Oxidation of NAD dimers by horseradish peroxidase
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منابع مشابه
Oxidation of NAD dimers by horseradish peroxidase.
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 ...
متن کاملMechanism of Oxidation by Horseradish Peroxidase Compound
Binding of p-cresol to native horseradish peroxidase was investigated by differential spectrophotometry, and the value lo3 Kdiss = 3 M was obtained at neutral and acid pH; binding is not competitive with that of cyanide and hydroxide. The Soret region spectrum of Compound II of the enzyme was measured in the steady state at pH 4.26, 6.89, and 10.95, and the differences were found to be too smal...
متن کاملOxidation of horseradish peroxidase compound II to compound I.
In the reaction between equimolar amounts of horseradish peroxidase and chlorite, the native enzyme is oxidized directly to Compound II (Hewson, W.D., and Hager, L.P. (1979) J. Biol. Chem. 254, 3175-3181). At acidic pH but not at alkaline values, this initial reaction is followed by oxidation of Compound II to Compound I. The highly pH-dependent chemistry of Compound II can be readily demonstra...
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Philip J. KERSTEN,* 11 B. KALYANARAMAN,t Kenneth E. HAMMEL,4 Bengt REINHAMMAR§ and T. Kent KIRK*¶ * Forest Products Laboratory, USDA Forest Service, Madison, WI 53705 and Department of Bacteriology, University of Wisconsin, Madison, WI 53706, tNational Biomedical ESR Center, Medical College of Wisconsin, Milwaukee, WI 53226, $Department of Chemistry, SUNY College of Environmental Sciences and F...
متن کاملComparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes.
Lignin peroxidase oxidizes non-phenolic substrates by one electron to give aryl-cation-radical intermediates, which react further to give a variety of products. The present study investigated the possibility that other peroxidative and oxidative enzymes known to catalyse one-electron oxidations may also oxidize non-phenolics to cation-radical intermediates and that this ability is related to th...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1985
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2260391