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_a9783110109504 _qprint |
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_a9783110884715 _qPDF |
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_a10.1515/9783110884715 _2doi |
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| 035 | _a(DE-B1597)9783110884715 | ||
| 035 | _a(DE-B1597)53971 | ||
| 035 | _a(OCoLC)1105851472 | ||
| 040 |
_aDE-B1597 _beng _cDE-B1597 _erda |
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| 072 | 7 |
_aSCI000000 _2bisacsh |
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| 084 | _aonline - DeGruyter | ||
| 245 | 0 | 0 |
_aFlavins and Flavoproteins 1987 : _bProceedings of the Ninth International Symposium, Atlanta, Georgia, USA, June 7–12, 1987 / _ced. by D. E. Edmondson, D. B. McCormick. |
| 250 | _aReprint 2019 | ||
| 264 | 1 |
_aBerlin ; _aBoston : _bDe Gruyter, _c[2019] |
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| 264 | 4 | _c©1987 | |
| 300 |
_a1 online resource (XXIII, 775 p.) : _bNum. figs. |
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| 336 |
_atext _btxt _2rdacontent |
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| 337 |
_acomputer _bc _2rdamedia |
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| 338 |
_aonline resource _bcr _2rdacarrier |
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_atext file _bPDF _2rda |
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_tFrontmatter -- _tPreface -- _tOrganizing committee -- _tAcknowledgements -- _tContents -- _tSTRUCTURE AND MECHANISMS OF FLAVOENZYMES -- _tAbsolute stereochemistry of flavins in enzyme - catalyzed reactions -- _tConserved cysteine pairs of mercuric ion reductase: an investigation of function via site-directed mutagenesis -- _tReduced forms of native mercuric reductase and their reactions with mercuric compounds - activity vs inhibition -- _tRapid-scan stopped-flow studies of the flavoenzyme mercuric reductase during catalytic turnover -- _tThe penultimate cysteines in mercuric reductase aid in the reduction of mercury -- _tThe active center of glutathione reductase at 1.54 A resolution -- _tKinetic isotope effect studies on yeast, spinach and human erythrocyte glutathione reductases -- _tExcited electronic states of flavin-containing coenzyme models -- _tTrypanothione reductase from Trypanosoma cruzi -- _tInactivation of two-electron reduced Escherichia coll glutathione reductase by NADPH and NADH -- _tStudies on the active site of human erythrocyte glutathione reductase using 6-SCN-FAD and 6-mercapto - FAD -- _tProtein engineering of glutathione reductase from Escherichia coli -- _tStudies on the active sites of lipoamide dehydrogenase and glutathione reductase -- _tCloning, organisation and nucleotide sequence of the Azotobacter vinelandii gene for lipoamide dehydrogenase -- _tReaction of pig heart lipoamide dehydrogenase with monobromoacetone and 1,3-dibromoacetone -- _tSite-directed mutagenesis of thioredoxin reductase -- _tEffects of urea on redox properties of streptococcal NADH peroxidase -- _tThree dimensional structure of baker's yeast flavocytochrome b2 -- _tMechanism of L-lactate dehydrogenation catalyzed by flavocytochrome b.2 from baker's yeast -- _tInactivation of yeast flavocytochrone b.2 with fluoropyruvate. Modification of the active site histidine -- _tEvidence for an alteration of the flavin behavior induced by 2-methyl - 2,4 - pentandiol in cerevis iae flavocytochrome b2 -- _tMedium chain acyl-CoA dehydrogenase from pig kidney: Aspects of the reductive half - reaction -- _tCrystal structure of the general acyl-CoA dehydrogenase -- _tInactivation 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 -- _t2 - Bromo-octanoyl CoA: Apseudo-substrateforgeneral acyl-CoA dehydrogenase -- _tReaction of pig kidney medium chain acyl-CoA dehydrogenase with ^ - oxidation intermediates -- _tMedium chain acyl-CoA dehydrogenase from pig kidney: I n activation of the reduced enzyme by 2-octynoy1-CoA -- _tOxidation - reduction of general acyl-CoA dehydrogenase by the butyryl-CoA / crotonyl-CoA couple. A new investigation of the rapid reaction kinetics -- _tCatalytic versatility of butyryl-CoA dehydrogenase from M. elsdenii -- _tOxidation-reduction potential of glutaryl-CoA dehydrogenase from Paracoccus denitrifleans -- _t13C NMR studies on the complexes and reaction intermediates of D-amino acid oxidase -- _t13C-,15N-, and 31P- NMR studies on 6-hydroxy-L-nicotine oxidase from Arthrobacter oxidans -- _tA study on the interaction between reduced D-amino acid oxidase and ligands -- _tD-Amino acid oxidase from the yeast Rhodotorula gracilis -- _tPurification and properties of D-aspartate oxidase from beef kidney -- _tSpectral and kinetic studies on Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating) -- _tTime - resolved flavin fluorescence of pyridoxine-5-P oxidase from sheep brain -- _tAn active site thiol in lactate oxidase -- _tCan methylenetetrahydrofolate reductase be used to evade the methyl trap? -- _tThe catalytic mechanism of DNA photolyase -- _tFLAVOENZYME STRUCTURE AND ELECTRON TRANSFER MECHANISMS -- _tSequence and structure of Anacvstis nidulans flavodoxin: Comparisons with flavodoxins from other species -- _tC-13, N-15, and two-dimensional NMR techniques in flavoprotein research -- _tTwo dimensional NMR studies on Megasphaera elsdenii -- _tFlavodoxin 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 -- _tPulse radiolysis studies on flavodoxin -- _tResonance raman investigations of flavins and flavoproteins -- _tSpectral studies on hydrogen bonded alloxazines -- _tUse of flavin and flavodoxin semiquinones as kinetic probes to elucidate the factors which determine reaction rate constants and biological specificity for electron transfer proteins -- _tFactors influencing the rate of electron transfer from flavodoxin to cytochrome c. -- _tA computer graphics model of the complex formed between flavodoxin and the tetraheme cytochrome c.3 -- _tCloning and nucleotide sequence of a bacterial flavodoxin gene: Towards the site-directed mutagenesis of the flavin binding site -- _tFlavin binding site differences between Photobacterium phosphoreum lumazine protein and Megasphaera elsdenii flavodoxin. An investigation using circular dichroism and fluorescence -- _tFerredoxin and ferredoxin-NADP+oxidoreductase interactions: Mapping of their binding sites -- _tComplex formation between ferredoxin-NADP+-oxidoreductase and flavodoxin -- _tMechanism of ferredoxin-NADP+ reductase reaction NADP radical, semiquinone and fully reduced enzyme-NADP+ charge transfer complex as the reaction intermediates -- _tIn vivo deactivation/activation of ferredoxin-NADP+- oxidoreductase from the cyanobacteria Anabaena variabills -- _tIsolation from Desulfovibrio desulfuricans of a flavoprotein with NADH-H+ oxidoreductase activity towards a protein containing a rubredoxin-like center -- _tMicrosomal electron transport system focused on NADPH-cytochrome P-450 reductase -- _tTime - resolved fluorescence spectroscopy on NADPH-cytochrome P-450 reductase -- _tStudies on the reactions of flavin- and nicotinamide nucleotide analogues with a bacterial electron-transferring flavoprotein -- _tKinetics of ligand binding, amino acid sequence, and crystallization of Chlorobium and Chromatium flavocytochrome c. -- _tRedox properties of flavocytochrome c. |
| 505 | 0 | 0 |
_t-- _tElectron transfer kinetics of phthalate oxygenase reductase, an iron sulfur center containing flavoprotein -- _tCD and potentiometry of the FAD of nitrate reductase -- _tKinetic studies on glutamate synthase from Azospirillum bras ilense -- _tRedox interactions of the FAD in xanthine oxidase with other centers of the protein -- _tLaser flash photolysis studies of intramolecular electron transfer between the FAD and Fe/S II centers in xanthine oxidase -- _tMechanism of action of chicken liver xanthine dehydrogenase -- _tInterconversion between O-dependent and NAD - dependent types of rat liver xanthine dehydrogenase -- _tReactivity of chicken liver xanthine dehydrogenase containing artificial flavins -- _tThe molybdenum cofactor of milk xanthine oxidase -- _tIsolation of a cDNA sequence coding for a part of xanthine dehydrogenase from rat liver -- _tFLAVIN BIOSYNTHESIS/ METABOLISM/ AND MEDICAL ASPECTS -- _tBiosynthesis of flavins and deazaflavins -- _tThe icosahedral ß60 capsid of heavy riboflavin synthase (6,7- dimethyl-8-ribityllumazine synthase/riboflavin synthase) -- _tCharacterization of human riboflavin-binding immunoglobulins -- _tRiboflavin uptake by isolated rat kidney cells -- _tPurification and characterization of the bifunctional enzyme FAD synthetase from Brevibacterium ammoniapenes -- _tAn update on flavin metabolism in rats and humans -- _tEffects of quinacrine, tetracycline, adriamycin and chloroquine upon flavin metabolism in rats -- _tRole of flavoproteins in the neurotoxic action of MPTP -- _tBiosynthesis of flavoproteins -- _tBiological and Medical Aspects of D-Amino Acid Oxidase — Biogenesis and in vivo reaction with D-propargylglycine — -- _tMolecular and cellular biology of D-amino acid oxidase -- _tLocalization of D-amino acid oxidase in rat cerebellum -- _tBiosynthesis of D-amino acid oxidase and molecular cloning of the cDNA -- _tCharacterization of a partially purified nitroaryl reductase -- _tFLAVOENZYME HYDROXYLASES -- _tCrystallographic studies on the mechanism of hydroxybenzoate hydroxylase from Psudomonas fluorescens -- _tApplications of deuterium and tritium isotope effects to the elucidation of kinetic mechanisms of flavoprotein hydroxylases -- _tChemical modification of tyrosine-38 in j>.