期刊
BIOCHEMISTRY
卷 52, 期 33, 页码 5514-5516出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi400741c
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资金
- National Institute of General Medical Sciences [P30 GM103519]
- National Science Foundation [MCB-1054447]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1054447] Funding Source: National Science Foundation
Selenoprotein S (SelS, VIMP) is an intrinsically disordered enzyme that utilizes selenocysteine to catalyze the reduction of disulfide bonds and peroxides. Here it is demonstrated that selenocysteine is the residue oxidized by the peroxide substrate. It is possible to trap the reaction intermediate selenenic acid when the resolving cysteine is mutated. The selenocysteine allows SelS to rapidly re-form its selenenylsulfide bond following its reduction, and to resist inactivation by H2O2. We propose that SelS's peroxidase mechanism is similar to that of atypical 2-Cys peroxiredoxin and that selenocysteine allows SelS to sustain activity under oxidative stress.
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