Mechanism of HRP-catalyzed nitrite oxidation by H2 O2 revisited: Effect of nitroxides on enzyme inactivation and its catalytic activity

Free Radical Biology & Medicine
Amram SamuniSara Goldstein

Abstract

The peroxidative activity of horseradish peroxidase (HRP) undergoes progressive inactivation while catalyzing the oxidation of nitrite by H2O2. The extent of inactivation increases as the pH increases, [nitrite] decreases or [H2O2] increases, and is accompanied by a loss of the Soret peak of HRP along with yellow-greenish coloration of the solution. HRP-catalyzed nitrite oxidation by H2O2 involves not only the formation of compounds I and II as transient heme species, but also compound III, all of which in turn, oxidize nitrite yielding •NO2. The rate constant of nitrite oxidation by compound III is at least 10-fold higher than that by compound II, which is also reducible by •NO2 where its reduction by nitrite is the rate-determining step of the catalytic cycle. The extent of the loss of the Soret peak of HRP is lower than the loss of its peroxidative activity implying that deterioration of the heme moiety leading to iron release only partially contributes toward heme inactivation. Cyclic stable nitroxide radicals, such as 2,2,6,6-tetramethyl-piperidine-N-oxyl (TPO), 4-OH-TPO and 4-NH2-TPO at µM concentrations detoxify •NO2 thus protecting HRP against inactivation mediated by this radical. Hence, HRP inactivation proceeds via n...Continue Reading

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Citations

Nov 25, 2018·Biosensors & Bioelectronics·Indra Memdi KhorisEnoch Y Park
Jul 30, 2019·Biochimica Et Biophysica Acta. General Subjects·Eric MaimonSara Goldstein
Sep 1, 2020·Free Radical Biology & Medicine·Amram Samuni, Sara Goldstein

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