-hydroxybenzoate hydroxylase from Pseudomonas fluorescens by 5'-Pfluorosulfonylbenzoyladenosine: A probe for the elucidation of the NADPH binding site? -- _tPhenol Complexes of Phenol Hydroxylase -- _tThe involvement of SH-groups in cooperativity of phenol binding sites in phenol hydroxylase -- _t6-Thiocyanate-FAD and 6-mercapto-FAD as active site probes of phenol hydroxylase -- _tHysteretic behavior of anthranilate hydroxylase -- _tRedox potentials of salicylate hydroxylase -- _tThe oxidative half-reaction of 2-methyl-3-hydroxypyridine-5 - carboxylic acid oxygenase from Pseudomonas sp. MA-1 -- _tLipid stabilization of the flavin hydroperoxide in the microsomal flavin-containing monooxygenase -- _tFLAVIN-DEPENDENT BIOLUMINESCENCE -- _tOne-electron transfers in flavin systems: Relevance to the postulated C1EEL mechanism in bacterial bioluminescence -- _tCharacterization of new "bleached" products obtained on treating flavins and flavoproteins with dithionite -- _tFlavin-mediated hydrogen peroxide production by biological and chemical photosystems -- _tOn the chemical mechanisms of bacterial luciferase, an updating -- _tStudies on the mechanism of bacterial bioluminescence. Evidence compatible with a one electron transfer process and a CIEEL mechanism in the luciferase reaction -- _tStructural analysis of bacterial luciferase -- _tSequence similarity between the a subunit of luciferase from Vibrio harvevl and clostridial flavodoxin -- _tIsolation and characterization of a yellow fluorescent protein from Vibrio fischeri strain Y-1 -- _tPurification and characterization of an unusual nonfluores cent flavoprotein from Photobacterium leiognathi -- _tPurification and some properties of FP390 from P. phosphoreum -- _tSTRUCTURE, MECHANISM, AND BIOSYNTHESIS OF FLAVOENZYMES CONTAINING COVALENTLY-BOUND FLAVINS -- _t8α-Imidazolylflavins: Application of their redox and spectral properties to flavoenzyme systems -- _tX-ray study of flavoenzymes containing covalently bound flavins -- _tStructural studies of P-cresol methylhydroxylase -- _tThe chemical and stereochemical course of oxidation of 4- ethylphenol and other 4-alkylphenols by ^-cresol methylhydroxylase -- _tRedox properties of trimethylamine dehydrogenase -- _tRedox properties of Escherichia coll fumarate reductase -- _tReactions of lumiflavin with aminyl and a-amino radicals of piperazine -- _tKinetic probes of the proposed radical mechanism of monoamine oxidase -- _tStopped-flow studies on the mechanism of the oxidation of N—methyl - 4 - phenyl - 1 , 2 , 3 , 6 - tetrahydropyridine (HPTP) by monoamine oxidase -- _tMethoxatin containing methylamine dehydrogenase: Enzyme reduction by primary amines -- _tInteraction of bacterial sarcosine oxidase with folate derivatives -- _tSulfhydryl groups and the binding site of noncovalently bound FAD ofCorvnebacterlum sarcosine oxidase -- _tDimethylglycine dehydrogenase from pig liver mitochondria: Purification and properties -- _tComparison 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 -- _tCovalent binding of FAD to Bacillus subtllis succinate dehydrogenase -- _t6 - Hydroxy-D-nicotine oxidase: Expression of the flavoenzyme as a covalently flavinylated polypeptide -- _tThe flavin-binding sites of 6-hydroxy-D- and 6-hydroxy-Lnicotine oxidase -- _tLIST OF PARTICIPANTS -- _tAUTHOR INDEX -- _tSUBJECT INDEX -- _tBackmatter |
| 506 | 0 |
_arestricted access _uhttp://purl.org/coar/access_right/c_16ec _fonline access with authorization _2star |
|
| 538 | _aMode of access: Internet via World Wide Web. | ||
| 546 | _aIn English. | ||
| 588 | 0 | _aDescription based on online resource; title from PDF title page (publisher's Web site, viewed 30. Aug 2021) | |
| 650 | 4 | _aFlavine. | |
| 650 | 4 | _aFlavoenzym. | |
| 650 | 7 |
_aSCIENCE / General. _2bisacsh |
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_aAckrell, Brian A. C. _eautore |
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| 700 | 1 |
_aMerrill, A. H. _eautore |
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| 700 | 1 |
_aMeyer, T. E. _eautore |
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| 700 | 1 |
_aMeyer, Terrance E. _eautore |
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| 700 | 1 |
_aMierlo, Carlo P.M. van _eautore |
