Reconciling the chemistry and biology of reactive oxygen species
Abstract
There is a vast literature on the generation and effects of reactive oxygen species in biological systems, both in relation to damage they cause and their involvement in cell regulatory and signaling pathways. The biological chemistry of different oxidants is becoming well understood, but it is often unclear how this translates into cellular mechanisms where redox changes have been demonstrated. This review addresses this gap. It examines how target selectivity and antioxidant effectiveness vary for different oxidants. Kinetic considerations of reactivity are used to assess likely targets in cells and how reactions might be influenced by restricted diffusion and compartmentalization. It also highlights areas where greater understanding is required on the fate of oxidants generated by cellular NADPH oxidases and on the identification of oxidant sensors in cell signaling.
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UV light may indirectly cause DNA damage via production of singlet oxygen or free radicals in photodynamic reactions.
“UV light may also indirectly cause DNA damage via production of singlet oxygen or free radicals in photodynamic reactions.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [21]
Cites
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 · see citing works
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952 · see citing works
Free Radicals in Biology and Medicine
Halliwell, B., & Gutteridge, J. M. C. (2015) · doi:10.1093/acprof:oso/9780198717478.001.0001 · Cited by 8,990 · see citing works
Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
Esterbauer, H., Schaur, R. J., & Zollner, H. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90192-6 · Cited by 6,672 · see citing works
ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
D'Autréaux, B., & Toledano, M. B. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2256 · Cited by 3,642 · see citing works
NOX enzymes and the biology of reactive oxygen
Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125 · see citing works
Structure, mechanism and regulation of peroxiredoxins
Wood, Z. A., Schröder, E., Harris, J. R., & Poole, L. B. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)00003-8 · Cited by 2,546 · see citing works
The Pecking Order of Free Radicals and Antioxidants: Lipid Peroxidation, α-Tocopherol, and Ascorbate
Buettner, G. R. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1074 · Cited by 2,417 · see citing works
Myeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282 · see citing works
Imlay, J. A. (2003) · Annual Review of Microbiology · doi:10.1146/annurev.micro.57.030502.090938 · Cited by 2,206 · see citing works
H <sub>2</sub> O <sub>2</sub> , a Necessary Evil for Cell Signaling
Rhee, S. G. (2006) · Science · doi:10.1126/science.1130481 · Cited by 2,160 · see citing works
Peroxynitrite: biochemistry, pathophysiology and development of therapeutics
Szabó, C., Ischiropoulos, H., & Radi, R. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2222 · Cited by 2,134 · see citing works
Antimicrobial reactive oxygen and nitrogen species: concepts and controversies
Fang, F. C. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro1004 · Cited by 1,676 · see citing works
Hydrogen peroxide sensing and signaling
Veal, E. A., Day, A. M., & Morgan, B. A. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.016 · Cited by 1,604 · see citing works
Oxidant signals and oxidative stress
Finkel, T. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00002-4 · Cited by 1,393 · see citing works
Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling
Wood, Z. A., Poole, L. B., & Karplus, P. A. (2003) · Science · doi:10.1126/science.1080405 · Cited by 1,369 · see citing works
Genetically encoded fluorescent indicator for intracellular hydrogen peroxide
Belousov, V. V., Fradkov, A. F., Lukyanov, K. A., Staroverov, D. B., Shakhbazov, K., Terskikh, A. V., & Lukyanov, S. (2006) · Nature Methods · doi:10.1038/nmeth866 · Cited by 1,260 · see citing works
Activation of the OxyR Transcription Factor by Reversible Disulfide Bond Formation
Zheng, M., Åslund, F., & Storz, G. (1998) · Science · doi:10.1126/science.279.5357.1718 · Cited by 1,197 · see citing works
Hydrogen Peroxide: A Signaling Messenger
Stone, J. R., & Yang, S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.243 · Cited by 1,175 · see citing works
