The DOI matches its Crossref record; 147 of the 147 references it cites were found in a registry or an index.
Peroxynitrite reactivity with amino acids and proteins
Abstract
Peroxynitrite, the product of the fast reaction between nitric oxide ((*)NO) and superoxide O(2)(*-) radicals, is an oxidizing and nitrating agent which is able to traverse biological membranes. The reaction of peroxynitrite with proteins occurs through three possible pathways. First, peroxynitrite reacts directly with cysteine, methionine and tryptophan residues. Second, peroxynitrite reacts fast with transition metal centers and selenium-containing amino acids. Third, secondary free radicals arising from peroxynitrite homolysis such as hydroxyl and nitrogen dioxide, and the carbonate radical formed in the presence of carbon dioxide, react with protein moieties too. Nitration of tyrosine residues is being recognized as a marker of the contribution of nitric oxide to oxidative damage. Peroxynitrite-dependent tyrosine nitration is likely to occur through the initial reaction of peroxynitrite with carbon dioxide or metal centers leading to secondary nitrating species. The preferential protein targets of peroxynitrite and the role of proteins in peroxynitrite detoxifying pathways are discussed.
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“Interestingly, the nitroproteome appears to be quite specific, and pathological responses may be due to modification of particularly sensitive proteins, including those that regulate signaling and cell metabolism (49–52).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [49]
In the citing paper
“Interestingly, the nitroproteome appears to be quite specific, and pathological responses may be due to modification of particularly sensitive proteins, including those that regulate signaling and cell metabolism (49–52).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [49]
In the citing paper
“The protonated form of ONOO— (ONOOH, pKa = 6.5 to 6.8) decomposes rapidly to RNS, yielding approximately 28% of free •NO2 and •OH radical [123], Figure 5 down.”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [123]
In the citing paper
“Peroxynitrite and reactive species derived from it (e.g., nitrogen dioxide) are important in inflammatory responses [85] and can modulate cell signaling [87-90], in part by promoting the oxidation or nitration of a broad range of biomolecules [62].”
From Regulation of obesity and insulin resistance by nitric oxide (2014) · cites this paper as [87]
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Metadata
- Authors
- Alvarez, B., & Radi, R.
- Venue
- Amino Acids
- Published
- 2003-09-26
- Volume
- 25
- Issue
- 3-4
- Pages
- 295-311
- ISSN
- 0939-4451 (ISSN-L)
- 1438-2199
- OpenAlex
- W2141352921
- Cited by
- 560
- References
- 147
- Citations by year
- 2026: 9 · 2025: 9 · 2024: 15 · 2023: 18 · 2022: 23 · 2021: 24 · 2020: 14 · 2019: 16 · 2018: 19 · 2017: 25 · 2016: 31 · 2015: 27 · 2014: 44 · 2013: 28 · 2012: 22
- FWCI
- 7.01
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Amino Acids (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- peroxynitrite, nitric oxide, superoxide, protein oxidation, protein nitration, tyrosine nitration, cysteine, methionine, tryptophan, transition metal centers, selenium-containing amino acids, hydroxyl radicals, nitrogen dioxide, carbonate radical, oxidative damage
- MeSH terms
- Amino Acids, Animals, Antioxidants, Cytosol, Free Radicals, Humans, Models, Chemical, Nitric Oxide, Oxidation-Reduction, Proteins, Superoxides, Molecular Structure, Peroxynitrous Acid
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