Cysteine residues as catalysts for covalent peptide and protein modification: a role for thiyl radicals?

Christian Schöneich

Journal: Biochemical Society transactions 2012;39(5):1254-9

PMID: 21936798

Free Full Text on PubMed Central View on PubMed

Abstract

Cysteine thiyl radicals engage in reversible intramolecular hydrogen-transfer reactions with amino acid residues in peptides and proteins. These reactions can be experimentally demonstrated through covalent hydrogen-deuterium exchange when experiments are carried out in (2)H2O. To this end, hydrogen-transfer reactions have been observed between cysteine thiyl radicals and glycine, alanine, serine, valine and leucine in both model peptides and a protein, insulin. The relevance of such reactions for protein oxidation under conditions of oxidative stress is discussed.

Address: Department of Pharmaceutical Chemistry, University of Kansas, Lawrence, KS 66047, USA. [email protected]

DOI: 10.1042/BST0391254

Link outs

Free resources

Full Text Sources:

Subscription / membership required

Full Text Sources:

https://portlandpress.com/biochemsoctrans/article-...

MeSH Terms: Amino Acids, Carbon, Cysteine, Deuterium Exchange Measurement, Free Radicals, Hydrogen, Insulin, Molecular Structure, Peptides, Sulfhydryl Compounds