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| 700 | 1 |
_aMierlo, Carlo van _eautore |
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| 700 | 1 |
_aMiiller, Franz _eautore |
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| 700 | 1 |
_aMiller, S. M. _eautore |
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| 700 | 1 |
_aMiura, R. _eautore |
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| 700 | 1 |
_aMiyake, Y. _eautore |
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| 700 | 1 |
_aMiyake, Yoshihiro _eautore |
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| 700 | 1 |
_aMomoi, Kyoko _eautore |
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| 700 | 1 |
_aMoore, M. _eautore |
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| 700 | 1 |
_aMoore, Melissa J. _eautore |
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| 700 | 1 |
_aMoura, I. _eautore |
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| 700 | 1 |
_aMoura, J. J. G. _eautore |
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| 700 | 1 |
_aMuller, F. _eautore |
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| 700 | 1 |
_aMurata, M. _eautore |
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| 700 | 1 |
_aMüller, Franz _eautore |
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| 700 | 1 |
_aNagata, T. _eautore |
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| 700 | 1 |
_aNagursky, Heiner _eautore |
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| 700 | 1 |
_aNakamura, Makoto _eautore |
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| 700 | 1 |
_aNakamura, Takao _eautore |
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| 700 | 1 |
_aNegri, Armando _eautore |
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| 700 | 1 |
_aNeujahr, Haiina Y. _eautore |
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| 700 | 1 |
_aNeujahr, Halina Y. _eautore |
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| 700 | 1 |
_aNishikimi, Morimitsu _eautore |
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| 700 | 1 |
_aNishina, Yasuzo _eautore |
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| 700 | 1 |
_aNishino, T. _eautore |
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| 700 | 1 |
_aNishino, Takeshi _eautore |
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| 700 | 1 |
_aNishino, Tomoko _eautore |
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| 700 | 1 |
_aNishiyama, Kyoko _eautore |
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| 700 | 1 |
_aNisimoto, Y. _eautore |
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| 700 | 1 |
_aNitta, Satoshi _eautore |
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| 700 | 1 |
_aNozaki, Mitsuhiro _eautore |
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| 700 | 1 |
_aOhishi, Nobuko _eautore |
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| 700 | 1 |
_aOhnishi, Norihiro _eautore |
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| 700 | 1 |
_aOka, M. _eautore |
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| 700 | 1 |
_aOzawa, Takayuki _eautore |
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| 700 | 1 |
_aO’Kane, D. J. _eautore |
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| 700 | 1 |
_aO’Kane, Dennis J. _eautore |
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| 700 | 1 |
_aO’Nuallain, Eoin M. _eautore |
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| 700 | 1 |
_aPai, E. F. _eautore |
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| 700 | 1 |
_aPai, Emil F. _eautore |
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| 700 | 1 |
_aPattridge, Katherine A. _eautore |
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| 700 | 1 |
_aPeck, H. D. _eautore |
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| 700 | 1 |
_aPerham, R. N. _eautore |
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| 700 | 1 |
_aPinto, J. T. _eautore |
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| 700 | 1 |
_aPollegioni, L. _eautore |
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| 700 | 1 |
_aPoole, Leslie B. _eautore |
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| 700 | 1 |
_aPoulsen, L. L. _eautore |
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| 700 | 1 |
_aPowell, John _eautore |
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| 700 | 1 |
_aPowell, P. J. _eautore |
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| 700 | 1 |
_aPowlowski, Justin _eautore |
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| 700 | 1 |
_aProngay, Andrew J. _eautore |
