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Biochim Biophys Acta. 1980 Jan 11;611(1):87-98.

The glutathione peroxidase activity of glutathione S-transferases.

Abstract

Glutatione transferases (RX:glutathione R-transferases, EC 2.5.1.18) B and AA were purified from rat liver to investigate the mechanism for their apparent GSH peroxidase activity (GSSG formation). Both transferases catalyze an overall reaction in which loss of cumene hydroperoxide is accompanied by a stoichiometric increase in GSSG. Inclusion of cysteamine, a thiol, results in a reduction of GSSG formation but has no effect on hydroperoxide loss. Cysteamine does not inhibit the transferase-catalyzed conjugation of GSH and 1-chloro-2,4-dinitrobenzene. Peroxidase reactions carried out in the presence of cyanide, another nucleophile, also result in a reduction of GSSG formation without altering the rate of cumene hydroperoxide loss; cyanide does not inhibit transferase activity with 1-chloro-2,4-dinitrobenzene. Both cysteamine and cyanide are capable of blocking GSSG formation in the non-enzymic oxidation of GSH by hydrogen peroxide without blocking H2O2 loss. These results are consistent with a mechanism for GSH transferases in which nucleophilic attack by GS- on hydroperoxide results in a reactive intermediate, presumably the sulfenic acid of glutathione, GSOH. GSH + ROOH in equilibrium GSHO + ROH (1) This sulfenic acid then reacts non-enzymically with GSH to produce GSSG. GSOH + GSH in equilibrium GSSG + H2O (2) The summing of Reactions 1 and 2 explains the observed stoichiometry. Cysteamine and cyanide can compete with GSH for the sulfenic acid in Reaction 2, thus reducing GSSG formation. Thios.

PMID:
7350921
DOI:
10.1016/0005-2744(80)90045-5
[Indexed for MEDLINE]

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