Thioredoxin Structure and Mechanism: Conformational Changes on Oxidation of the Active-site Sulfhydryls to a Disulfide

Overview

Journal Structure

Publisher Cell Press

Specialties Biochemistry
Biotechnology
Cell Biology
Molecular Biology

Date 1995 Mar 15

PMID 7788289

Citations 110

Authors

A Holmgren

Affiliations

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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.

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