توضیحاتی در مورد کتاب Flavins and Flavoproteins: Proceedings of the Eighth International Symposium, Brighton, England, July 9–13, 1984
نام کتاب : Flavins and Flavoproteins: Proceedings of the Eighth International Symposium, Brighton, England, July 9–13, 1984
ویرایش : Reprint 2019
عنوان ترجمه شده به فارسی : فلاوین ها و فلاووپروتئین ها: مجموعه مقالات هشتمین سمپوزیوم بین المللی، برایتون، انگلستان، 9 تا 13 ژوئیه، 1984
سری :
نویسندگان : R. C. Bray (editor), P. C. Engel (editor), S. G. Mayhew (editor)
ناشر : De Gruyter
سال نشر : 1984
تعداد صفحات : 960
ISBN (شابک) : 9783111521350 , 9783110098792
زبان کتاب : English
فرمت کتاب : pdf
حجم کتاب : 41 مگابایت
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فهرست مطالب :
Preface\nOrganising Committee/Local Committee/Acknowledgements\nContents\nParticipants\nFlavin Chemistry\nThe influence of hydrogen bond formation with the N(l) atom on the orbital structure of flavin\nSpectral and photochemical properties of alloxazines\nπ...π-interactions of flavins : novel coenzyme models of the cyclophane type\nA laser flash photolysis study of the triplet states of lumichromes\nThe dark formation of radicals in flavinium cation/acid systems\nENDOR studies on flavin radicals\nOn the role of some flavin adducts as one-electron donors\nPhotoinactivation of flavin redox catalysis: the reductive flavin photoadduct formation\nFlavin oxygen chemistry brought to date\nPulse radiolysis studies on the equilibria between reduced and oxidized free flavin species and the effect of molecular oxygen\nEffect of pH on the oxidation-reduction properties of 8α - imidazole flavins\nStudies of intermediates in reactions of flavins and sulphydryl compounds\nA kinetic study on the acid-catalysed phosphate migration in riboflavin phosphates\nChemical structure of nekoflavin\nFlavoprotein Structure\nBinding mode and action of FAD in glutathione reductase\nActive site chemical modification and sequencing of flavoproteins\nMolecular genetic approaches to the study of E. coli flavoproteins\nGlutathione reductase: mutation, cloning and sequence analysis of the gene in E. coli\nThe coenzyme binding site of glutathione reductase. Correlation of X-ray studies with kinetic data\n13C-NMR study on the active sites of lipoamide dehydrogenase and glutathione reductase\nX-ray crystallographic studies on lipoamide dehydrogenase from Azotobacter vinelandii\nMobility of lipoamide dehydrogenase in and out of the pyruvate dehydrogenase complex from Azotobacter vinelandii\nPartial amino acid sequence of pig heart lipoamide dehydrogenase\nThe amino acid sequence encompassing the active site histidine residue of lipoamide dehydrogenase from Escherichia coli labelled with a bifunctional arsenoxide\nInactivation of pig heart lipoamide dehydrogenase by 1,3-dibromoacetone\nThe evolution of mercuric reductase, and a redox transfer model for mercuric ion detoxification in bacteria\nStructural studies on ferredoxin-NADP+ oxidoreductase from Spirulina, a blue-green alga\nThe amino acid sequence and partial tertiary structure of ferredoxin-NADP+ oxidoreductase from spinach\nOn the nature of ferredoxin: ferredoxin-NADP+ reductase complex\nProperties of a cross-linked complex between ferredoxin-NADP+ reductase and ferredoxin\nOn the enigma of old yellow enzyme\'s spectral properties\n\"On the enigma of old yellow enzyme\'s spectral properties\"\nNMR studies on the old yellow enzyme\nStructural and kinetic characteristics of dimethylglycine dehydrogenase and sarcosine dehydrogenase\nEvidence for two spatially distinct domains on each subunit of methylenetetrahydrofolate reductase\nStructure of NADH-cytochrome b5 reductase of human erythrocytes\nStructural comparison of the succinate dehydrogenase and fumarate reductase of Escherichia coli\nLack of assembly of succinate and NADH-ubiquinone oxidoreductases in iron-deficient rat skeletal muscle mitochondria\nCrystal structure study of trimethylamine dehydrogenase\nThe flavin domain of assimilatory NADH: nitrate reductase from Chlorella vulgaris\nPolarized absorption spectra of flavocytochrome b2 single crystals\nFMN-protein interactions in flavodoxin from A. nidulans\nPhotochemical formation of a stable red derivative of flavodoxin\nDesulfovibrio vulgaris flavodoxin. A 13C and 15N NMR investigation\n13C-NMR study on the interaction of riboflavin with riboflavin-binding protein\nThe structure of glycolate oxidase from spinach\nENDOR studies of flavoproteins\nResonance Raman study on the complexes of D-amino acid oxidase\nThe role of arginines in D-amino acid oxidase\nThe effect of the methylation of histidine-217 in pig kidney D-amino acid oxidase on ligand binding and on catalysis\nStoichiometry of the self-association of D-amino acid oxidase\n31P