PMID: 8973647Dec 1, 1996Paper

Class-pi glutathione S-transferase is unable to regain its native conformation after oxidative inactivation by hydrogen peroxide

European Journal of Biochemistry
N Sluis-CremerH Dirr

Abstract

The oxidation of protein sulphydryls to disulphides and their reduction back to sulphydryls is an early cellular response to oxidative stress. Hydrogen-peroxide-mediated oxidation of class-pi glutathione S-transferase results in the formation of disulphide bonds, which inhibits its catalytic function yet allows it to retain its non-substrate-ligand-binding properties. The overall hydrodynamic volume of the oxidised class-pi glutathione S-transferase type-1 homodimer (GSTP1-1) is decreased, and its tertiary-structural and secondary-structural elements are changed with respect to the native protein. Structural differences appear to be prominent in domain 1 of oxidised GSTP1-1, in that the exposure of both tryptophan residues is increased, while the electric potential about one of them is altered. Treatment of the oxidised protein with dithiothreitol or glutathione restores its enzymatic capabilities, albeit with lower specific activities for 1-chloro-2,4-dinitrobenzene and ethacrynic acid. The hydrophobic binding site (H-site) for electrophilic substrates is negatively affected in that the K(m) and catalytic-efficiency values are diminished significantly with respect to those values obtained for the native protein. The dithiothre...Continue Reading

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Citations

Feb 25, 2006·Neurochemistry International·Luciane Rosa FeksaClovis Milton Duval Wannmacher
Jul 25, 2015·Archiv der Pharmazie·Mustafa Muhlis Alparslan, Özkan Danış
Jan 10, 2019·Current Medicinal Chemistry·Agnieszka Ścibior, Joanna Kurus
Apr 8, 2009·Xenobiotica; the Fate of Foreign Compounds in Biological Systems·R Appiah-OpongN P E Vermeulen

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