Killing activity of neutrophils is mediated through activation of proteases by K+ flux
Reeves, E. P., Lu, H., Jacobs, H. L., Messina, C. G. M., Bolsover, S., Gabella, G., Potma, E. O., Warley, A., Roes, J., & Segal, A. W. (2002) · Nature · doi:10.1038/416291a · Cited by 1,153 · see citing works
Galati, G., & O'Brien, P. J. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.04.034 · Cited by 1,101 · see citing works
Molecular mechanisms of quinone cytotoxicity
O'Brien, P. J. (1991) · Chemico-Biological Interactions · doi:10.1016/0009-2797(91)90029-7 · Cited by 1,031 · see citing works
Denu, J. M., & Tanner, K. G. (1998) · Biochemistry · doi:10.1021/bi973035t · Cited by 945 · see citing works
Transcriptional Regulator of Oxidative Stress-Inducible Genes: Direct Activation by Oxidation
Storz, G., Tartaglia, L. A., & Ames, B. N. (1990) · Science · doi:10.1126/science.2183352 · Cited by 864 · see citing works
Wardman, P. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.06.026 · Cited by 863 · see citing works
Superoxide accelerates DNA damage by elevating free-iron levels
Keyer, K., & Imlay, J. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13635 · Cited by 841 · see citing works
Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
Winterbourn, C. C., & Metodiewa, D. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00051-9 · Cited by 799 · see citing works
Self-citationPattison, D. I., & Davies, M. J. (2001) · Chemical Research in Toxicology · doi:10.1021/tx0155451 · Cited by 790 · see citing works
How human neutrophils kill and degrade microbes: an integrated view
Nauseef, W. M. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00550.x · Cited by 756 · see citing works
Redox Redux: Revisiting PTPs and the Control of Cell Signaling
Tonks, N. K. (2005) · Cell · doi:10.1016/j.cell.2005.05.016 · Cited by 702 · see citing works
Reactive nitrogen species in the chemical biology of inflammation
Dedon, P. C., & Tannenbaum, S. R. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.12.017 · Cited by 676 · see citing works
Hydrogen Peroxide: A Key Messenger That Modulates Protein Phosphorylation Through Cysteine Oxidation
Rhee, S. G., Bae, Y. S., Lee, S.-R., & Kwon, J. (2000) · Science s STKE · doi:10.1126/stke.2000.53.pe1 · Cited by 646 · see citing works
The inactivation of Fe-S cluster containing hydro-lyases by superoxide
Flint, D. H., Tuminello, J. F., & Emptage, M. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41538-4 · Cited by 637 · see citing works
Modeling the Reactions of Superoxide and Myeloperoxidase in the Neutrophil Phagosome
Winterbourn, C. C., Hampton, M. B., Livesey, J. H., & Kettle, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605898200 · Cited by 634 · see citing works
Self-citationKwon, J., Lee, S.-R., Yang, K.-S., Ahn, Y., Kim, Y. J., Stadtman, E. R., & Rhee, S. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407396101 · Cited by 631 · see citing works
Kissner, R., Nauser, T., Bugnon, P., Lye, P. G., & Koppenol, W. H. (1997) · Chemical Research in Toxicology · doi:10.1021/tx970160x · Cited by 629 · see citing works
Protein Sulfenic Acids in Redox Signaling
Poole, L. B., Karplus, P. A., & Claiborne, A. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.44.101802.121735 · Cited by 598 · see citing works
Åslund, F., Zheng, M., Beckwith, J., & Storz, G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6161 · Cited by 586 · see citing works
Zhao, H., Joseph, J., Fales, H. M., Sokoloski, E. A., Levine, R. L., Vasquez-Vivar, J., & Kalyanaraman, B. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501719102 · Cited by 576 · see citing works
Structural Basis of the Redox Switch in the OxyR Transcription Factor
Choi, H., Kim, S.-J., Mukhopadhyay, P., Cho, S., Woo, J.-R., Storz, G., & Ryu, S.-E. (2001) · Cell · doi:10.1016/s0092-8674(01)00300-2 · Cited by 560 · see citing works
Methods of Detection of Vascular Reactive Species
Tarpey, M. M., & Fridovich, I. (2001) · Circulation Research · doi:10.1161/hh1501.094365 · Cited by 552 · see citing works
Quantifying changes in the thiol redox proteome upon oxidative stress in vivo
Leichert, L. I. O., Gehrke, F., Gudiseva, H. V., Blackwell, T. W., Ilbert, M., Walker, A. K., Strahler, J. R., Andrews, P., & Jakob, U. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707723105 · Cited by 520 · see citing works
Superoxide sensitivity of the Escherichia coli aconitase.
