Metals are directly involved in the redox interconversion of Saccharomyces cerevisiae glutathione reductase.
作者： Jos� Peinado , Javier Florindo , C. Garc�a-Alfonso , E. Mart�nez-Galisteo , Antonio Llobell
DOI: 10.1007/BF00229534
关键词:
摘要: Redox inactivation of glutathione reductase involves metal cations, since chelators protected against NADPH-inactivation, 3 µM EDTA or 10 DETAPAC yielding full protection. Ag+, Zn2+ and Cd2+ potentiated the redox promoted by NADPH alone, while Cr3+, Fe2+, Fe3+, Cu+, Cu2+ enzyme. The effect was time-dependent, unlike conventional inhibition. Glutathione interconversion did not require dioxygen, excluding participation active oxygen species produced cations. One ion required per enzyme subunit to yield being reactivated EDTA. could arise from blocking dithiol formed at site reduced like Cd2+.
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