Oxidoreduction of Protein Thiols in Redox Regulation

Biochem Soc Trans. 2005 Dec;33(Pt 6):1378-81. doi: 10.1042/BST20051378.

Abstract

Protein cysteines can undergo various forms of oxidation, some of them reversible (disulphide formation, glutathionylation and S-nitrosylation). While in the past these were viewed as protein damage in the context of oxidative stress, there is growing interest in oxidoreduction of protein thiols/disulphides as a regulatory mechanism. This review discusses the evolution of the concept of redox regulation from that of oxidative stress and the redox state of protein cysteines in different cellular compartments.

Publication types

  • Review

MeSH terms

  • Antioxidants
  • Cysteine / chemistry
  • Disulfides / chemistry
  • Glutaredoxins
  • Glutathione / metabolism
  • Oxidation-Reduction
  • Oxidative Stress
  • Oxidoreductases / metabolism
  • Proteins / chemistry*
  • Sulfhydryl Compounds / chemistry*
  • Thioredoxins / metabolism

Substances

  • Antioxidants
  • Disulfides
  • Glutaredoxins
  • Proteins
  • Sulfhydryl Compounds
  • Thioredoxins
  • Oxidoreductases
  • Glutathione
  • Cysteine