Abstract
Glutathione reductase (GR; E.C. 1.6.4.2) is a flavoprotein that catalyzes the NADPH-dependent reduction of oxidized glutathione (GSSG). In this study we tested the effects of Al3+, Ba2+, Ca2+, Li+, Mn2+, Mo6+, Cd2+, Ni2+, and Zn2+ on purified bovine liver GR. In a range of 10 μM–10 mM concentrations, Al3+, Ba2+, Li+, Mn2+, and Mo6+, and Ca2+ at 5 μM–1.25 mM, had no effect on bovine liver GR. Cadmium (Cd2+), nickel (Ni2+), and zinc (Zn2+) showed inhibitory effects on this enzyme. The obtained IC50 values of Cd2+, Ni2+, and Zn2+ were 0.08, 0.8, and 1 mM, respectively. Cd2+ inhibition was non-competitive with respect to both GSSG (KiGSSG 0.221 ± 0.02 mM) and NADPH (KiNADPH 0.113 ± 0.008 mM). Ni2+ inhibition was non-competitive with respect to GSSG (KiGSSG 0.313 ± 0.01 mM) and uncompetitive with respect to NADPH (KiNADPH 0.932 ± 0.03 mM). The effect of Zn2+ on GR activity was consistent with a non-competitive inhibition pattern when the varied substrates were GSSG (KiGSSG 0.320 ± 0.018 mM) and NADPH (KiNADPH 0.761 ± 0.04 mM), respectively.
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