One- and two-electron reduction of quinones by glutathione reductase.
Yeast glutathione reductase (E.C. 1.6.4.2) catalyzes the oxidation of NADPH by p-quinones and ferricyanide with a maximal turnover number (TNmax) of 4-5 s-1.NADP+ stimulates the reaction and the TNmax/Km value of acceptors is reached at NADP+/NADPH greater than or equal to 100. TNmax is increased up to 30-33 s-1. The stimulatory effect of NADP+ may be associated with its complexation with the NADPH-binding site in the reduced enzyme (Kd = 40-60 microM). It is suggested that NADP+ shifts the electron density towards FAD in the two-electron-reduced enzyme and, evidently, changes its one-electron-reduction potentials, while quinones oxidize an equilibrium form of glutathione reductase containing reduced FAD. In the absence of NADP+ the reduction of quinones by glutathione reductase proceeds mainly in a two-electron manner. At NADP+/NADPH = 100 a one-electron reduction makes up 44% of the total process. At pH 6.0-7.0 the reduced forms of naphthoquinones undergo cyclic redox conversions. A hyperbolic dependence exists of the log TN/Km of quinones on their one-electron-reduction potentials.
Cénas
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NK
Institute of Biochemistry, Lithuanian Academy of Sciences, Vilnus, U.S.S.R.
Rakauskiené
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GA
Kulys
J J
JJ
D002384:Catalysis; D008058:Dihydrolipoamide Dehydrogenase / Q000378:metabolism; D004579:Electron Transport; D005980:Glutathione Reductase / Q000502:physiology*; D006863:Hydrogen-Ion Concentration; D009249:NADP / Q000502:physiology; D010084:Oxidation-Reduction; D011809:Quinones; D012441:Saccharomyces cerevisiae / Q000201:enzymology
D011809:Quinones; D009249:NADP; D008058:Dihydrolipoamide Dehydrogenase; D005980:Glutathione Reductase