Formation of peroxides in amino acids and proteins exposed to oxygen free radicals

S. Gebicki*, J. M. Gebicki

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

264 Citations (Scopus)

Abstract

Dilute aqueous solutions of BSA or lysozyme gave positive tests for peroxides after exposure to reactive oxygen species. The reactive species were generated by γ-irradiation, reduction of H2O2 with Fe2+ ions or thermal decomposition of an azo compound. Peroxides were assayed by an iodometric method. Identification of the new groups as hydroperoxides was confirmed by their ability to oxidize a range of compounds and by the kinetics of their reaction with iodide. The hydroperoxide groups were bound to the proteins and their yields (G values) corresponded to 1.2 -OOH groups per 100 eV of radiation energy absorbed for BSA, and 0.8 for lysozyme. The oxygen free radicals effective in protein peroxidation were the hydroxyl and organic peroxyl, but not superoxide or its protonated form. The efficiency of BSA peroxidation initiated by the hydroxyl radicals was 40%. Protein peroxides decayed spontaneously with a half-life of about 1.5 days at 20°C. Exposure of the common amino acids to hydroxyl free radicals showed that six of them (glutamate, isoleucine, leucine, lysine, proline and valine) were peroxidized with similar efficiency to the proteins, whereas the rest were inert or much less susceptible. These results suggest that some proteins may be peroxidized by a variety of agents in vivo and that their subsequent reactions with protective agents, such as ascorbate or glutathione, may decrease the antioxidant potential of cells and tissues.

Original languageEnglish
Pages (from-to)743-749
Number of pages7
JournalBiochemical Journal
Volume289
Issue number3
DOIs
Publication statusPublished - 1 Feb 1993

Fingerprint Dive into the research topics of 'Formation of peroxides in amino acids and proteins exposed to oxygen free radicals'. Together they form a unique fingerprint.

Cite this