Cited by 118Free Radicals and AntioxidantsRedox biology and oxidative stressAntioxidant Activity and Oxidative Stress

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Radical–radical reactions of superoxide: a potential route to toxicity

Winterbourn, Christine C., Kettle, Anthony J.·2003·Biochemical and Biophysical Research Communications

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Abstract

Superoxide reacts with many radicals, such as phenoxyl radicals, at near diffusion-controlled rates. These reactions are usually considered to be repair processes and have received little biological attention. However, addition of superoxide to give hydroperoxides and secondary oxidation products can also occur. The relative contributions of addition and repair vary depending on the properties of the phenol. With tyrosine, addition to give tyrosine hydroperoxide predominates, but in peptides the efficiency of hydroperoxide formation depends on the proximity of free amine groups. Radicals from other phenolic compounds, such as alpha-tocopherol and serotonin, also undergo addition reactions with superoxide. Physiologically, these reactions are likely to be more significant than dimerization when both radicals are generated together. They warrant attention as potential contributors to superoxide toxicity.

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Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178
Superoxide Dismutase
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952
Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide
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
Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly
Beckman, J. S., & Koppenol, W. H. (1996) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1996.271.5.c1424 · Cited by 5,513
Free Radicals in Biology and Medicine
Land, E. J. (1990) · International Journal of Radiation Biology · doi:10.1080/09553009014552071 · Cited by 4,871
The reaction of NO with superoxide
Huie, R. E., & Padmaja, S. (1993) · Free Radical Research Communications · doi:10.3109/10715769309145868 · Cited by 2,121
Biochemistry and pathology of radical-mediated protein oxidation
Dean, R. T., Fu, S., Stocker, R., & Davies, M. J. (1997) · Biochemical Journal · doi:10.1042/bj3240001 · Cited by 1,678
Melatonin in Humans
Brzezinski, A. (1997) · New England Journal of Medicine · doi:10.1056/nejm199701163360306 · Cited by 1,549
Nitric oxide regulation of superoxide and peroxynitrite-dependent lipid peroxidation. Formation of novel nitrogen-containing oxidized lipid derivatives
Rubbo, H., Radí, R., Trujillo, M., Telleri, R., Kalyanaraman, B., Barnes, S., KIRK, M. C., & Freeman, B. Α. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47160-8 · Cited by 1,350
Myeloperoxidase: a key regulator of neutrophil oxidant production
Kettle, A. J., & Winterbourn, C. C. (1997) · Redox Report · doi:10.1080/13510002.1997.11747085 · Cited by 671
Self-citation
Peroxynitrite‐mediated oxidative protein modifications
Ischiropoulos, H., & Al‐Mehdi, A. B. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00307-u · Cited by 608
Peroxynitrite reaction with carbon dioxide/bicarbonate. Kinetics and influence on peroxynitrite-mediated oxidations
Denicola, A., Freeman, B. A., Trujillo, M., & Radi, R. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0363 · Cited by 593
Photo-oxidation of proteins and its role in cataractogenesis
Davies, M. J., & Truscott, R. J. W. (2001) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/s1011-1344(01)00208-1 · Cited by 446
Superoxide as an intracellular radical sink
Winterbourn, C. C. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90512-s · Cited by 364
Self-citation
Tyrosyl radical generated by myeloperoxidase catalyzes the oxidative cross-linking of proteins.
Heinecke, J. W., Li, W., Francis, G. A., & Goldstein, J. A. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116531 · Cited by 354
The basic chemistry of nitrogen monoxide and peroxynitrite
Koppenol, W. H. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00093-8 · Cited by 340
Formation of peroxides in amino acids and proteins exposed to oxygen free radicals
Gebicki, S., & Gebicki, J. M. (1993) · Biochemical Journal · doi:10.1042/bj2890743 · Cited by 305
Mechanism of carbon dioxide-catalyzed oxidation of tyrosine by peroxynitrite
Lymar, S. V., Jiang, Q., & Hurst, J. K. (1996) · Biochemistry · doi:10.1021/bi960331h · Cited by 299
