Literature DB >> 3994664

Oxidation of NAD dimers by horseradish peroxidase.

L Avigliano, V Carelli, A Casini, A Finazzi-Agrò, F Liberatore.   

Abstract

Horseradish peroxidase catalyses the oxidation of NAD dimers, (NAD)2, to NAD+ in accordance with a reaction that is pH-dependent and requires 1 mol of O2 per 2 mol of (NAD)2. Horseradish peroxidase also catalyses the peroxidation of (NAD)2 to NAD+. In contrast, bacterial NADH peroxidase does not catalyse the peroxidation or the oxidation of (NAD)2. A free-radical mechanism is proposed for both horseradish-peroxidase-catalysed oxidation and peroxidation of (NAD)2.

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Year:  1985        PMID: 3994664      PMCID: PMC1144724          DOI: 10.1042/bj2260391

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  6 in total

1.  The biochemical basis of phagocytosis. I. Metabolic changes during the ingestion of particles by polymorphonuclear leukocytes.

Authors:  A J SBARRA; M L KARNOVSKY
Journal:  J Biol Chem       Date:  1959-06       Impact factor: 5.157

2.  The Streptococcus faecalis oxidases for reduced diphosphopyridine nucleotide. III. Isolation and properties of a flavin peroxidase for reduced diphosphopyridine nucleotide.

Authors:  M I DOLIN
Journal:  J Biol Chem       Date:  1957-03       Impact factor: 5.157

3.  The oxidation of reduced pyridine nucleotides by peroxidase.

Authors:  T AKAZAWA; E E CONN
Journal:  J Biol Chem       Date:  1958-05       Impact factor: 5.157

Review 4.  Oxidation states of peroxidase.

Authors:  I Yamazaki; K Yokota
Journal:  Mol Cell Biochem       Date:  1973-11-15       Impact factor: 3.396

5.  A dimer of diphosphopyridine nucleotide.

Authors:  R W Burnett; A L Underwood
Journal:  Biochemistry       Date:  1968-10       Impact factor: 3.162

6.  Formation of reduced nicotinamide adenine dinucleotide peroxide.

Authors:  C Bernofsky; S Y Wanda
Journal:  J Biol Chem       Date:  1982-06-25       Impact factor: 5.157

  6 in total
  2 in total

1.  Oxidation of nicotinamide coenzyme dimers by one-electron-accepting proteins.

Authors:  L Avigliano; V Carelli; A Casini; A Finazzi-Agrò; F Liberatore; A Rossi
Journal:  Biochem J       Date:  1986-08-01       Impact factor: 3.857

2.  Photoactivation studies of zinc porphyrin-myoglobin system and its application for light-chemical energy conversion.

Authors:  Chin-Hao Chang; Yi-Ting Hu; Chen-Fu Lo; Liyang Luo; Hung-Ming Lin; Cheng-Hsiang Chang; Ching-Yao Lin; Eric Wei-Guang Diau; Tung-Kung Wu
Journal:  Int J Biol Sci       Date:  2011-10-27       Impact factor: 6.580

  2 in total

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