Gardner, P. R., & Fridovich, I. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55001-8 · Cited by 514 · see citing works
Mahadev, K., Motoshima, H., Wu, X., Ruddy, J. M., Arnold, R. S., Cheng, G., Lambeth, J. D., & Goldstein, B. J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.5.1844-1854.2004 · Cited by 513 · see citing works
Vitamin E in human low-density lipoprotein. When and how this antioxidant becomes a pro-oxidant
Bowry, V. W., Ingold, K. U., & Stocker, R. (1992) · Biochemical Journal · doi:10.1042/bj2880341 · Cited by 511 · see citing works
Estimation of H 2 O 2 gradients across biomembranes
Antunes, F., & Cadenas, E. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01638-0 · Cited by 498 · see citing works
The NADPH oxidase of professional phagocytes—prototype of the NOX electron transport chain systems
Cross, A. R., & Segal, A. W. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.03.008 · Cited by 489 · see citing works
Winterbourn, C. C. (1985) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(85)90120-5 · Cited by 463 · see citing works
Self-citationKenmoku, S., Urano, Y., Kojima, H., & Nagano, T. (2007) · Journal of the American Chemical Society · doi:10.1021/ja068740g · Cited by 462 · see citing works
Specificity of a third kind: reactive oxygen and nitrogen intermediates in cell signaling
Nathan, C. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200318174 · Cited by 455 · see citing works
Molecular imaging of hydrogen peroxide produced for cell signaling
Miller, E. W., Tulyathan, O., Isacoff, E. Y., & Chang, C. J. (2007) · Nature Chemical Biology · doi:10.1038/nchembio871 · Cited by 450 · see citing works
The role of O2.− in the production of HO.: in vitro and in vivo
Liochev, S. I., & Fridovich, I. (1994) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)90239-9 · Cited by 423 · see citing works
Zielonka, J., Vasquez-Vivar, J. M., & Kalyanaraman, B. (2007) · Nature Protocols · doi:10.1038/nprot.2007.473 · Cited by 421 · see citing works
Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II
Choi, M. H., Lee, I. K., Kim, G. W., Kim, B. U., Han, Y.-H., Yu, D.-Y., Park, H. S., Kim, K. Y., Lee, J. S., Choi, C., et al. (2005) · Nature · doi:10.1038/nature03587 · Cited by 403 · see citing works
Redox-operated genetic switches: the SoxR and OxyR transcription factors
Pomposiello, P. J., & Demple, B. (2001) · Trends in biotechnology · doi:10.1016/s0167-7799(00)01542-0 · Cited by 403 · see citing works
Peskin, A. V., Low, F. M., Paton, L. N., Maghzal, G. J., Hampton, M. B., & Winterbourn, C. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700339200 · Cited by 394 · see citing works
Self-citationBiomarkers of myeloperoxidase-derived hypochlorous acid
Winterbourn, C. C., & Kettle, A. J. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00204-5 · Cited by 390 · see citing works
Self-citationTolédano, M. B., Kullik, I., Trinh, F., Baird, P. T., Schneider, T. D., & Storz, G. (1994) · Cell · doi:10.1016/s0092-8674(94)90702-1 · Cited by 389 · see citing works
Localizing NADPH Oxidase–Derived ROS
Ushio‐Fukai, M. (2006) · Science s STKE · doi:10.1126/stke.3492006re8 · Cited by 387 · see citing works
The reduction potential of nitric oxide (NO) and its importance to NO biochemistry
Bartberger, M. D., Liu, W., Ford, E., Miranda, K. M., Switzer, C., Fukuto, J. M., Farmer, P. J., Wink, D. A., & Houk, K. N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162095599 · Cited by 384 · see citing works
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 365 · see citing works
Self-citationPattison, D. I., & Davies, M. J. (2006) · Current Medicinal Chemistry · doi:10.2174/092986706778773095 · Cited by 359 · see citing works
Micromolar Intracellular Hydrogen Peroxide Disrupts Metabolism by Damaging Iron-Sulfur Enzymes
Jang, S., & Imlay, J. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607646200 · Cited by 353 · see citing works
Nox4 Is Required for Maintenance of the Differentiated Vascular Smooth Muscle Cell Phenotype
Clempus, R. E., Sorescu, D., Dikalova, A., Pounkova, L., Jo, P. C., Sorescu, G. P., Lassegue, B. P., & Griendling, K. K. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000251500.94478.18 · Cited by 334 · see citing works
Environmental-Dependent Acceleration of a Developmental Switch: The Floral Transition
Simpson, G. G., & Dean, C. (2000) · Science s STKE · doi:10.1126/stke.2000.18.pe1 · Cited by 318 · see citing works
Living with a Killer: The Effects of Hypochlorous Acid on Mammalian Cells
Pullar, J. M., Vissers, M. C. M., & Winterbourn, C. C. (2000) · IUBMB Life · doi:10.1080/713803731 · Cited by 315 · see citing works
Self-citationAdachi, T. K., Pimentel, D. R., Heibeck, T. H., Hou, X., Lee, Y. J., Jiang, B., Ido, Y., & Cohen, R. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313320200 · Cited by 301 · see citing works
Endogenous Reactive Intermediates as Modulators of Cell Signaling and Cell Death
West, J. D., & Marnett, L. J. (2006) · Chemical Research in Toxicology · doi:10.1021/tx050321u · Cited by 293 · see citing works
alpha, beta-Dihydroxyisovalerate dehydratase. A superoxide-sensitive enzyme.