Nitric Oxide Regulation of Superoxide and Peroxynitrite-dependent Lipid Peroxidation
KIRK, M. C., & Freeman, B. Α. (1994) · Cited by 270
Peroxidases
O'Brien, P. J. (2000) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(00)00201-5 · Cited by 264
Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plaque
Fu, S., Davies, M. J., Stocker, R., & Dean, R. T. (1998) · Biochemical Journal · doi:10.1042/bj3330519 · Cited by 256
Formation of dityrosine cross-links in proteins by oxidation of tyrosine residues
Aeschbach, R., Amadoò, R., & Neukom, H. (1976) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(76)90064-7 · Cited by 256
Nitric Oxide Inhibition of Lipid Peroxidation: Kinetics of Reaction with Lipid Peroxyl Radicals and Comparison with α-Tocopherol
O’Donnell, V. B., Chumley, P. H., Hogg, N., Bloodsworth, A., Darley-Usmar, V. M., & Freeman, B. Α. (1997) · Biochemistry · doi:10.1021/bi971891z · Cited by 253
Kinetics of Oxidation of Tyrosine and Dityrosine by Myeloperoxidase Compounds I and II
Marquez‐Curtis, L. A., & Dunford, H. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.51.30434 · Cited by 237
Reactions of Hindered Phenols. II. Base-Catalyzed Oxidations of Hindered Phenols*
Kharasch, M. S., & Joshi, B. S. (1957) · The Journal of Organic Chemistry · doi:10.1021/jo01362a034 · Cited by 230
Superoxide and iron: Partners in crime
Liochev, S. I., & Fridovich, I. (1999) · International Union of Biochemistry and Molecular Biology: Life · doi:10.1080/152165499307161 · Cited by 219
Singlet Oxygen-mediated Protein Oxidation: Evidence for the Formation of Reactive Side Chain Peroxides on Tyrosine Residues¶
Wright, A., Bubb, W. A., Hawkins, C. L., & Davies, M. J. (2002) · Photochemistry and Photobiology · doi:10.1562/0031-8655(2002)0760035sompoe2.0.co2 · Cited by 202
Platelets and inflammation
Klinger, M. H. F. (1997) · Anatomy and Embryology · doi:10.1007/s004290050075 · Cited by 201
The myoglobin protein radical. Coupling of Tyr-103 to Tyr-151 in the H2O2-mediated cross-linking of sperm whale myoglobin.
Tew, D. G., & de Montellano, P. R. O. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77915-0 · Cited by 181
Tyrosine Nitration by Simultaneous Generation of ⋅NO and O⨪2 under Physiological Conditions
Goldstein, S., Czapski, G., Lind, J., & Merényi, G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3031 · Cited by 177
Radical formation during the peroxidase catalyzed metabolism of carcinogens and xenobiotics: The reactivity of these radicals with GSH, DNA, and unsaturated lipid
O'Brien, P. J. (1988) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(88)90025-1 · Cited by 166
The effect of oxygen, antioxidants, and superoxide radical on tyrosine phenoxyl radical dimerization
Hunter, E. P. L., Desrosiers, M. F., & Simic, M. G. (1989) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(89)90064-6 · Cited by 153
Nitric oxide rapidly scavenges tyrosine and tryptophan radicals
Eiserich, J. P., Butler, J., van der Vliet, A., Cross, C. E., & Halliwell, B. B. (1995) · Biochemical Journal · doi:10.1042/bj3100745 · Cited by 151
Human Phagocytes Employ the Myeloperoxidase-Hydrogen Peroxide System to Synthesize Dityrosine, Trityrosine, Pulcherosine, and Isodityrosine by a Tyrosyl Radical-dependent Pathway
Jacob, J. S., Cistola, D. P., Hsu, F., Muzaffar, S., Mueller, D. M., Hazen, S. L., & Heinecke, J. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.33.19950 · Cited by 150
Glutathione-Dependent Generation of Reactive Oxygen Species by the Peroxidase-Catalyzed Redox Cycling of Flavonoids
Galati, G., Chan, T. S., Wu, B., & O'Brien, P. J. (1999) · Chemical Research in Toxicology · doi:10.1021/tx980271b · Cited by 148
The superoxide radical reacts with tyrosine-derived phenoxyl radicals by addition rather than by electron transfer
Jin, F., Leitich, J., & von Sonntag, C. (1993) · Journal of the Chemical Society Perkin Transactions 2 · doi:10.1039/p29930001583 · Cited by 146
Crosslinking of DNA and proteins induced by protein hydroperoxides
Gebicki, S., & Gebicki, J. M. (1999) · Biochemical Journal · doi:10.1042/bj3380629 · Cited by 127
Kinetic behavior and thermochemical properties of phenoxy radicals
Mahoney, L. R., & DaRooge, M. A. (1975) · Journal of the American Chemical Society · doi:10.1021/ja00849a039 · Cited by 124
Free radical combination reactions involving phenoxyl radicals
