作者: S. A. Lipton , Y.-B. Choi , N. J. Sucher , H. S.-V. Chen
DOI: 10.1007/978-3-662-03596-2_5
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摘要: In recent years, as endogenous sources of oxidizing and reducing agents have been discovered, redox modulation protein function has recognized an important mechanism for many cell types. For our purposes, we will confine review to covalent modification sulfhydryl (thiol) groups on cysteine residues. If they possess a sufficient potential, can react form adducts single or, if two free are vicinal (in close proximity), disulfide bonds may possibly be formed. Reducing regenerate (—SH) by donating electron(s). Considering agents, in addition the usual suspects including glutathione, ascorbate, vitamin E, lipoic acid, reactive oxygen species, nitric oxide its redox-related species recently come fore. This occurred largely because rediscovery application biological systems work from early part this century showing organic synthesis nitrosothiols (RS-NO) (reviewed Stamler et al. 1992). NO group donors represent different group, each with own distinctive chemistry, which lead entirely effects.