Affiliation:
1. Department of Pharmaceutical Chemistry, University of Kansas, Lawrence, KS 66047, U.S.A.
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 2H2O. 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.
Cited by
15 articles.
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