The Reaction of Chlorite with Horseradish Peroxidase and Chloroperoxidase

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The reaction of chlorite with horseradish peroxidase and chloroperoxidase. Enzymatic chlorination and spectral intermediates.

Chloroperoxidase and horseradish peroxidase use NaClOz as both the oxidant and the halogen donor for the peroxidative chlorination of monochlorodimedone. Previous studies have shown that both horseradish peroxidase and chloroperoxidase can catalyze iodination reactions with hydrogen peroxide as the oxidant; however, only chloroperoxidase catalyzes chlorination reactions under these conditions. ...

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The reaction of chloroperoxidase with chlorite and chlorine dioxide.

Chloroperoxidase catalyzes the dismutation of chlorite-forming chloride, chlorine dioxide, chlorate, and oxygen as products. The yields of chlorine dioxide are variable because chloroperoxidase also catalyzes the decomposition of this compound and, in addition, moderate concentrations of chlorine dioxide inactivate the enzyme. Chloride, chlorate, and oxygen are the products of the decomposition...

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Mechanism of the chlorination reaction catalyzed by horseradish peroxidase with chlorite.

Horseradish peroxidase and chlorite, NaC102, are able to catalyze chlorination of monochlorodimedone to form dichlorodimedone. Catalytic amounts of horseradish peroxidase act to disproportionate chlorite forming chlorine dioxide and chloride ion. The chlorine dioxide thus formed is responsible for the chlorination of monochlorodimedone. It was previously thought (Chiang, R., Rand-Meir, T., Maki...

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The reaction of ferrous horseradish peroxidase with hydrogen peroxide.

Hydrogen peroxide reacts with ferrous horseradish peroxidase and converts it to oxyperoxidase in a sequence of two reactions. The first is the reaction of ferrous peroxidase with HzOz to form Compound II; the second is the reaction of Compound II with HzOz to form oxyperoxidase. Both reactions follow second order kinetics, being first order with respect to each of the reactants. They proceed wi...

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Stoichiometry of the reaction between horseradish peroxidase and p-cresol.

Over a wide range of pH horseradish peroxidase compound I can be reduced quantitatively via compound II to the native enzyme by only 1 molar equivalent of p-cresol. Since 2 molar equivalents of electrons are required for the single turnover of the enzymatic cycle, p-cresol behaves as a 2-electron reductant. With p-cresol and compound I in a 1:1 ratio compound II and p-methylphenoxy radicals are...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1974

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(20)79890-x