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• W1976043762 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 *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." @default.
• W1976043762 created "2016-06-24" @default.
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• W1976043762 date "2003-06-19" @default.
• W1976043762 modified "2023-09-25" @default.
• W1976043762 title "Radical production from free and peptide-bound methionine sulfoxide oxidation by peroxynitrite and hydrogen peroxide/iron(II)" @default.
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• W1976043762 doi "https://doi.org/10.1016/s0014-5793(03)00674-4" @default.
• W1976043762 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12860391" @default.
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