasilense: structural and mechanistic studies --
Cloning and Expression of Azospirillum brasilense Glutamate Synthase --
Phototrophic Bacterial Flavocytochromes c --
Structure and Function of the Soluble Fumarate Reductase, Flavocytochrome c, from Shewanella putrefaciens --
XANTHINE DEHYDROGENASE: STRUCTURE AND PROPERTIES --
THE PRIMARY STRUCTURE OF HUMAN XANTHINE DEHYDROGENASE AND CHROMOSOMAL LOCATION OF THE GENE --
Overexpression and Characterization of Xanthine Dehydrogenase in a Baculovirus-Insectcell System --
Redox Potentials of Milk Xanthine Dehydrogenase --
Electron transfer in milk xanthine dehydrogenase as studied by pulse radiolysis --
A COMPARISON OF SUBSTRATE SPECIFICITY BETWEEN MILK XANTHINE OXIDASE AND XANTHINE DEHYDROGENASE --
CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION OF XANTHINE OXIDASE ISOLATED FROM BOVINE MILK --
NEW TIGHT BINDING INHIBITORS OF XANTHINE OXIDASE --
Molecular cloning and structural characterization of the gene locus coding for mouse xanthine oxidoreductase --
Mouse L929 cells are defective in the expression of xanthine oxidoreductase enzymatic activity and molybdenum (VI) salts can complement the deficit --
Physicochemical Properties of Retinal Oxidase Purified from Rabbit Hepatic Cytosol --
Mutagenesis of the Cysteine Residues of the FAD Domain of Nitrate Reductase --
Electron Transfer and Prototropic Equilibria in Two Complex Metalloflavoproteins --
THE ABSENCE OF PROTOHEME IN ACTIVE RESPIRATORY COMPLEX II OF THE THERMO ACIDOPHILIC ARCH AEON, SULFOLOBUS SP. STRAIN 7 --
Unique Properties of the "Rotenone Site" of NADH-Q Oxidoreductase --
Reconstitution of a Cell-free Superoxide Generation of Human Neutrophil --
FLAVOPROTEINS CONTAINING COVALENTLY-BOUND FLAVINS --
Preparation and Properties of Recombinant Corynebacterial Sarcosine Oxidase --
One-Step Cloning and Overexpression of the Sarcosine Oxidase Operon from Corynebacterium sp. P-1 --
L-GULONO-γ-LACTONE OXIDASE — cDNA CLONING AND ELUCIDATION OF THE GENETIC DEFECT IN A MUTANT RAT WITH OSTEOGENIC DISORDER --
HIGH-LEVEL EXPRESSION OF RAT L-GULONO-y-LACTONE OXIDASE IN SILKWORM CELLS WITH A BACULOVIRUS VECTOR --
Structures Responsible for FAD Binding and Substrate Recognition of Rat Liver Monoamine Oxidase --
Vanillyl-Alcohol Oxidase from Pénicillium simplicissimum: A Novel Flavoprotein Containing 8a-(N3-histidyl)-FAD --
Flavinylation of the Trimethylamine Dehydrogenase of Bacterium W3A1 Expressed in Escherichia coli --
A New Family of Flavoenzymes ? --
ENZYMES USING REDUCED FLAVIN FOR THEIR ACTIVITY --
THE BACTERIAL LUCIFERASE REACTION: MODEL OR MAVERICK IN FLAVIN BIOCHEMISTRY? --
KINETIC CONTROL OF FOLDING AND ASSEMBLY OF HETERODIMERIC BACTERIAL LUCIFERASE --
KINETIC MECHANISM OF THE BACTERIAL LUCIFERASE REACTION --
BACTERIAL LUCIFERASE: BIOLUMINESCENCE EMISSION USING LUMAZINES AS SUBSTRATES --
Studies on Escherichia coli Chorismate Synthase --
Characterization of the Vibrio harveyi NADPH:FMN Oxidoreductase Expressed in Escherichia coli --
LIST OF PARTICIPANTS --
AUTHOR INDEX --
SUBJECT INDEX --
Backmatter
Format:Mode of access: Internet via World Wide Web.
ISBN:9783110885774
9783110637335
DOI:10.1515/9783110885774
Access:restricted access
Hierarchical level:Monograph
Statement of Responsibility: ed. by Kunio Yagi.