Oxidation of NAD dimers by horseradish peroxidase
- 1 March 1985
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 226 (2) , 391-395
- https://doi.org/10.1042/bj2260391
Abstract
Horseradish peroxidase catalyzes 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 catalyzes the peroxidation of (NAD)2 to NAD. In contrast, bacterial [Streptococcus faecalis] NADH peroxidase does not catalyze the peroxidation or the oxidation of (NAD)2. A free-radical mechanism is proposed for both horseradish-peroxidase-catalyzed oxidation and peroxidation of (NAD)2.This publication has 6 references indexed in Scilit:
- Formation of reduced nicotinamide adenine dinucleotide peroxide.Journal of Biological Chemistry, 1982
- Oxidation states of peroxidaseMolecular and Cellular Biochemistry, 1973
- A dimer of diphosphopyridine nucleotideBiochemistry, 1968
- The Biochemical Basis of PhagocytosisJournal of Biological Chemistry, 1959
- THE OXIDATION OF REDUCED PYRIDINE NUCLEOTIDES BY PEROXIDASEJournal of Biological Chemistry, 1958
- THE STREPTOCOCCUS FAECALIS OXIDASES FOR REDUCED DIPHOSPHOPYRIDINE NUCLEOTIDE .3. ISOLATION AND PROPERTIES OF A FLAVIN PEROXIDASE FOR REDUCED DIPHOSPHOPYRIDINE NUCLEOTIDE1957