Kuo, C. F., Mashino, T., & Fridovich, I. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61255-4 · Cited by 247 · see citing works
Ford, E., Hughes, M., & Wardman, P. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00850-x · Cited by 229 · see citing works
The oxidation of 2′,7′-dichlorofluorescin to reactive oxygen species: A self-fulfilling prophesy?
Bonini, M. G., Rota, C., Tomasi, A., & Mason, R. P. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.10.042 · Cited by 223 · see citing works
Fessel, J. P., Porter, N. A., Moore, K. P., Sheller, J. R., & Roberts, L. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252649099 · Cited by 219 · see citing works
Lancaster, J. R. (2006) · Chemical Research in Toxicology · doi:10.1021/tx060061w · Cited by 219 · see citing works
Zheng, L., Settle, M., Brubaker, G., Schmitt, D., Hazen, S. L., Smith, J. D., & Kinter, M. T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407019200 · Cited by 206 · see citing works
[3] Kinetic factors that control the fate of thiyl radicals in cells
Wardman, P., & von Sonntag, C. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)51108-3 · Cited by 204 · see citing works
The carbonate radical and related oxidants derived from bicarbonate buffer
Medinas, D. B., Cerchiaro, G., Trindade, D. F., & Augusto, O. (2007) · IUBMB Life · doi:10.1080/15216540701230511 · Cited by 198 · see citing works
Ogusucu, R., Rettori, D., Munhoz, D. C., Netto, L. E. S., & Augusto, O. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.10.042 · Cited by 196 · see citing works
An assessment of proposed mechanisms for sensing hydrogen peroxide in mammalian systems
Stone, J. R. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.12.029 · Cited by 192 · see citing works
Vila, A., Tallman, K. A., Jacobs, A. T., Liebler, D. C., Porter, N. A., & Marnett, L. J. (2008) · Chemical Research in Toxicology · doi:10.1021/tx700347w · Cited by 192 · see citing works
Bonini, M. G., & Augusto, O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008456200 · Cited by 191 · see citing works
Superoxide Flux in Endothelial Cells via the Chloride Channel-3 Mediates Intracellular Signaling
Hawkins, B. J., Madesh, M., Kirkpatrick, C. J., & Fisher, A. B. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-09-0830 · Cited by 184 · see citing works
Catalytic and Chemical Competence of Regulation of Cdc25 Phosphatase by Oxidation/Reduction
Sohn, J., & Rudolph, J. (2003) · Biochemistry · doi:10.1021/bi0345081 · Cited by 183 · see citing works
Free-Radical Production and Oxidative Reactions of Hemoglobin
Winterbourn, C. C. (1985) · Environmental Health Perspectives · doi:10.1289/ehp.8564321 · Cited by 182 · see citing works
Self-citationUse and abuse of exogenous H2O2 in studies of signal transduction
Forman, H. J. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.01.011 · Cited by 182 · see citing works
Roos, D., & Winterbourn, C. C. (2002) · Science · doi:10.1126/science.1071271 · Cited by 170 · see citing works
Self-citationFluorescent probes for nitric oxide and hydrogen peroxide in cell signaling
Miller, E. W., & Chang, C. J. (2007) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2007.09.018 · Cited by 168 · see citing works
O'Brien, P. J. (1988) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(88)90025-1 · Cited by 166 · see citing works
Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin
Parsonage, D., Karplus, P. A., & Poole, L. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708308105 · Cited by 164 · see citing works
Proteomic detection of hydrogen peroxide-sensitive thiol proteins in Jurkat cells
Baty, J. W., Hampton, M. B., & Winterbourn, C. C. (2005) · Biochemical Journal · doi:10.1042/bj20050337 · Cited by 159 · see citing works
Self-citationBurkitt, M. J., & Wardman, P. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4578 · Cited by 154 · see citing works
Charge compensation during the phagocyte respiratory burst
Murphy, R., & DeCoursey, T. E. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.01.005 · Cited by 151 · see citing works
Kinetics of Peroxiredoxins and their Role in the Decomposition of Peroxynitrite
Trujillo, M., Ferrer‐Sueta, G., Thomson, L., Flohé, L., & Radí, R. (2007) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4020-6051-9_5 · Cited by 140 · see citing works
