Mechanism of inhibition of horseradish peroxidase by cyclopropanone hydrate.

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Mechanism of inhibition of horseradish peroxidase by cyclopropanone hydrate.

Cyclopropanone hydrate irreversibly inactivates horseradish peroxidase in a time-dependent manner in the presence of oxidizing agent, hydrogen peroxide. The inhibition reaction is a second order reaction of cyclopropanone hydrate with compound I, the 2 electron-oxidized form of peroxidase, and results in covalent modification of the heme cofactor. A new propionic acid side chain is substituted ...

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Mechanism 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...

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Mechanism of inhibition of horseradish peroxidase-catalysed iodide oxidation by EDTA.

EDTA inhibits horseradish peroxidase (HRP)-catalysed iodide oxidation in a concentration and pH-dependent manner. It is more effective at pH 6 than at lower pH values. A plot of log Kiapp. values as a function of pH yields a sigmoidal curve from which a pKa value of 5.4 can be calculated for an ionizable group on the catalytically active HRP for EDTA inhibition. Among the structural analogues o...

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Mechanism of horseradish peroxidase inactivation by benzhydrazide: a critical evaluation of arylhydrazides as peroxidase inhibitors.

Many compounds are oxidized by haem enzymes, such as peroxidases and cytochromes P450, to highly reactive intermediates that function as enzyme inactivators. To evaluate the potential of arylhydrazides as selective metabolically activated peroxidase inhibitors, the mechanism of HRPC (horseradish peroxidase isoenzyme C) inhibition by BZH (benzhydrazide) was investigated in detail. No oxygen cons...

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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 ...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1982

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(20)65144-4