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

FEBS Letters

Nakao, Lia S²  Iwai, Leo K¹  Augusto, Ohara²  Kalil, Jorge¹ 

[1] Laboratório de Imunologia, Instituto do Coração, Universidade de São Paulo, 05403-00 São Paulo, SP, Brazil;Departamento de Bioquı́mica, Instituto de Quı́mica, Universidade de São Paulo, C.P. 26077, 05513-970 São Paulo, SP, Brazil

关键词: Methionine sulfoxide;    Methionine sulfoxide reductase;    Protein-derived radical;    Electron paramagnetic resonance;    Oxidative stress;    Aging;    EPR;    electron paramagnetic resonance;    DBNBS;    3;    5-dibromo-4-nitrosobenzenesulfonic acid;    MNP;    2-methyl-2-nitrosopropane;    Msr;    methionine sulfoxide reductase;    peroxynitrite;    the sum of peroxynitrite anion (ONOO−;    oxoperoxonitrate (−1)) and peroxynitrous acid (ONOOH;    hydrogen oxoperoxonitrate) unless specified;   

DOI  :  10.1016/S0014-5793(03)00674-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown