Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide

Abstract

The recent high-resolution solution structures of human and Escherichia coli thioredoxin in their oxidized and reduced states support a catalytic model of protein disulfide reduction involving binding of a target protein and nucleophilic attack by the active-site Cys32 thiolate to form a transition state mixed disulfide.