Jönsson, M., Lind, J., Reitberger, T., Eriksen, T. E., & Merényi, G. (1993) · The Journal of Physical Chemistry · doi:10.1021/j100133a018 · Cited by 117
Tyrosyl radical production by myeloperoxidase: a phagocyte pathway for lipid peroxidation and dityrosine cross-linking of proteins
Heinecke, J. W. (2002) · Toxicology · doi:10.1016/s0300-483x(02)00192-0 · Cited by 116
Neutrophil interactions with endothelium and platelets: possible role in the development of cardiovascular injury
SIMINIAK, T., Flores, N. A., & Sheridan, D. J. (1995) · European Heart Journal · doi:10.1093/oxfordjournals.eurheartj.a060880 · Cited by 111
Phenol Coupling Initiated by One-electron Oxidation of Tyrosine Units in Peptides and Histone
Prütz, W. A., Butler, J., & Land, E. J. (1983) · International Journal of Radiation Biology and Related Studies in Physics Chemistry and Medicine · doi:10.1080/09553008314550981 · Cited by 110
Eosinophil peroxidase produces hypobromous acid in the airways of stable asthmatics
Aldridge, R. E., Chan, T., van Dalen, C. J., Senthilmohan, R., WINN, M. C., Venge, P., Town, G. I., & Kettle, A. J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00976-0 · Cited by 109
Self-citation
Mechanism of the Formation and Proteolytic Release of H2O2-induced Dityrosine and Tyrosine Oxidation Products in Hemoglobin and Red Blood Cells
Giulivi, C., & Davies, K. J. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010697200 · Cited by 105
Oxidation of serotonin by superoxide radical: Implications to neurodegenerative brain disorders
Wrona, M. Z., & Dryhurst, G. (1998) · Chemical Research in Toxicology · doi:10.1021/tx970185w · Cited by 105
Defects in leukocyte-mediated initiation of lipid peroxidation in plasma as studied in myeloperoxidase-deficient subjects: systematic identification of multiple endogenous diffusible substrates for myeloperoxidase in plasma
Zhang, R., Shen, Z., Nauseef, W. M., & Hazen, S. L. (2002) · Blood · doi:10.1182/blood.v99.5.1802.h8001802_1802_1810 · Cited by 95
Detection and reactions of the globin radical in haemoglobin
McArthur, K. M., & Davies, M. J. (1993) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(93)90002-9 · Cited by 91
Inhibition of glyceraldehyde-3-phosphate dehydrogenase by peptide and protein peroxides generated by singlet oxygen attack
Morgan, P. E., Dean, R. T., & Davies, M. J. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.02845.x · Cited by 89
Biological fate of amino acid, peptide and protein hydroperoxides
Fu, S., Gebicki, S., Jessup, W., Gebicki, J. M., & Dean, R. T. (1995) · Biochemical Journal · doi:10.1042/bj3110821 · Cited by 88
Oxidized amino acids in the urine of aging rats: potential markers for assessing oxidative stress in vivo
Leeuwenburgh, C., Hansen, P. A., Holloszy, J. O., & Heinecke, J. W. (1999) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1999.276.1.r128 · Cited by 87
Modulation of cellular tryptophan metabolism in human fibroblasts by transforming growth factor-β: Selective inhibition of indoleamine 2,3-dioxygenase and tryptophanyl-tRNA synthetase gene expression
Yuan, W., Collado-Hidalgo, A., Yufit, T., Taylor, M. W., & Varga, J. (1998) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(199810)177:1 · Cited by 85
Myeloperoxidase-catalyzed oxidation of melatonin by activated neutrophils
de Oliveira Silva, S., Ximenes, V. F., Catalani, L. H., & Campa, A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3993 · Cited by 72
Myeloperoxidase-Dependent Generation of a Tyrosine Peroxide by Neutrophils
Winterbourn, C. C., Pichorner, H., & Kettle, A. J. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.9773 · Cited by 71
Self-citation
THE BETA-AGONIST CONTROVERSY
Taylor, D. R., Sears, M. R., & Cockcroft, D. W. (1996) · Medical Clinics of North America · doi:10.1016/s0025-7125(05)70465-x · Cited by 70
Generation of Superoxide and Tyrosine Peroxide as a Result of Tyrosyl Radical Scavenging by Glutathione
Pichorner, H., Metodiewa, D., & Winterbourn, C. C. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.0064 · Cited by 70
Self-citation
Inactivation of cellular caspases by peptide‐derived tryptophan and tyrosine peroxides
Hampton, M. B., Morgan, P. E., & Davies, M. J. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03240-4 · Cited by 61
Reaction of superoxide with phenoxyl-type radicals
