Biological significance of nitric oxide-mediated protein modifications

Andrew J. Gow, Christiana R. Farkouh, David A. Munson, Michael A. Posencheg, Harry Ischiropoulos

Research output: Contribution to journalReview articlepeer-review

317 Citations (Scopus)


Nitric oxide (NO), despite an apparently simple diatomic structure, has a wide variety of functions in both physiology and pathology and within every major organ system. It has become an increasingly important scientific challenge to decipher how this wide range of activity is achieved. To this end a number of investigators have begun to explore how NO-mediated posttranslational modifications of proteins may represent mechanisms of cellular signaling. These modifications include: 1) binding to metal centers; 2) nitrosylation of thiol and amine groups; 3) nitration of tyrosine, tryptophan, amine, carboxylic acid, and phenylalanine groups; and 4) oxidation of thiols (both cysteine and methionine residues) and tyrosine. However, two particular modifications have recently received much attention, nitrosylation of thiols to produce S-nitrosothiol and nitration of tyrosine residues to produce nitrotyrosine. It is the purpose of this review to examine the possibility that these modifications may play a role in NO-mediated signaling.

Original languageEnglish
JournalAmerican Journal of Physiology - Lung Cellular and Molecular Physiology
Issue number2 31-2
Publication statusPublished - Aug 2004
Externally publishedYes


  • Nitration
  • Nitrosylation
  • Nitrotyrosine
  • Posttranslational modification
  • S-nitrosothiol

ASJC Scopus subject areas

  • Pulmonary and Respiratory Medicine
  • Cell Biology
  • Physiology

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