Vincent Massey

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Scope and limitation of single electron transfer in biology

Peter Hemmerich, Vincent Massey, Heinrich Michel, Christian Schug

Structure and Bonding > Biochemistry > 93-123

This article is thought to be a supplement to an earlier one “Mechanism of Hydrogen Transfer in Redox Enzymes”³³). Most of the basic concepts and hypotheses put forward then, are still valid. Substantial new evidence supporting our views has been advanced since then. The new data presented here concern modified or as we call them “mutilated flavins”, namely 5-deaza- and 5-thiaflavin, which upon incorporation...

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Use of 8-Substituted-FAD Analogues To Investigate the Hydroxylation Mechanism of the Flavoprotein 2-Methyl-3-hydroxypyridine-5-carboxylic Acid Oxygenase ^† ^, ^‡

Pimchai Chaiyen, Jeerus Sucharitakul, Jisnuson Svasti, Barrie Entsch, more

Biochemistry > 2004 > 43 > 13 > 3933 - 3943

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Studies of the Mechanism of Phenol Hydroxylase: Effect of Mutation of Proline 364 to Serine ^†

Dong Xu, Cristofer Enroth, Ylva Lindqvist, David P. Ballou, more

Biochemistry > 2002 > 41 > 46 > 13627 - 13636

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The reactivity of oxygen with flavoproteins

Vincent Massey

International Congress Series > 2002 > 1233 > Complete > 3-11

The ways in which various flavoproteins modulate the reactivity of the reduced flavin with molecular oxygen constitute a major unsolved problem in the field. The contributions of redox potentials, both of the flavin and the O ₂ /O ₂ ^- couple, their dependence on the protein environment surrounding the flavin, and the possibility of control through multi-step access of oxygen to...

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Function of two arginine residues of l-lactate oxidase

Kazuko Yorita, Hideo Misaki, Mitsuru Matsumoto, Vincent Massey

International Congress Series > 2002 > 1233 > Complete > 69-75

Two arginine residues, Arg-181 and Arg-268, at the active site of l-lactate oxidase from Aerococcus viridans were targeted for site-directed mutagenesis for analyzing the mechanism of the reductive half-reaction by substrate α-hydroxyacids. Replacement of either Arg-181 or Arg-268 by Lys resulted in significant slowing of reduction by l-lactate but had little effect on the reoxidation rate by oxygen...

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Studies of the Mechanism of Phenol Hydroxylase: Mutants Tyr289Phe, Asp54Asn, and Arg281Met ^†

Dong Xu, David P. Ballou, Vincent Massey

Biochemistry > 2001 > 40 > 41 > 12369 - 12378

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Mechanistic Studies of Cyclohexanone Monooxygenase: Chemical Properties of Intermediates Involved in Catalysis ^†

Dawei Sheng, David P. Ballou, Vincent Massey

Biochemistry > 2001 > 40 > 37 > 11156 - 11167

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Synergistic Interactions of Multiple Mutations on Catalysis during the Hydroxylation Reaction of p -Hydroxybenzoate Hydroxylase: Studies of the Lys297Met, Asn300Asp, and Tyr385Phe Mutants Reconstituted with 8-Cl-Flavin ^†

Mariliz Ortiz-Maldonado, Sara M. Aeschliman, David P. Ballou, Vincent Massey

Biochemistry > 2001 > 40 > 30 > 8705 - 8716

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A Rate-Limiting Conformational Change of the Flavin in p -Hydroxybenzoate Hydroxylase Is Necessary for Ligand Exchange and Catalysis: Studies with 8-Mercapto- and 8-Hydroxy-Flavins ^†

Mariliz Ortiz-Maldonado, David P. Ballou, Vincent Massey

Biochemistry > 2001 > 40 > 4 > 1091 - 1101

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Primary Structure of the Snake Venom L-Amino Acid Oxidase Shows High Homology with the Mouse B Cell Interleukin 4-InducedFig1Protein

Andrei A. Raibekas, Vincent Massey

Biochemical and Biophysical Research Communications > 1998 > 248 > 3 > 476-478

The 2.8-kb sequence of cDNA encoding southeastern diamondback rattlesnake venom L-amino acid oxidase was determined. A translated single open reading frame revealed a 58.7-kDa polypeptide containing a signal sequence and FAD binding motif. The protein similarity search and analysis showed that the snake L-amino acid oxidase possesses the highest degree of homology (37% of identity) with a protein...

