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Direct EPR Detection of the Carbonate Radical Anion Produced from Peroxynitrite and Carbon Dioxide
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The biological effects of peroxynitrite have been recently considered to be largely dependent on its reaction with carbon dioxide, which is present in high concentrations in intra- and extracellular compartments. Peroxynitrite anion (ONOO-) reacts rapidly with carbon dioxide, forming an adduct, nitrosoperoxocarboxylate (ONOOCO2-), whose decomposition has been proposed to produce reactive intermediates such as the carbonate radical (CO-3). Here, by the use of rapid mixing continuous flow electron paramagnetic resonance (EPR), we directly detected the carbonate radical in flow mixtures of peroxynitrite with bicarbonate-carbon dioxide over the pH range of 6-9. The radical was unambiguously identified by its EPR parameters (g = 2.0113; line width = 5.5 G) and by experiments with bicarbonate labeled with 13C. In this case, the singlet EPR signal obtained with 12C bicarbonate splits into the expected doublet because of 13C (a(13C)= 11.7 G). The singlet spectrum of the unlabeled radical was invariant between pH 6 and 9, confirming that in this pH range the detected radical is the carbonate radical anion (CO-3). Importantly, in addition to contributing to the understanding of nitrosoperoxocarboxylate decomposition pathways, this is the first report unambiguously demonstrating the formation of the carbonate radical anion at physiological pHs by direct EPR spectroscopy.
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“The carbonate radical can be formed in vivo by the reaction of the hydroxyl radical with carbonate or bicarbonate (138) or via the reaction of peroxynitrite with carbon dioxide (Eq. 30) (112, 608, 640).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [112]
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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
The reaction of NO with superoxide
Huie, R. E., & Padmaja, S. (1993) · Free Radical Research Communications · doi:10.3109/10715769309145868 · Cited by 2,121
Harrison's Principles of Internal Medicine
Verghese, A. (1994) · JAMA · doi:10.1001/jama.1994.03520080084052 · Cited by 1,367
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
Maienthal, M. (1979) · Journal of AOAC INTERNATIONAL · doi:10.1093/jaoac/62.6.1364b · Cited by 1,102
Oxidative Damage and Tyrosine Nitration from Peroxynitrite
Beckman, J. S. (1996) · Chemical Research in Toxicology · doi:10.1021/tx9501445 · Cited by 993
Oxidative chemistry of nitric oxide: the roles of superoxide, peroxynitrite, and carbon dioxide
Squadrito, G. L., & Pryor, W. A. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00095-1 · Cited by 800
Kissner, R., Nauser, T., Bugnon, P., Lye, P. G., & Koppenol, W. H. (1997) · Chemical Research in Toxicology · doi:10.1021/tx970160x · Cited by 629
Denicola, A., Freeman, B. A., Trujillo, M., & Radi, R. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0363 · Cited by 593
Biochemistry by numbers: simulation of biochemical pathways with Gepasi 3
Mendes, P. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01103-1 · Cited by 574
Research works printed but not linked: 6
- Augusto, 1996, Braz. J. Med. Biol. Res., 29, 853
- Pryor, 1995, Am. J. Physiol., 168, L699
- Mendes, 1993, Comput. Appl. Biosci., 9, 563
- Lilie, 1978, Radiat. Phys. Chem., 11, 225
- Eriksen, 1985, Radiat. Phys. Chem., 26, 197
- Gomes, L. F., The Role of Carbon-centered Radicals on Hydrazine Toxicity. Ph.D. thesis, 1996, Instituto de Quı́mica, Universidade de São Paulo.
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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
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Alvarez, B., & Radi, R. (2003) · Amino Acids · doi:10.1007/s00726-003-0018-8 · Cited by 560
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Augusto, O., Bonini, M. G., Amanso, A. M., Linares, E., Santos, C. C. X., & De Menezes, S. L. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00786-4 · Cited by 555
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Burns, J. M., Cooper, W. J., Ferry, J. L., King, D. W., DiMento, B. P., McNeill, K., Miller, C. J., Miller, W. L., Peake, B. M., Rusak, S. A., et al. (2012) · Aquatic Sciences · doi:10.1007/s00027-012-0251-x · Cited by 454
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Goldstein, S., Lind, J., & Merényi, G. (2005) · Chemical Reviews · doi:10.1021/cr0307087 · Cited by 412
Raedschelders, K., Ansley, D. M., & Chen, D. D. Y. (2011) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2011.11.004 · Cited by 393
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Nitric oxide, antioxidants and prooxidants in plant defence responses
Groß, F., Durner, J., & Gaupels, F. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00419 · Cited by 352
NAD(P)H, a directly operating antioxidant?
