Creation of allotypic active sites during oxidative stress

Hamid Mirzaei, Fred Regnier

Research output: Contribution to journalArticlepeer-review

38 Scopus citations


Oxidative stress is a factor in a series of diseases and aging, primarily through irreversible oxidative modification of proteins.1-3 A major question is how nonenzymatic oxidation has the specificity to impact cellular regulation. Here, we report the degree to which in vivo protein oxidation to the ketone and aldehyde level is random using yeast as a simple model system and hydrogen peroxide as an environmental oxidative stress agent. Among 415 affinity-selected proteins identified throughout the matrix of stressed cells, oxidation sites were found in 87, predominantly on lysine, arginine, proline, histidine, threonine, and methionine residues. In almost all cases, one to two specific oxidation sites on the exterior of proteins were identified using MS-derived sequence and publicly available 3-D structural data. This suggests that, when regulation or disease progression is mediated by protein oxidation, specific new "allotypic active sites" are being created in proteins that trigger the process.

Original languageEnglish (US)
Pages (from-to)2159-2168
Number of pages10
JournalJournal of Proteome Research
Issue number9
StatePublished - Sep 2006


  • Allotypic active sites
  • Avidin affinity chromatography
  • Biotin hydrazide
  • Biotinylation
  • Carbonylation
  • Hydrogen peroxide
  • In vivo oxidation
  • Oxidative stress
  • Protein carbonyls
  • Proteomics
  • Site-specific oxidation
  • Yeast

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)


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