期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 617, 期 -, 页码 26-37出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2016.09.013
关键词
Thiolate; Hydrogen peroxide; Sulfenyl amide; Glutathione; Redox signaling
资金
- National Institutes of Health, USA [ES023864]
- Novo Nordisk Foundation [NNF13OC0004294]
- Human Frontier Science Program, Italy [RGP0013/2014]
- Novo Nordisk Fonden [NNF13OC0004294] Funding Source: researchfish
Oxidation of critical signaling protein cysteines regulated by H2O2 has been considered to involve sulfenic acid (RSOH) formation. RSOH may subsequently form either a sulfenyl amide (RSNHR') with a neighboring amide, or a mixed disulfide (RSSR') with another protein cysteine or glutathione. Previous studies have claimed that RSOH can be detected as an adduct (e.g., with 5,5-dimethylcyclohexane-1,3-dione; dimedone). Here, kinetic data are discussed which indicate that few proteins can form RSOH under physiological signaling conditions. We also present experimental evidence that indicates that (1) dimedone reacts rapidly with sulfenyl amides, and more rapidly than with sulfenic acids, and (2) that disulfides can react reversibly with amides to form sulfenyl amides. As some proteins are more stable as the sulfenyl amide than as a glutathionylated species, the former may account for some of the species previously identified as the sulfenome - the cellular complement of reversibly-oxidized thiol proteins generated via sulfenic acids. (C) 2016 Elsevier Inc. All rights reserved.
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