Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide
作者： Arne Holmgren
DOI: 10.1016/S0969-2126(01)00153-8
关键词:
摘要: The recent high-resolution solution structures of human and Escherichia coli thioredoxin in their oxidized reduced states support a catalytic model protein disulfide reduction involving binding target nucleophilic attack by the active-site Cys32 thiolate to form transition state mixed disulfide.
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