Srinivasan, C., Liba, A., Imlay, J. A., Valentine, J. S., & Gralla, E. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004239200 · Cited by 134 · see citing works
Sharov, V. S., Dremina, E. S., Galeva, N. A., Williams, T. D., & Schöneich, C. (2006) · Biochemical Journal · doi:10.1042/bj20051214 · Cited by 121 · see citing works
Diffusion of free nitric oxide
Lancaster, J. R. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)68007-0 · Cited by 118 · see citing works
Yao, Y., Yin, D., Jas, G. S., et al. (1996) · Biochemistry · doi:10.1021/bi951712i · Cited by 113 · see citing works
Oxidative lipidomics of γ-irradiation-induced intestinal injury
Tyurina, Y. Y., Tyurin, V. A., Epperly, M. W., Greenberger, J. S., & Kagan, V. E. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.08.021 · Cited by 86 · see citing works
The Fate of the Oxidizing Tyrosyl Radical in the Presence of Glutathione and Ascorbate
Sturgeon, B. E., Sipe, H. J., Barr, D. P., Corbett, J. T., Martinez, J. G., & Mason, R. P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.46.30116 · Cited by 86 · see citing works
Mass spectrometry of protein modifications by reactive oxygen and nitrogen species
Schöneich, C., & Sharov, V. S. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.08.013 · Cited by 85 · see citing works
Nox regulation of smooth muscle contraction
Ritsick, D. R., Edens, W. A., Finnerty, V., & Lambeth, J. D. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.006 · Cited by 67 · see citing works
Sethuraman, M., Clavreul, N., Huang, H., et al. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.12.012 · Cited by 66 · see citing works
Peskin, A. V., & Winterbourn, C. C. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00502-1 · Cited by 60 · see citing works
Self-citationBrown, O. R., & Yein, F. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)90672-1 · Cited by 60 · see citing works
Amino acid and protein oxidation in cardiovascular disease
Brennan, M., & Hazen, S. L. (2003) · Amino Acids · doi:10.1007/s00726-003-0023-y · Cited by 56 · see citing works
Nitric Oxide, Oxygen, and Superoxide Formation and Consumption in Macrophage Cultures
Nalwaya, N., & Deen, W. M. (2005) · Chemical Research in Toxicology · doi:10.1021/tx049879c · Cited by 56 · see citing works
Davies, S. S., Zackert, W. E., Luo, L. Y., et al. (2005) · Analytical Biochemistry · doi:10.1016/j.ab.2005.10.012 · Cited by 48 · see citing works
Ascorbate interacts with reduced glutathione to scavenge phenoxyl radicals in HL60 cells
Cuddihy, S. L., Parker, A. K., Harwood, D. T., Vissers, M. C. M., & Winterbourn, C. C. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.01.021 · Cited by 34 · see citing works
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Kamaly, N., Yameen, B., Wu, J., & Farokhzad, O. C. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00346 · Cited by 3,070 · see citing works
Mechanisms of DNA damage, repair, and mutagenesis
Chatterjee, N., & Walker, G. C. (2017) · Environmental and Molecular Mutagenesis · doi:10.1002/em.22087 · Cited by 2,039 · see citing works
Chemistry and biology of reactive oxygen species in signaling or stress responses
Dickinson, B. C., & Chang, C. J. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.607 · Cited by 1,821 · see citing works
Defining roles of specific reactive oxygen species (ROS) in cell biology and physiology
Sies, H., Belousov, V. V., Chandel, N. S., Davies, M. J., Jones, D. P., Mann, G. E., Murphy, M. P., Yamamoto, M., & Winterbourn, C. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00456-z · Cited by 1,735 · see citing works
Self-citationThe role of oxidative stress in neurodegenerative diseases
Kim, G. H., Kim, J. E., Rhie, S. J., & Yoon, S. (2015) · Experimental Neurobiology · doi:10.5607/en.2015.24.4.325 · Cited by 1,355 · see citing works
Thiol chemistry and specificity in redox signaling
Winterbourn, C. C., & Hampton, M. B. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.004 · Cited by 1,226 · see citing works
Self-citation13 reasons why the brain is susceptible to oxidative stress
Cobley, J. N., Fiorello, M. L., & Bailey, D. M. (2018) · Redox Biology · doi:10.1016/j.redox.2018.01.008 · Cited by 1,215 · see citing works
Oxygen radicals, nitric oxide, and peroxynitrite: Redox pathways in molecular medicine
