Glutathione reductase functions as vanadate(V) reductase.
The oxidation of NADPH by vanadate(V) in the presence of glutathione reductase showed typical enzymatic kinetics. The oxidation was inhibited by N-ethylmaleimide, a glutathione reductase inhibitor. Superoxide dismutase had no significant effect on the oxidation, indicating noninvolvement of the superoxide radical. The vanadate(V) reduction was found to be a one-electron transfer process. These results suggest a new pathway for vanadate(V) metabolism and a new function of glutathione reductase.
Shi
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Department of Chemistry, West Virginia University, Morgantown 26505.
Dalal
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D000818:Animals; D002417:Cattle; D004578:Electron Spin Resonance Spectroscopy; D005980:Glutathione Reductase / Q000378:metabolism*; D007413:Intestinal Mucosa / Q000201:enzymology; D007700:Kinetics; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction; D013997:Time Factors; D014638:Vanadates / Q000378:metabolism*
D014638:Vanadates; D009249:NADP; D005980:Glutathione Reductase