d’Alessandro, N., Bianchi, G., Fang, X., Jin, F., Schuchmann, H., & von Sonntag, C. (2000) · Journal of the Chemical Society Perkin Transactions 2 · doi:10.1039/b003346o · Cited by 59
NADPH Oxidase of Neutrophils Elevates o,o′-Dityrosine Cross-Links in Proteins and Urine during Inflammation
Bhattacharjee, S., Pennathur, S., Byun, J., Crowley, J. R., Mueller, D. M., Gischler, J., Hotchkiss, R. S., & Heinecke, J. W. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2557 · Cited by 55
Quantitative Studies on the Peroxidation of Human Low-Density Lipoprotein Initiated by Superoxide and by Charged and Neutral Alkylperoxyl Radicals1
Bedard, L. L., Young, M. J., Hall, D., Paul, T., & Ingold, K. U. (2001) · Journal of the American Chemical Society · doi:10.1021/ja011076d · Cited by 52
Pulse radiolysis study on the reactivity of Trolox C phenoxyl radical with superoxide anion
Cadenas, E., Merényi, G., & Lind, J. U. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)80966-4 · Cited by 52
Reaction of the superoxide radical with the N-centered radical derived from N-acetyltryptophan methyl ester
Fang, X., Jin, F., Jin, H., & Sonntag, C. V. (1998) · Journal of the Chemical Society, Perkin Transactions 2 · doi:10.1039/a706979k · Cited by 51
Characterization of a Tyrosyl Radical in Prostaglandin Endoperoxide Synthase-2
Hsi, L. C., Hoganson, C. W., Babcock, Ǵ., & Smith, W. L. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.2114 · Cited by 46
Induction of DNA damage by oxidised amino acids and proteins
Luxford, C., Dean, R. T., & Davies, M. J. (2002) · Biogerontology · doi:10.1023/a:1015228001561 · Cited by 43
Tyrosine Iminoxyl Radical Formation from Tyrosyl Radical/Nitric Oxide and Nitrosotyrosine
Sturgeon, B. E., Glover, R. E., Chen, Y., Burka, L. T., & Mason, R. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106835200 · Cited by 40
Assays using horseradish peroxidase and phenolic substrates require superoxide dismutase for accurate determination of hydrogen peroxide production by neutrophils
Kettle, A. J., Carr, A. C., & Winterbourn, C. C. (1994) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)90111-2 · Cited by 39
Self-citation
The irreversible inactivation of ribonucleotide reductase from Escherichia coli by superoxide radicals
Gaudu, P., Nivière, V., Pétillot, Y., Kauppi, B., & Fontecave, M. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00480-2 · Cited by 37
Production and identification of bityrosine in horseradish peroxidase-H2O2-tyrosine system
Ushijima, Y., Nakano, M., & Goto, T. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)91370-6 · Cited by 33
Tryptamine-4,5-dione, a Putative Endotoxic Metabolite of the Superoxide-Mediated Oxidation of Serotonin, Is a Mitochondrial Toxin: Possible Implications in Neurodegenerative Brain Disorders
Jiang, X., Wrona, M. Z., & Dryhurst, G. (1999) · Chemical Research in Toxicology · doi:10.1021/tx9801615 · Cited by 32
Effectiveness of phenol antioxidants and the properties of quinolide peroxides
Roginskii, V. A., Dubinskii, V. Z., Shlyapnikova, I. A., & Miller, V. B. (1977) · European Polymer Journal · doi:10.1016/0014-3057(77)90178-1 · Cited by 29
Effects of β2-agonists on airway tone and bronchial responsiveness
Larj, M. J., & Bleecker, E. R. (2002) · Journal of Allergy and Clinical Immunology · doi:10.1067/mai.2002.130045 · Cited by 28
Submolecular adventures of brain tyrosine: what are we searching for now?
Kochman, A., Kośka, C., & Metodiewa, D. (2002) · Amino Acids · doi:10.1007/s00726-001-0114-6 · Cited by 24
Oxidation of Human α-Thrombin by the Myeloperoxidase-H2O2-chloride System: Structural and Functional Effects
Landolfi, R., & Cristofaro, R. D. (2000) · Thrombosis and Haemostasis · doi:10.1055/s-0037-1613796 · Cited by 24
The β-Agonist Controversy
Ziment, I. (1995) · CHEST Journal · doi:10.1378/chest.107.5_supplement.198s · Cited by 23
Drug derived radicals: mediators of the side effects of anti-inflammatory drugs?
Halliwell, B. B., Evans, P., Kaur, H., & Chirico, S. (1992) · Annals of the Rheumatic Diseases · doi:10.1136/ard.51.11.1261 · Cited by 19
Nitric oxide: a radical molecule in quest of free radicals in proteins
Guittet, O., Roy, B., & Lepoivre, M. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050356 · Cited by 19
ChemInform Abstract: THE KINETIC BEHAVIOR AND THERMOCHEMICAL PROPERTIES OF PHENOXY RADICALS
Mahoney, L. R., & DaRooge, M. A. (1975) · ChemInform · doi:10.1002/chin.197542077 · Cited by 6