Radi, R. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1804932115 · Cited by 1,142 · see citing works
The basics of thiols and cysteines in redox biology and chemistry
Poole, L. B. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.11.013 · Cited by 1,031 · see citing works
DNA Base Damage by Reactive Oxygen Species, Oxidizing Agents, and UV Radiation
Cadet, J., & Wagner, J. R. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012559 · Cited by 903 · see citing works
Unraveling the biological roles of reactive oxygen species
Murphy, M. P., Holmgren, A., Larsson, N.-G., Halliwell, B., Chang, C. J., Kalyanaraman, B., Rhee, S. G., Thornalley, P. J., Partridge, L., Gems, D., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.010 · Cited by 836 · see citing works
Self-citationNADPH Oxidases (NOX): An Overview from Discovery, Molecular Mechanisms to Physiology and Pathology
Vermot, A., Petit-Härtlein, I., Smith, S. M. E., & Fieschi, F. (2021) · Antioxidants · doi:10.3390/antiox10060890 · Cited by 766 · see citing works
Metzler, K. D., Goosmann, C., Lubojemska, A., Zychlinsky, A., & Papayannopoulos, V. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.06.044 · Cited by 741 · see citing works
T cell lipid peroxidation induces ferroptosis and prevents immunity to infection
Matsushita, M., Freigang, S., Schneider, C., Conrad, M., Bornkamm, G. W., & Kopf, M. (2015) · Journal of Experimental Medicine · doi:10.1084/jem.20140857 · Cited by 672 · see citing works
“Indeed, RAS–RAF–MEK signaling has been shown to be required for erastin-induced ferroptosis of tumor cells (Yagoda et al., 2007).”
BackgroundNox4 Is a Protective Reactive Oxygen Species Generating Vascular NADPH Oxidase
Schröder, K., Zhang, M., Benkhoff, S., Mieth, A., Pliquett, R., Kosowski, J., Kruse, C., Luedike, P., Michaelis, U. R., Weissmann, N., et al. (2012) · Circulation Research · doi:10.1161/circresaha.112.267054 · Cited by 622 · see citing works
Kaempferol and inflammation: from chemistry to medicine
Devi, K. P., Malar, D. S., Nabavi, S. F., Sureda, A., Xiao, J., Nabavi, S. M., & Daglia, M. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.05.002 · Cited by 619 · see citing works
Taking a good look at free radicals in the aging process
Hekimi, S., Lapointe, J., & Wen, Y. (2011) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.06.008 · Cited by 606 · see citing works
Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides
Rhee, S. G., Woo, H. A., Kil, I. S., & Bae, S. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.283432 · Cited by 603 · see citing works
Ageing, age-related diseases and oxidative stress: What to do next?
Luo, J., Mills, K., le Cessie, S., Noordam, R., & van Heemst, D. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100982 · Cited by 581 · see citing works
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · see citing works
Shields, H. J., Traa, A., & Van Raamsdonk, J. M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.628157 · Cited by 478 · see citing works
Redox Reactions and Microbial Killing in the Neutrophil Phagosome
Winterbourn, C. C., & Kettle, A. J. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4827 · Cited by 468 · see citing works
Self-citationMammalian Mitochondrial Complex I: Biogenesis, Regulation, and Reactive Oxygen Species Generation
Koopman, W. J. H., Nijtmans, L. G. J., Dieteren, C. E. J., Roestenberg, P., Valsecchi, F., Smeitink, J. A. M., & Willems, P. H. G. M. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2743 · Cited by 411 · see citing works
Dicarbonyl stress in cell and tissue dysfunction contributing to ageing and disease
Rabbani, N., & Thornalley, P. J. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.01.140 · Cited by 353 · see citing works
Kundu, K., Knight, S. F., Willett, N., Lee, S., Taylor, W. R., & Murthy, N. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200804851 · Cited by 339 · see citing works
Reactive oxygen species and fibrosis: further evidence of a significant liaison
Richter, K., & Kietzmann, T. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2445-3 · Cited by 322 · see citing works
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 · see citing works
Oxidative and nitrosative stress in Parkinson's disease
