Oxidation of substituted anilines by horseradish peroxidase compound II
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چکیده
منابع مشابه
Oxidation 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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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 کاملCobalt-substituted horseradish peroxidase.
Horseradish peroxidase can be reconstituted with cobalt porphyrin to give a cobaltic holoenzyme having physicochemical properties quite similar to those of the native ferric protein. The cobaltic protein (Co3+HRP) can be reduced to the cobaltous form (CoHRP), the analogue of ferroperoxidase and the reduced cobalt protein can bind O2 to form an analogue of oxyferroperoxidase (Compound III). Sinc...
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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 کاملKinetics of the oxidation of p-aminobenzoic acid catalyzed by horseradish peroxidase compounds I and II.
The kinetics of p-aminobenzoic acid oxidation catalyzed by horseradish peroxidase Compounds I and II was investigated intensively as a function of pH at 25 degrees in aqueous solutions of ionic strength 0.11. All of the rate data were collected from single turnover experiments involving reactions of a single enzyme compound. In reactions of both compounds, deviations from first order behavior w...
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ژورنال
عنوان ژورنال: Canadian Journal of Chemistry
سال: 1990
ISSN: 0008-4042,1480-3291
DOI: 10.1139/v90-331