Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide.
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.
Holmgren
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Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.
D004220:Disulfides / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013438:Sulfhydryl Compounds / Q000737:chemistry* / Q000378:metabolism*; D013879:Thioredoxins / Q000737:chemistry* / Q000378:metabolism*
D004220:Disulfides; D013438:Sulfhydryl Compounds; D013879:Thioredoxins