Abstract
Many biological oxidations proceed via formation of radicals and/or peroxides. The tripeptide γ-glutamylcysteinylglycine or reduced glutathione (GSH) is known to protect cells against oxidative damage. This function can be executed in three different ways: 1. GSH, like other thiols, can act as a radical acceptor1, thereby forming the disulphide GSSG (oxidized glutathione): $$GSH + R. \to GS.RH2GS. \to GSSG$$ 2. Peroxides may be eliminated either by catalase (in case of hydrogen (peroxide) or by GSH in the glutathione peroxidase reaction2: Open image in new window 3. Oxidative reactions may also give rise to formation of disulphide bridges in proteins, often leading to unfolding and denaturation of these proteins. Glutathione is able to restore the function of these proteins by reduction of such disulphides, with formation of mixed disulphides as intermediates3,4: $$GSH + R - S - S - R' \rightleftharpoons G - S - S - R + R' - SHGSH + G - S - S - R \rightleftharpoons GSSG + R - SH$$
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