Tsang, A. H. K., & Chung, K. K. K. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.12.006 · Cited by 300 · see citing works
The sirtuins, oxidative stress and aging: an emerging link
Merksamer, P. I., Liu, Y., He, W., Hirschey, M. D., Chen, D., & Verdin, E. (2013) · Aging · doi:10.18632/aging.100544 · Cited by 275 · see citing works
T cells and reactive oxygen species
Belikov, A. V., Schraven, B., & Simeoni, L. (2015) · Journal of Biomedical Science · doi:10.1186/s12929-015-0194-3 · Cited by 264 · see citing works
Functions, Therapeutic Applications, and Synthesis of Retinoids and Carotenoids
Álvarez, R., Vaz, B., Gronemeyer, H., & de Lera, Á. R. (2014) · Chemical Reviews · doi:10.1021/cr400126u · Cited by 260 · see citing works
Banana peels as a bioactive ingredient and its potential application in the food industry
Mohd Zaini, H., Roslan, J., Saallah, S., Munsu, E., Sulaiman, N. S., & Pindi, W. (2022) · Journal of Functional Foods · doi:10.1016/j.jff.2022.105054 · Cited by 259 · see citing works
Ulfig, A., & Leichert, L. I. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03591-y · Cited by 239 · see citing works
Requejo, R., Hurd, T. R., Costa, N. J., & Murphy, M. P. (2010) · The FEBS Journal · doi:10.1111/j.1742-4658.2010.07576.x · Cited by 231 · see citing works
Oxidative stress and antioxidants: Distress or eustress?
Niki, E. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.11.017 · Cited by 209 · see citing works
Hurd, T. R., Requejo, R., Filipovska, A., Brown, S., Prime, T. A., Robinson, A. J., Fearnley, I. M., & Murphy, M. P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803432200 · Cited by 182 · see citing works
Detection of superoxide anion and hydrogen peroxide production by cellular NADPH oxidases
Nauseef, W. M. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.04.040 · Cited by 180 · see citing works
Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies
Kciuk, M., Marciniak, B., Mojzych, M., & Kontek, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197264 · Cited by 168 · see citing works
“One of the most reactive oxygen species (ROS) is hydroxyl radical (OH*), with its high DNA damaging capacity [21].”
BackgroundCadet, J., & Wagner, J. R. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.05.001 · Cited by 169 · see citing works
Dicarbonyls and glyoxalase in disease mechanisms and clinical therapeutics
Rabbani, N., Xue, M., & Thornalley, P. J. (2016) · Glycoconjugate Journal · doi:10.1007/s10719-016-9705-z · Cited by 169 · see citing works
Fungal antioxidant pathways promote survival against neutrophils during infection
Leal, S. M., Vareechon, C., Cowden, S., Cobb, B. A., Latgé, J.-P., Momany, M., & Pearlman, E. (2012) · Journal of Clinical Investigation · doi:10.1172/jci63239 · Cited by 146 · see citing works
Jiang, Z., Rompala, G. R., Zhang, S., Cowell, R. M., & Nakazawa, K. (2013) · Biological Psychiatry · doi:10.1016/j.biopsych.2012.12.004 · Cited by 128 · see citing works
Influence of vitamin C and vitamin E on redox signaling: implications for exercise adaptations
Cobley, J. N., McHardy, H., Morton, J. P., Nikolaidis, M. G., & Close, G. L. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.03.018 · Cited by 118 · see citing works
Leal, S. M., Roy, S., Vareechon, C., Carrion, S. D., Clark, H., Lopez-Berges, M. S., diPietro, A., Schrettl, M., Beckmann, N., Redl, B., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003436 · Cited by 111 · see citing works
Nrf2 promotes survival following exposure to ionizing radiation
Sekhar, K. R., & Freeman, M. L. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.04.035 · Cited by 109 · see citing works
Topical hypochlorite ameliorates NF-κB–mediated skin diseases in mice
Leung, T. H., Zhang, L. F., Wang, J., Ning, S., Knox, S. J., & Kim, S. K. (2013) · Journal of Clinical Investigation · doi:10.1172/jci70895 · Cited by 107 · see citing works
The Plasma Membrane: A Platform for Intra- and Intercellular Redox Signaling
Nordzieke, D. E., & Medraño-Fernandez, I. (2018) · Antioxidants · doi:10.3390/antiox7110168 · Cited by 90 · see citing works
Wlaschek, M., Singh, K., Sindrilaru, A., Crisan, D., & Scharffetter-Kochanek, K. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.036 · Cited by 76 · see citing works
“reactivity and low diffusion distance [30,31] is difficult in vivo.”
