Tyrosine phosphorylation/dephosphorylation regulates peroxynitrite-mediated peptide nitration

Wei Qun Shi, Hui Cai, Dian Dou Xu, Xiao Yang Su, Peng Lei, Yu Fen Zhao, Yan Mei Li

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


Proteins are targets of reactive nitrogen species such as peroxynitrite and nitrogen dioxide. Among the various amino acids in proteins, tyrosine and tryptophan residues are especially susceptible to attack by reactive nitrogen species. On the other hand, protein tyrosine phosphorylation has gained much attention in respect to cellular regulatory events and signal transduction. Peroxynitrite-mediated nitration of peptide YPPPPPW and phosphopeptide pYPPPPPW were studied at pH 7.4. The predominant nitrated products were separated and identified by reverse phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (LC-MS). The nitration sites were established by tandem electrospray ionization-mass spectrometry (LC-MS/MS). A regulatory effect of tyrosine phosphorylation/dephosphorylation on peptide nitration was observed. YPPPPPW was predominantly nitrated at tyrosine residue while pYPPPPPW was nitrated at tryptophan one. Our results can help in understanding the biochemical significance of the relationship of tyrosine phosphorylation and nitration in proteins.

Original languageEnglish (US)
Pages (from-to)1-5
Number of pages5
JournalRegulatory Peptides
Issue number1-3
StatePublished - Dec 1 2007
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Endocrinology
  • Clinical Biochemistry
  • Cellular and Molecular Neuroscience


  • Nitration
  • Peroxynitrite
  • Phosphorylation
  • Tryptophan
  • Tyrosine


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