NMR and chemical studies on the phosphorus residues in milk xanthine oxidase\nSpecific modification of NAD+ binding site of chicken liver xanthine oxidase with 5\' - p - fluoro - sulphonylbenzoyladenosine\nStudies by electron paramagnetic resonance spectroscopy of the environment of the metal in the molybdenum cofactor from xanthine oxidase\nCoupling between Mo(V) and reduced Fe/S 1 centres in aldehyde oxidase and xanthine oxidase\nPartial amino acid sequence of L - lactate oxidase from M. smegmatis\nChemical modification of sulphydryl groups in p - hydroxybenzoate hydroxylase from Pseudomonas fluorescens\nChemical modification of phenol hydroxylase by p-nitrobenzenes ulphonyl fluoride\nStudies of 2,5-diketocamphane monooxygenase from Pseudomonas putida ATCC 17453\nRecent progress in bioluminescence: cloning of the structural genes encoding bacterial luciferase, analysis of the encoded sequences, and crystallization of the enzyme\nProbing the bacterial luciferase aldehyde site by affinity and photoaffinity labeling\nThe catalytic turnover of bacterial luciferase produces a quasi-stable species of altered conformation\nElectron microscopy and X-ray diffraction studies on heavy riboflavin synthase from Bacillus subtilis\nHeavy riboflavin synthase from Bacillus subtilis. Primary structure and reaggregation of the B subunits\nEnzyme Reaction Mechanisms\nMechanism of α,β-dehydrogenation of fatty acid CoA derivatives by flavin enzymes\nButyryl-CoA dehydrogenase: Aspects of acceptor and substrate specificity\nOxygen reactivity of butyryl-CoA dehydrogenase from Megasphaera elsdenii and from ox liver mitochondria\nSuicide inactivation of short-chain acyl-CoA dehydrogenases by propionyl-CoA. Formation of a substrate - flavin adduct\nStructure of the flavin N-5 adduct free radical obtained following inhibition of short-chain acyl-CoA dehydrogenase by propionyl-CoA\nPurification and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria\nMechanism of action of short-chain, medium-chain and long-chain acyl-CoA dehydrogenases isolated from rat liver\nInactivation of pig kidney general acyl-CoA dehydrogenase by 2-alkynoyl-CoA derivatives\nOn the inactivation of general acyl-CoA dehydrogenase from pig kidney by methylenecyclopropyl-acetyl-CoA, a metabolite of hypoglycin\nStructure-function correlation in B-oxidation enzymes\nPurification and characterization of glutaryl-CoA dehydrogenase, electron transfer flavoprotein and ETF-CoQ oxidoreductase from Paracoccus denitrificans\nReactions of ETF and ETF-CoQ oxidoreductase\nCorrelation between redox state of ETF and dehydrogenation of octanoyl-CoA\nSome observations on an acrylyl-CoA reductase from Clostridium kluyveri and an NADH-dependent fumarate reductase from Enterobacter agglomerans\nCharacterization of the mode of electron transport of NADPH-adrenodoxin reductase\nStudies on forward and reverse reactions of adrenodoxin reductase by electronic and NMR spectroscopy\nTransient kinetics of ferredoxin-NADP+ reductase reaction\nSome new ideas about the possible regulation of redox potentials in flavoprotein, with special reference to flavodoxins\nMethylenetetrahydrofolate reductase: an imperfect enzyme?\nProbing the catalytic mechanism of glutathione reductase with 2,4,6-trinitrobenzenesulphonate\nMultifunctionality of yeast glutathione reductase\nThe reaction between NADPH and mercuric reductase\nDehydrohalogenation and intermolecular hydrogen transfer reactions catalyzed by some lactate-oxidizing enzymes\nOn the mechanism of inactivation of flavocytochrome b2 (baker\'s yeast) by acetylenic substrates\nIntermolecular hydrogen transfer during transhydrogenation catalysed by flavocytochrome b2 and lactate oxidase\nProduct binding as modulator of flavin redox parameters: a mechanism of activity control in dehydrogenase-e-transferase?\nT-jump investigation of intramolecular electron exchanges in Hansenula anomala yeast flavocytochrome b2, L-lactate-cytochrome c oxidoreductase\nA pulse radiolysis study of flavocytochrome b2: differences in reactivity with carboxylate radicals between flavin and haem b2\nThe distribution of reducing equivalents among some species in succinate dehydrogenase upon reduction by succinate\nIonic species of the flavin and the catalytic cycle of succinate dehydrogenase\nESR spectroscopic studies of succinate dehydrogenase and fumarate reductase from Escherichia coli\nFumarate reductase from Escherichia coli requires the frdC and frdD gene products for quinone reductase activity\nGlutamate synthase from Azospirillum brasilense\nOxidation-reduction properties of glycolate oxidase\nStudies with the flavin-dependent alcohol oxidase from yeast: properties and catalytic mechanism\nPulse radiolysis studies on the formation