Spin trapping of glutathiyl and protein radicals produced from nitric oxide-derived oxidants

Ohara Augusto*, Marcelo G. Bonini, Daniel F. Trindade

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

13 Scopus citations

Abstract

Despite the importance of protein radicals in cell homeostasis and cell injury, their formation, localization, and propagation reactions remain obscure, mainly because of the difficulties in detecting and characterizing radicals, in general, and protein radicals, in particular. New approaches based on spin trapping coupled with other methodologies are under development/testing but so far they have been applied mainly to the study of protein-tyrosyl and protein-tryptophanyl radicals. Here, our aim is to emphasize the importance of developing new methodologies for the detection of glutathyil and protein-cysteinyl radicals under physiological conditions. To this end, we summarize current EPR evidence supporting the view that glutathione and protein-cysteines are among the preferential targets of nitric oxide-derived oxidants and that they are oxidized to the glutathiyl and protein-cysteinyl radicals, respectively. The possible intermediacy of these species in the biological formation of mediators of protein-cysteine redox signaling, such as S-nitrosothiols and sulfenic acids, is also discussed.

Original languageEnglish (US)
Pages (from-to)1224-1232
Number of pages9
JournalFree Radical Biology and Medicine
Volume36
Issue number10
DOIs
StatePublished - May 15 2004
Externally publishedYes

Keywords

  • BM
  • BSA
  • Bovine serum albumin
  • Carbonate radical anion
  • EPR spin trapping
  • Free radicals
  • Generic biomolecule
  • Glutathiyl radical
  • Nitric oxide
  • Nitrogen dioxide
  • Nitrosoactive stress
  • Peroxynitrite
  • Protein-cysteinyl radical
  • Signaling pathways
  • Superoxide anion

ASJC Scopus subject areas

  • Biochemistry
  • Physiology (medical)

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