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| 700 | 1 |
_aPueyo, J. J. _eautore |
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| 700 | 1 |
_aPust, Stefan _eautore |
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| 700 | 1 |
_aRamsay, Rona R. _eautore |
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| 700 | 1 |
_aRao, K. K. _eautore |
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| 700 | 1 |
_aRatti, S. _eautore |
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| 700 | 1 |
_aRayment, I. _eautore |
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| 700 | 1 |
_aRivlin, R. S. _eautore |
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| 700 | 1 |
_aRonchi, S. _eautore |
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| 700 | 1 |
_aSahlman, Lena _eautore |
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| 700 | 1 |
_aSaint-Martin, P. _eautore |
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| 700 | 1 |
_aSaito, T. _eautore |
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| 700 | 1 |
_aSancho, J. _eautore |
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| 700 | 1 |
_aSandström, A. _eautore |
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| 700 | 1 |
_aSchirmer, R. H. _eautore |
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| 700 | 1 |
_aSchneider, Monika _eautore |
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| 700 | 1 |
_aSchopfer, Lawrence M. _eautore |
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| 700 | 1 |
_aSchott, Karin _eautore |
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| 700 | 1 |
_aSchreuder, Herman A. _eautore |
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| 700 | 1 |
_aSchulz, G. E. _eautore |
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| 700 | 1 |
_aSchulz, Georg E. _eautore |
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| 700 | 1 |
_aSchwarzkopf, Bruno _eautore |
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| 700 | 1 |
_aSchweitzer, D. _eautore |
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| 700 | 1 |
_aSchöllhammer, T. _eautore |
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| 700 | 1 |
_aScrutton, N. S. _eautore |
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| 700 | 1 |
_aSejlitz, Torsten _eautore |
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| 700 | 1 |
_aShibata, Toshihiro _eautore |
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| 700 | 1 |
_aShiga, Kiyoshi _eautore |
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| 700 | 1 |
_aSimonetta, M. Pilone _eautore |
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| 700 | 1 |
_aSinger, T. P. _eautore |
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| 700 | 1 |
_aSinger, Thomas P. _eautore |
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| 700 | 1 |
_aSolomonson, L. P. _eautore |
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| 700 | 1 |
_aStaab, H. A. _eautore |
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| 700 | 1 |
_aStankovich, M. T. _eautore |
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| 700 | 1 |
_aStankovich, Marian T. _eautore |
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| 700 | 1 |
_aSteenkamp, D. J. _eautore |
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| 700 | 1 |
_aStewart, D. E. _eautore |
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| 700 | 1 |
_aStockman, Brian J. _eautore |
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| 700 | 1 |
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| 700 | 1 |
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| 700 | 1 |
_aSurdhar, P. S. _eautore |
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| 700 | 1 |
_aSuzuki, H. _eautore |
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| 700 | 1 |
_aSuzuki, Haruo _eautore |
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| 700 | 1 |
_aSwarte, Myra B. A. _eautore |
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| 700 | 1 |
_aSwenson, Richard P. _eautore |
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| 700 | 1 |
_aSzafran, M. M. _eautore |
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| 700 | 1 |
_aTakeshima, Katsuhito _eautore |
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| 700 | 1 |
_aTaylor, K. L. _eautore |
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| 700 | 1 |
_aTaylor, M. G. _eautore |
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| 700 | 1 |
_aTegoni, M. _eautore |
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| 700 | 1 |
_aThorpe, C. _eautore |