and decay of the flavin 4a-hydroperoxide species of glucose oxidase\nE.coli pyruvate oxidase: a hysteretic enzyme\nMechanism and functionality of FMN in liver pyridoxine (pyridoxamine) 5\'-phosphate oxidase\nEnzymatic properties of yeast pyridoxamine-P oxidase\nA photo-labelling reagent of brain pyridoxine-5-P oxidase\nNon-stereospecific reduction of monoamine oxidase from bovine liver by analogs of amphetamine\nThe kinetics of NADPH-dependent reduction of FAD and cytochrome b in a solubilised preparation of the superoxide generating oxidase of neutrophils\nFlavoprotein monooxygenases\nThe nature of the 4a-hydroperoxyflavin in the mammalian flavin-containing monooxygenase\nThe effect of pH and ionic strength on the binding of NADPH and NADPH analogues to p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens: the importance of monopole-monopole and monopole-dipole interactions\nKinetic mechanism of the reductive half of reaction catalysed by sailcylate hydroxylase\nThe pH dependence of enzyme-phenol complexes of phenol hydroxylase\nDifferential induction and characterization of flavoprotein hydroxylases in Pseudomonas cepacia\nSteroid monoxygenase from Cylindrocarpon radicicola. An FAD-containing Baeyer-Villiger type oxygenase\nUnusual properties of the flavocytochrome p-cresol methylhydroxylase\nIdentification of the luciferase-bound flavin-4a-hydroxide as the primary emitter in the bacterial bioluminescenee reaction\nStudies on the bacterial luciferase reaction: isotope effects on the light emission. Is a \"CIEEL\" mechanism involved?\nProbes for the active site of bacterial luciferase\nThe cellobiose oxidoreductases of Sporotrichum pulverulentum\nThe equilibration of reducing equivalents within milk xanthine oxidiase\nReactions between xanthine oxidase and 4-hydroxy-7-azapteridine\n“Type 1” and “Type 2” rapid and slow EPR signals from the molybdenum centres of molybdenum-containing hydroxylases and their significance\nRe-sulphuration of xanthine oxidase\nReactivation of desulpho-xanthine oxidase by an enzymatic system\nThe existence of desulpho-xanthine dehydrogenase in rat liver\nThe structures and catalytic mechanisms of molybdenum centres in enzymes studied by e.p.r and X-ray spectroscopy\nBiochemistry of naturally-occurring deazaflavin coenzymes\nInteraction of the herbicide sulfometuron methyl with acetolactate synthase: a slow-binding inhibitor\nThe rate-determining step in pteridine-dependent monooxygenases is not ring cleavage\nThe one-electron reduction of riboflavin-binding protein\nModified Flavins in Flavoproteins\n8-azidoflavins: photoaffinity labels for flavoproteins\nGlutathione reductase species containing FAD analogues\nFlavin analogue studies of pig kidney electron transferring flavoprotein\nChemically modified flavins as probes of phenol hydroxylase structure and function\n4-thioflavins as active site probes of flavoproteins: reaction with sulphite and formation of 4-hydroxy-4-sulphonylflavins\nOxygen reactivity of 4-thio-FAD p-hydroxybenzoate hydroxylase\nOxygen reactions of para-hydroxy benzoate hydroxylase containing 6-hydroxy-FAD\nThe effect of pH and modifications in position 8 on the oxidation of reduced p-hydroxybenzoate hydroxylase\nReaction of bacterial luciferase from Vibrio harveyi with 8-substituted flavins\nBiomedical Aspects\nIntestinal absorption of riboflavin\nTransfer of hydrogen atoms from pentose phosphate to the xylene ring of riboflavin\nBiosynthesis of riboflavin Enzymatic formation of 6,7-dimethyl-8-ribityllumazine\nCell-free biosynthesis of lipoamide dehydrogenase\nCovalently 14C-riboflavin-labeled proteins in Arthrobacter oxidans and their possible relationship to 6-hydroxy-D-nicotine oxidase\nElectron immunochemical localization of 6-hydroxy-nicotine oxidases in Arthrobacter oxidans\nCloning in Escherichia coli of the 6-hydroxy-D-nicotine oxidase gene from Arthrobacter oxidans\nHydroxylation of riboflavin 7- and 8-methyl groups in mammals\nMammalian metabolism of flavins\nFlavoenzymes as drug targets\nStudies on Esherichia coli photolyase: role of flavin in DNA repair\nElectron transfer to nitrogenase in K-pneumoniae nifF gene cloned and the gene product, a flavodoxin, purified and partially characterised\nPractical Applications of Flavoprotein Studies\nIn vitro synthesis of (bio)chemicals using flavin-containing enzymes\nFlavin cofactors covalently attached to electron-conducting supports: electrochemical and enzyme activity\nLuminometric determination of immunoadsorbed flavoproteins and of flavin adenine dinucleotide\nFlavins as labels in immunoassays: I. Design and synthesis of flavin labels\nFlavins as labels in immunoassays: II. Properties of flavin labels and their use in immunoassay\nAuthor Index\nSubject Index