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Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a
1Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.
Structure (London, England : 1993)
|March 15, 1995
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.