Kirsch, M., & de GROOT, H. (2001) · The FASEB Journal · doi:10.1096/fj.00-0823hyp · Cited by 333
Zhao, Y., Patange, A. D., Sun, D., & Tiwari, B. K. (2020) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12644 · Cited by 326
Biochemical basis and metabolic interplay of redox regulation
Zhang, L., Wang, X., Cueto, R., Effi, C., Zhang, Y., Tan, H., Qin, X., Ji, Y., Yang, X., & Wang, H. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101284 · Cited by 308
Connecting the Chemical and Biological Properties of Nitric Oxide
Toledo, J. C., & Augusto, O. (2012) · Chemical Research in Toxicology · doi:10.1021/tx300042g · Cited by 294
Self-citationSantos, C. X. C., Anjos, E. I., & Augusto, O. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1491 · Cited by 275
Self-citationTherapeutic Hypercapnia Reduces Pulmonary and Systemic Injury following In Vivo Lung Reperfusion
Laffey, J. G., Tanaka, M., Engelberts, D., LUO, X., Yuan, S., Tanswell, A. K., Post, M., Lindsay, T. F., & Kavanagh, B. P. (2000) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.162.6.2003066 · Cited by 258
Ford, E., Hughes, M., & Wardman, P. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00850-x · Cited by 229
Modolo, L. V., Augusto, O., Almeida, I. M. G., Magalhaes, J. R., & Salgado, I. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.05.078 · Cited by 229
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Self-citationDetection and quantification of nitric oxide–derived oxidants in biological systems
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Self-citationApocynin inhibits peroxynitrite formation by murine macrophages
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Kinetic and mechanistic considerations to assess the biological fate of peroxynitrite
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Modolo, L. V., Augusto, O., Almeida, I. M. G., Pinto-Maglio, C. A. F., Oliveira, H. C., Seligman, K., & Salgado, I. (2006) · Plant Science · doi:10.1016/j.plantsci.2006.02.010 · Cited by 147
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Self-citationWhat really happens in the neutrophil phagosome?
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Modification of tryptophan and tryptophan residues in proteins by reactive nitrogen species
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Self-citationCatalysis of Peroxide Reduction by Fast Reacting Protein Thiols
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Self-citationZhang, H., Andrekopoulos, C., Joseph, J., Chandran, K., Karoui, H., Crow, J. P., & Kalyanaraman, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302051200 · Cited by 107
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Stadler, K., Bonini, M. G., Dallas, S., Jiang, J., Radí, R., Mason, R. P., & Kadiiska, M. B. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.06.023 · Cited by 81
Self-citationVercesi, A. E. (2006) · Frontiers in bioscience · doi:10.2741/1990 · Cited by 81
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Crean, C. W., Geacintov, N. E., & Shafirovich, V. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200500991 · Cited by 78
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Nitric oxide, peroxynitrite and lipoxygenase in atherogenesis: mechanistic insights
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Interactions of Nitric Oxide and Peroxynitrite with Low-Density Lipoprotein
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Peroxynitrous acid: controversy and consensus surrounding an enigmatic oxidant
Koppenol, W. H., Bounds, P. L., Nauser, T., Kissner, R., & Rüegger, H. (2012) · Dalton Transactions · doi:10.1039/c2dt31526b · Cited by 72
Activation of src tyrosine kinases by peroxynitrite
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Metadata
- Authors
- Bonini, M. G., Radi, R., Ferrer-Sueta, G., Ferreira, A. M. D. C., & Augusto, O.
- Affiliations
- Universidade de São Paulo (BR)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-04
- Volume
- 274
- Issue
- 16
- Pages
- 10802-10806
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2039241150
- Cited by
- 293
- References
- 39
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 6 · 2023: 3 · 2022: 5 · 2021: 4 · 2020: 9 · 2019: 10 · 2018: 9 · 2017: 8 · 2016: 8 · 2015: 6 · 2014: 8 · 2013: 8 · 2012: 13
- FWCI
- 14.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Electron Spin Resonance Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Keywords
- carbonate radical anion, peroxynitrite, carbon dioxide, bicarbonate, pH dependence, physiological pH, radical detection
- MeSH terms
- Carbon Dioxide, Carbonates, Electron Spin Resonance Spectroscopy, Free Radicals, Hydrogen-Ion Concentration, Nitrates
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