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| 700 | 1 |
_aThorpe, Colin _eautore |
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| 700 | 1 |
_aThunnissen, Marjolein M. G. M. _eautore |
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| 700 | 1 |
_aTitlow, Christian _eautore |
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| 700 | 1 |
_aTojo, Hiroaasa _eautore |
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| 700 | 1 |
_aTojo, Hiromasa _eautore |
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| 700 | 1 |
_aTollin, Gordon _eautore |
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| 700 | 1 |
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| 700 | 1 |
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| 700 | 1 |
_aTsushima, Keizo _eautore |
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| 700 | 1 |
_aTu, S.-C. _eautore |
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| 700 | 1 |
_aTu, Shiao-Chun _eautore |
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| 700 | 1 |
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| 700 | 1 |
_aUrban, Philippe _eautore |
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| 700 | 1 |
_aUshijiaa, Hidetaka _eautore |
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| 700 | 1 |
_aUtterback, Margot _eautore |
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| 700 | 1 |
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| 700 | 1 |
_aVanin, Elio F. _eautore |
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| 700 | 1 |
_aVanoni, M. A. _eautore |
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| 700 | 1 |
_aVervoort, J. _eautore |
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| 700 | 1 |
_aVervoort, Jacques _eautore |
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| 700 | 1 |
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| 700 | 1 |
_aVisser, Antonie J.W. _eautore |
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| 700 | 1 |
_aVisser, Ton _eautore |
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| 700 | 1 |
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| 700 | 1 |
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| 700 | 1 |
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| 700 | 1 |
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| 700 | 1 |
_aWalsh, Christopher T. _eautore |
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| 700 | 1 |
_aWampler, J. E. _eautore |
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| 700 | 1 |
_aWang, L.-H. _eautore |
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| 700 | 1 |
_aWang, Lee-Ho _eautore |
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| 700 | 1 |
_aWatanabe, Fusao _eautore |
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| 700 | 1 |
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| 700 | 1 |
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| 700 | 1 |
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| 700 | 1 |
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| 700 | 1 |
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| 700 | 1 |
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| 700 | 1 |
_aWilliams, Charles H. _eautore |
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| 700 | 1 |
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| 700 | 1 |
_aWu, J. _eautore |
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| 700 | 1 |
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| 700 | 1 |
_aXia, Z. -x _eautore |
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| 700 | 1 |
_aYagi, Kunio _eautore |
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| 700 | 1 |
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| 700 | 1 |
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| 700 | 1 |
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| 700 | 1 |
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| 700 | 1 |
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| 700 | 1 |
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| 700 | 1 |
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| 700 | 1 |
_aZiegler, M. M. _eautore |
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| 700 | 1 |
_aZipplies, M. F. _eautore |
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| 850 | _aIT-RoAPU | ||
| 856 | 4 | 0 | _uhttps://doi.org/10.1515/9783110884715 |
| 856 | 4 | 0 | _uhttps://www.degruyter.com/isbn/9783110884715 |
| 856 | 4 | 2 |
_3Cover _uhttps://www.degruyter.com/cover/covers/9783110884715.jpg |
| 942 | _cEB | ||
| 999 |
_c248816 _d248816 |
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