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 ·CH3 and ·CH2CH2CH 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. © 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Nakao, L. S., Iwai, L. K., Kalil, J., & Augusto, O. (2003). Radical production from free and peptide-bound methionine sulfoxide oxidation by peroxynitrite and hydrogen peroxide/iron(II). FEBS Letters, 547(1–3), 87–91. https://doi.org/10.1016/S0014-5793(03)00674-4