Metal and redox modulation of cysteine protein function

Chem Biol. 2003 Aug;10(8):677-93. doi: 10.1016/s1074-5521(03)00174-1.


In biological systems, the amino acid cysteine combines catalytic activity with an extensive redox chemistry and unique metal binding properties. The interdependency of these three aspects of the thiol group permits the redox regulation of proteins and metal binding, metal control of redox activity, and ligand control of metal-based enzyme catalysis. Cysteine proteins are therefore able to act as "redox switches," to sense concentrations of oxidative stressors and unbound zinc ions in the cytosol, to provide a "storage facility" for excess metal ions, to control the activity of metalloproteins, and to take part in important regulatory and signaling pathways. The diversity of cysteine's multiple roles in vivo is equally as fascinating as it is promising for future biochemical and pharmacological research.

Publication types

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

MeSH terms

  • Catalysis
  • Cysteine / chemistry
  • Cysteine / physiology*
  • Cysteine Endopeptidases / chemistry
  • Cysteine Endopeptidases / metabolism
  • Drug Design
  • Ligands
  • Metals / chemistry*
  • Molecular Structure
  • Oxidation-Reduction
  • Oxidoreductases / chemistry
  • Oxidoreductases / metabolism
  • Proteins / chemistry
  • Proteins / physiology*


  • Ligands
  • Metals
  • Proteins
  • Oxidoreductases
  • Cysteine Endopeptidases
  • Cysteine