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Peroxide Reductase Activity of NADH Dehydrogenase of an AlkaliphilicBacillusin the Presence of a 22-kDa Protein Component fromAmphibacillus xylanus

Noriyuki Koyama, Tsutomu Koitabashi, Youichi Niimura, Vincent Massey

Biochemical and Biophysical Research Communications > 1998 > 247 > 3 > 659-662

The NADH oxidase ofAmphibacillus xylanusshows high NADH-peroxide reductase activity for hydrogen peroxide and alkyl hydroperoxides in the presence of a 22-kDa disulfide-containing protein component (Y. Niimura, L. B. Poole, and V. Massey,J.Biol.Chem.270, 25645–25650, 1995). It was found that the membrane-bound NADH dehydrogenase of an alkaliphilicBacillus(YN-1) involved in the respiratory chain also...

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Purification and characterization of Sporolactobacillus inulinus NADH oxidase and its physiological role in aerobic metabolism of the bacterium

Yoshitaka Nishiyama, Vincent Massey, Yukiko Anzai, Toshihiro Watanabe, more

Journal of Fermentation and Bioengineering > 1997 > 84 > 1 > 22-27

NADH oxidase was purified to homogeneity from aerobic cells of Sporolactobacillus inulinus. The N-terminal amino acid sequence showed high similarity to those of the NADH oxidase from Amphibacillus xylanus and the H ₂ O ₂ -forming NADH oxidase from Streptococcus mutans. S. inulinus NADH oxidase is a homodimer composed of subunits and with a molecular mass of 53 kDa. It catalyzes the...

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Search results for: Vincent Massey

Scope and limitation of single electron transfer in biology

Use of 8-Substituted-FAD Analogues To Investigate the Hydroxylation Mechanism of the Flavoprotein 2-Methyl-3-hydroxypyridine-5-carboxylic Acid Oxygenase ^† ^, ^‡

Studies of the Mechanism of Phenol Hydroxylase: Effect of Mutation of Proline 364 to Serine ^†

The reactivity of oxygen with flavoproteins

Function of two arginine residues of l-lactate oxidase

Studies of the Mechanism of Phenol Hydroxylase: Mutants Tyr289Phe, Asp54Asn, and Arg281Met ^†

Mechanistic Studies of Cyclohexanone Monooxygenase: Chemical Properties of Intermediates Involved in Catalysis ^†

Synergistic Interactions of Multiple Mutations on Catalysis during the Hydroxylation Reaction of p -Hydroxybenzoate Hydroxylase: Studies of the Lys297Met, Asn300Asp, and Tyr385Phe Mutants Reconstituted with 8-Cl-Flavin ^†

A Rate-Limiting Conformational Change of the Flavin in p -Hydroxybenzoate Hydroxylase Is Necessary for Ligand Exchange and Catalysis: Studies with 8-Mercapto- and 8-Hydroxy-Flavins ^†

Primary Structure of the Snake Venom L-Amino Acid Oxidase Shows High Homology with the Mouse B Cell Interleukin 4-InducedFig1Protein

Peroxide Reductase Activity of NADH Dehydrogenase of an AlkaliphilicBacillusin the Presence of a 22-kDa Protein Component fromAmphibacillus xylanus

Purification and characterization of Sporolactobacillus inulinus NADH oxidase and its physiological role in aerobic metabolism of the bacterium

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