Radical production from free and peptide-bound methionine sulfoxide oxidation by peroxynitrite and hydrogen peroxide/iron(II).

Abstract Methionine sulfoxide is a post-translational protein modification that has been receiving increasing attention in the literature. Here we used electron paramagnetic resonance spin trapping techniques to show that free and peptide-bound methionine sulfoxide is oxidized by hydrogen peroxide/iron(II)-EDTA and peroxynitrite through the intermediacy of the hydroxyl radical to produce both CH 3 and CH 2 CH 2 CH radicals. The results indicate that methionine sulfoxide residues are important targets of reactive oxygen- and nitrogen-derived species in proteins. Since the produced protein-derived radicals can propagate oxidative damage, the results add a new antioxidant route for the action of the enzyme peptide methionine sulfoxide reductase.