BackgroundMunnamalai, V., Weaver, C. J., Weisheit, C. E., Venkatraman, P., Agim, Z. S., Quinn, M. T., & Suter, D. M. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12734 · Cited by 70 · see citing works
ROS-Activated Ratiometric Fluorescent Polymeric Nanoparticles for Self-Reporting Drug Delivery
Zhang, M., Song, C.-C., Su, S., Du, F.-S., & Li, Z.-C. (2018) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.7b18438 · Cited by 64 · see citing works
Vitamin C Deficiency Causes Muscle Atrophy and a Deterioration in Physical Performance
Takisawa, S., Funakoshi, T., Yatsu, T., Nagata, K., Aigaki, T., Machida, S., & Ishigami, A. (2019) · Scientific Reports · doi:10.1038/s41598-019-41229-7 · Cited by 63 · see citing works
Schröter, J., & Schiller, J. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/8386362 · Cited by 51 · see citing works
Heme proteins in lactic acid bacteria
Baureder, M., & Hederstedt, L. (2013) · Advances in Microbial Physiology · doi:10.1016/b978-0-12-410515-7.00001-9 · Cited by 45 · see citing works
Jirapanjawat, T., Ney, B., Taylor, M. C., Warden, A. C., Afroze, S., Russell, R. J., Lee, B. M., Jackson, C. J., Oakeshott, J. G., Pandey, G., et al. (2016) · Applied and Environmental Microbiology · doi:10.1128/aem.02500-16 · Cited by 45 · see citing works
Versatile fluorescent probes for imaging the superoxide anion in living cells and in vivo
Xiao, H., Zhang, W., Li, P., Zhang, W., Wang, X., & Tang, B. (2020) · Angewandte Chemie · doi:10.1002/ange.201906793 · Cited by 45 · see citing works
Frijhoff, J., Dagnell, M., Augsten, M., Beltrami, E., Giorgio, M., & Östman, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.12.022 · Cited by 43 · see citing works
Cobley, J. N., Margaritelis, N. V., Morton, J. P., Close, G. L., Nikolaidis, M. G., & Malone, J. K. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00182 · Cited by 43 · see citing works
Role of hypohalous acids in basement membrane homeostasis
Colon, S., Page-McCaw, P., & Bhave, G. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2017.7245 · Cited by 38 · see citing works
Measuring Mitochondrial Protein Thiol Redox State
Requejo, R., Chouchani, E. T., Hurd, T. R., Menger, K. E., Hampton, M. B., & Murphy, M. P. (2010) · Methods in Enzymology · doi:10.1016/s0076-6879(10)74008-8 · Cited by 31 · see citing works
The ambiguous aspects of oxygen
Napolitano, G., Fasciolo, G., & Venditti, P. (2022) · Oxygen · doi:10.3390/oxygen2030027 · Cited by 30 · see citing works
Foti, A., Dorendorf, F., & Leimkühler, S. (2017) · PLOS ONE · doi:10.1371/journal.pone.0182061 · Cited by 26 · see citing works
A Redox-Switchable Colorimetric Probe for “Naked-Eye” Detection of Hypochlorous Acid and Glutathione
Han, Q., Zhou, F., Wang, Y., Feng, H., Meng, Q., Zhang, Z., & Zhang, R. (2019) · Molecules · doi:10.3390/molecules24132455 · Cited by 23 · see citing works
Sharina, I. G., & Martin, E. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6687 · Cited by 19 · see citing works
- Authors
- Winterbourn, C. C.
- Affiliations
- University of Otago (NZ)
- Corresponding author
- Winterbourn, Christine C
- Venue
- Nature Chemical Biology
- Published
- 2008-04-17
- Volume
- 4
- Issue
- 5
- Pages
- 278-286
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W1991952977
- Cited by
- 2,504
- References
- 108
- Citations by year
- 2026: 113 · 2025: 136 · 2024: 133 · 2023: 167 · 2022: 182 · 2021: 189 · 2020: 190 · 2019: 182 · 2018: 179 · 2017: 152 · 2016: 167 · 2015: 127 · 2014: 126 · 2013: 136 · 2012: 101
- FWCI
- 5.66
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- reactive oxygen species, antioxidant effectiveness, redox signaling, NADPH oxidase, restricted diffusion, compartmentalization, oxidative damage, signal transduction
- MeSH terms
- Enzymes, Kinetics, Mitochondria, NADP, Oxidation-Reduction, Reactive Oxygen Species, Oxidative Stress
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