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

Structure. 1995 Mar 15;3(3):239-43. doi: 10.1016/s0969-2126(01)00153-8.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Disulfides / chemistry*
  • Disulfides / metabolism*
  • Humans
  • Oxidation-Reduction
  • Protein Conformation
  • Sulfhydryl Compounds / chemistry*
  • Sulfhydryl Compounds / metabolism*
  • Thioredoxins / chemistry*
  • Thioredoxins / metabolism*

Substances

  • Disulfides
  • Sulfhydryl Compounds
  • Thioredoxins