Peroxide modification of monoalkylated glutathione reductase. Stabilization of an active-site cysteine-sulfenic acid.
作者： H. Miller , A. Claiborne
DOI: 10.1016/S0021-9258(18)55003-1
关键词:
摘要: Hydrogen peroxide reacts with two-electron reduced glutathione reductase (GR EH2 species) to give the native oxidized enzyme (E) without detectable intermediates. Prior alkylation of interchange thiol iodoacetamide, however, dramatically changes both course and overall rate reaction. This oxidation, monitored spectrally, is characterized by an intermediate (EHRint) enhanced long wavelength absorbance extending 800 nm. species decays in a second peroxide-dependent phase form (EHRox) easily distinguished from E. Quenching experiments catalase allow isolation stable mixture consisting 36% monoalkylated GR (EHR), 60% EHRint, 4% EHRox; NADPH titration anaerobic dithiothreitol addition lead quantitative reduction EHRint EHR, there increase titer 0.8-SH/FAD on reduction. Of four titratable thiols present 2.7 are lost oxidation EHRox 0.7-0.8 mol cysteic acid/FAD formed. On basis these other observations, we conclude that thiol, which blocks disulfide formation, allows reaction at remaining charge-transfer proceed via stabilized cysteine-sulfenic acid (EHRint), undergoes further corresponding (EHRox).
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