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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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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
“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]
Citations
Cites
Beckman, J. S., Beckman, T. W., Chen, J., Marshall, P. A., & Freeman, B. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1620 · Cited by 7,029
Peroxynitrite oxidation of sulfhydryls.
Radí, R., Beckman, J. S., Bush, K., & Freeman, B. Α. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64313-7 · Cited by 2,492
The reaction of NO with superoxide
Huie, R. E., & Padmaja, S. (1993) · Free Radical Research Communications · doi:10.3109/10715769309145868 · Cited by 2,121
Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase
Ischiropoulos, H., Zhu, L., Chen, J., Tsai, M., Martin, J. C., Smith, C. D. L., & Beckman, J. S. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90431-u · Cited by 1,499
Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
Eiserich, J. P., Hristova, M., Cross, C. E., Jones, A. D., Freeman, B. A., Halliwell, B., & van der Vliet, A. (1998) · Nature · doi:10.1038/34923 · Cited by 1,496
Peroxynitrite, a cloaked oxidant formed by nitric oxide and superoxide
Koppenol, W. H., Moreno, J. J., Pryor, W. A., Ischiropoulos, H., & Beckman, J. S. (1992) · Chemical Research in Toxicology · doi:10.1021/tx00030a017 · Cited by 1,338
Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite
van der Vliet, A., Eiserich, J. P., Halliwell, B., & Cross, C. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.7617 · Cited by 780
MacMillan-Crow, L.-A., Crow, J. P., Kerby, J. D., Beckman, J. S., & Thompson, J. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11853 · Cited by 769
Unraveling peroxynitrite formation in biological systems
Radi, R., Peluffo, G., Alvarez, M. N., Naviliat, M., & Cayota, A. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00373-7 · Cited by 735
Inhibition of Mitochondrial Electron Transport by Peroxynitrite
Radi, R., Rodriguez, M., Castro, L., & Telleri, R. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1013 · Cited by 693
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Bonilla, I. M., Sridhar, A., Nishijima, Y., Györke, S., Cardounel, A. J., & Carnes, C. A. (2013) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0b013e31828748ca · Cited by 10
Choromańska, B., Myśliwiec, P., Kozłowski, T., Łuba, M., Wojskowicz, P., Dadan, J., Myśliwiec, H., Choromańska, K., Makarewicz, K., Zalewska, A., et al. (2021) · Journal of Inflammation Research · doi:10.2147/jir.s337910 · Cited by 10
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Lewis, S. J., Hoque, A., Sandock, K., Robertson, T. P., Bates, J. N., & Kooy, N. W. (2006) · Vascular Pharmacology · doi:10.1016/j.vph.2006.06.004 · Cited by 10
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He, J., Becares, E. R., Thulstrup, P. W., Gamon, L. F., Pedersen, J. N., Otzen, D. E., Gourdon, P. E., Davies, M. J., & Hägglund, P. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101631 · Cited by 9
Lushchak, O. V., Nykorak, N. Z., Ohdate, T., Inoue, Y., & Lushchak, V. I. (2009) · Biochemistry (Moscow) · doi:10.1134/s0006297909040130 · Cited by 9
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Mak, A. M., & Wong, M. W. (2005) · Chemical Physics Letters · doi:10.1016/j.cplett.2005.01.010 · Cited by 9
Lai, J.-T., Fang, H.-L., Hsieh, W., & Lin, W.-C. (2008) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.70681 · Cited by 9
Şentürk, A., Alver, A., Karkucak, M., Küçük, M., & Rendi, T. A. (2023) · The American Journal of the Medical Sciences · doi:10.1016/j.amjms.2023.09.002 · Cited by 8
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Xu, Z., Qian, J., Ge, Y.-F., Wang, Y., & Chen, H. (2022) · Molecules · doi:10.3390/molecules27154858 · Cited by 8
Pozzi, N., Lancellotti, S., CRISTOFARO, R. D., & Filippis, V. D. (2011) · Biophysical Chemistry · doi:10.1016/j.bpc.2011.07.007 · Cited by 8
Sartore, G., Piarulli, F., Ragazzi, E., Burlina, S., Chilelli, N. C., Sarais, C., Marin, R., Manzato, E., Fedele, D., & Lapolla, A. (2011) · International Journal of Cardiology · doi:10.1016/j.ijcard.2011.06.026 · Cited by 8
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Jacob, C., Doering, M., & Burkholz, T. (2009) · Wiley eBooks · doi:10.1002/9783527627585.ch4 · Cited by 8
Li, L., Zhang, J., Liu, L., Gu, C., Wu, X., Yan, L., & Zhang, Y. (2023) · Microchemical Journal · doi:10.1016/j.microc.2023.109855 · Cited by 7
Wojewoda, M., Walczak, J., Duszyński, J., & Szczepanowska, J. (2015) · Biochemical Pharmacology · doi:10.1016/j.bcp.2015.03.016 · Cited by 7
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Kohutiar, M., Ivica, J., Vytášek, R., Skoumalová, A., Illner, J., Santorova, P., & Wilhelm, J. (2016) · Physiological Research · doi:10.33549/physiolres.933175 · Cited by 7
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Xie, F., Zhou, R., Jian, C., Zhang, L., & He, Y. (2023) · Analytical Methods · doi:10.1039/d3ay00517h · Cited by 5
Świderska-Kołacz, G., Kumański, K., & Parka, B. (2012) · Cited by 5
Sabbah, H. N., Wang, M., Gupta, R. C., Rastogi, S., Ilsar, I., Viole, T., & Brewer, R. J. (2009) · Journal of Cardiac Failure · doi:10.1016/j.cardfail.2009.01.003 · Cited by 5
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Arunachalam, G., Samuel, S. M., Ding, H., & Triggle, C. R. (2014) · Springer eBooks · doi:10.1007/978-3-642-30018-9_5 · Cited by 5
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Sierens, J., Narimisa, M., Demeestere, K., Heugebaert, T. S. A., Nikiforov, A., Geyter, N. D., & Meulenaer, B. D. (2026) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5c12473 · Cited by 2
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Zhao, Z., Liang, J.-P., Dou, D., Qi, Z., & Zhou, Z. (2025) · Journal of Physics D Applied Physics · doi:10.1088/1361-6463/adfaa2 · Cited by 2
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Pezzotti, G., Yasukochi, Y., Ohgitani, E., Nakashio, M., Shin‐Ya, M., Adachi, T., Yamamoto, T., Ikegami, S., Zhu, W., Higasa, K., et al. (2025) · RSC Chemical Biology · doi:10.1039/d4cb00237g · Cited by 1
Zhao, J., Liu, K., Ren, T., Ma, X., Qin, Z., & Jin, L. (2026) · Plasma Processes and Polymers · doi:10.1002/ppap.70213 · Cited by 1
León, L., Lissi, E. A., Celedón, G., Gonzalez, G., Pazos, F., Álvarez, C., & Lanio, M. E. (2014) · The Protein Journal · doi:10.1007/s10930-014-9582-x · Cited by 1
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Zhang, X., & Li, D. (2006) · Cited by 1
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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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