Kunio Yagi 
Flavins and Flavoproteins 1993 [PDF ebook] 
Proceedings of the Eleventh International Symposium, Nagoya, Japan, July 27–31, 1993

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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 rib A CODING FOR GTP CYCLOHYDROLASE II AND rib C 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 spec

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Limba Engleză ● Format PDF ● Pagini 909 ● ISBN 9783110885774 ● Mărime fișier 189.3 MB ● Editor Kunio Yagi ● Editura De Gruyter ● Oraș Berlin/Boston ● Publicat 2020 ● Ediție 1 ● Descărcabil 24 luni ● Valută EUR ● ID 7913814 ● Protecție împotriva copiilor Adobe DRM
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