Research works printed but not linked: 1

S. Hoskin, Oxidation of β-agonists. B. Med. Sci. thesis, University of Otago, 2002

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Authors: Winterbourn, C. C., & Kettle, A. J.
Corresponding author: Winterbourn, Christine C.
ORCID: Winterbourn, Christine C.
Kettle, Anthony J.
Venue: Biochemical and Biophysical Research Communications
Publisher: Elsevier BV
Published: 2003-06
Volume: 305
Issue: 3
Pages: 729-736
ISSN: 0006-291X (ISSN-L)
DOI: 10.1016/s0006-291x(03)00810-6
OpenAlex: W1967305386
Cited by: 118
References: 76
Citations by year: 2026: 3 · 2025: 2 · 2024: 2 · 2023: 6 · 2022: 2 · 2021: 7 · 2020: 3 · 2019: 3 · 2018: 2 · 2017: 4 · 2016: 3 · 2015: 6 · 2014: 10 · 2013: 4 · 2012: 8
FWCI: 4.92
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Biochemical and Biophysical Research Communications (publishedVersion)
PubMed (publishedVersion)
Funders: Health Research Council of New Zealand
Topics: Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
Keywords: superoxide, phenoxyl radicals, radical-radical reactions, hydroperoxide formation, phenol oxidation, alpha-tocopherol, serotonin, radical dimerization, diffusion-controlled reaction
MeSH terms: Animals, Free Radicals, Indoles, Models, Chemical, Nitric Oxide, Peptides, Peroxides, Phenols, Proteins, Superoxides, Tyrosine, Vitamin E

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Radical–radical reactions of superoxide: a potential route to toxicity

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