Evidence for a common selenolate intermediate in the glutathione peroxidase-like catalysis of α-(phenylselenenyl) ketones and diphenyl diselenide
The glutathione peroxidase-like catalysis of α-(phenylselenenyl) ketones was investigated. Degradation studies demonstrated the rapid cleavage of the aliphatic carbon-selenium bond of α-(phenylselenenyl) ketones by glutathione at pH 6.9 in a methanolic phosphate buffer under argon. On treatment with excess glutathione under aerobic conditions, α-(phenylselenenyl) ketones, S- (phenylselenenyl)glutathione and diphenyl diselenide were all shown to give benzeneselenolate. This material was found to be oxidized by hydrogen peroxide considerably faster than α-(phenylselenenyl) ketones, S- (phenylselenenyl)glutathione or diphenyl diselenide. A catalytic mechanism involving benzeneselenolate, benzeneselenenic acid and S- (phenylselenenyl)glutathione as crucial intermediates was proposed to account for the glutathione peroxidase-like catalysis of α-(phenylselenenyl) ketones and diphenyl diselenide.
Engman, Lars,Andersson, Claes,Morgenstern, Ralf,Cotgreave, Ian A.,Andersson, Carl-Magnus,Hallberg, Anders
An accurate mass spectrometric approach for the simultaneous comparison of GSH, Cys, and Hcy in L02 cells and HepG2 cells using new NPSP isotope probes
A novel accurate method was developed for simultaneous quantitative comparison of GSH, Cys and Hcy in normal cells and cancer cells using new NPSP isotope probes based on LC/ESI-MS.
Li, Lu,Wang, Xiuli,Li, Qingling,Liu, Pengyuan,Xu, Kehua,Chen, Hao,Tang, Bo
supporting information
p. 11317 - 11320
(2015/07/07)
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