Cited by 28Redox biology and oxidative stressNitric Oxide and Endothelin EffectsNeutrophil, Myeloperoxidase and Oxidative Mechanisms

Detection and characterization of in vivo nitration and oxidation of tryptophan residues in proteins

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Bregere, Catherine, Rebrin, Igor, Sohal, Rajindar S.·2008·Methods in Enzymology

Abstract

Oxygen and nitrogen centered reactive species can cause specific structural modifications in amino acids and proteins, such as the addition of a nitro group onto aromatic residues. Heretofore, studies on protein nitration have mainly focused on the in vitro and in vivo nitro addition to tyrosine residues (3-nitrotyrosine or 3NT), whereas the formation of nitrotryptophan in proteins in vivo and/or its functional significance has remained quite obscure. A novel structural modification, involving the addition of nitro and hydroxy groups to tryptophan, has been detected in the mitochondrial protein succinyl-CoA:3-oxoacid CoA transferase (SCOT) in rat heart. Modified SCOT accumulated progressively with age, which was associated with an elevation of its activity. The specific biochemical properties of this novel amino acid were characterized by a combination of HPLC-electrochemical detection and mass spectrometric analysis. This chapter describes the experimental steps involved in the characterizations and a procedure for the synthesis of nitrohydroxytryptophan. Similar methodology can be applied to the identification of nitrohydroxytryptophan in other proteins.

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Crossref · 10.1016/s0076-6879(08)01219-6

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  • The effects of peroxynitrite on nitration of Tyr or Trp and S-nitrosylation of Cys likely depend on cellular status of antioxidants, various microenvironments including surface exposure, peptide loop structure, local charge groups, and the presence of competing amino acids nearby.

    “The effects of peroxynitrite on nitration of Tyr or Trp and S-nitrosylation of Cys likely depend on cellular status of antioxidants, various microenvironments including surface exposure, peptide loop structure, local charge groups, and the presence of competing amino acids nearby (e.g., Cys near the potentially-nitrated Trp or Tyr), as suggested [98].”

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Authors
Bregere, C., Rebrin, I., & Sohal, R. S.
Affiliations
University of Southern California (US)
Venue
Methods in Enzymology
Publisher
Elsevier
Published
2008
Volume
441
Pages
339-349
ISSN
0076-6879 (ISSN-L)
OpenAlex
W1583290442
Cited by
28
References
21
Citations by year
2025: 1 · 2023: 2 · 2022: 1 · 2020: 1 · 2018: 1 · 2016: 1 · 2015: 3 · 2014: 5 · 2012: 3
FWCI
4.31
Type
book chapter
Language
en
Open access
Locations
  • Methods in enzymology on CD-ROM/Methods in enzymology (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health
  • National Institute on Aging (R01 AG13563, R01AG013563)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
  • Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Keywords
protein oxidation, nitrotyrosine, mitochondrial proteins, rat heart, aging, reactive oxygen species, reactive nitrogen species
MeSH terms
Animals, Humans, Nitrates, Oxidation-Reduction, Proteins, Tryptophan

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