Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling

Brand, Martin D.

doi:10.1016/j.freeradbiomed.2016.04.001

Cited by 1,063Mitochondrial Function and PathologyRedox biology and oxidative stressCoenzyme Q10 studies and effects

Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling

Brand, Martin D.·2016·Free Radical Biology and Medicine

DOI 10.1016/j.freeradbiomed.2016.04.001

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Abstract

This review examines the generation of reactive oxygen species by mammalian mitochondria, and the status of different sites of production in redox signaling and pathology. Eleven distinct mitochondrial sites associated with substrate oxidation and oxidative phosphorylation leak electrons to oxygen to produce superoxide or hydrogen peroxide: oxoacid dehydrogenase complexes that feed electrons to NAD+; respiratory complexes I and III, and dehydrogenases, including complex II, that use ubiquinone as acceptor. The topologies, capacities, and substrate dependences of each site have recently clarified. Complex III and mitochondrial glycerol 3-phosphate dehydrogenase generate superoxide to the external side of the mitochondrial inner membrane as well as the matrix, the other sites generate superoxide and/or hydrogen peroxide exclusively in the matrix. These different site-specific topologies are important for redox signaling. The net rate of superoxide or hydrogen peroxide generation depends on the substrates present and the antioxidant systems active in the matrix and cytosol. The rate at each site can now be measured in complex substrate mixtures. In skeletal muscle mitochondria in media mimicking muscle cytosol at rest, four sites dominate, two in complex I and one each in complexes II and III. Specific suppressors of two sites have been identified, the outer ubiquinone-binding site in complex III (site III Qo) and the site in complex I active during reverse electron transport (site I Q). These suppressors prevent superoxide/hydrogen peroxide production from a specific site without affecting oxidative phosphorylation, making them excellent tools to investigate the status of the sites in redox signaling, and to suppress the sites to prevent pathologies. They allow the cellular roles of mitochondrial superoxide/hydrogen peroxide production to be investigated without catastrophic confounding bioenergetic effects. They show that sites III Qo and I Q are active in cells and have important roles in redox signaling (e.g. hypoxic signaling and ER-stress) and in causing oxidative damage in a variety of biological contexts.

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Mitochondria are a susceptible target of oxidative damage, which causes a malicious circle of events in endothelial cells.
“Additionally, mitochondria are a susceptible target of oxidative damage, which causes a malicious circle of events in ECs [224,225,226].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [226]
Accumulation of reactive oxygen species in muscle and neuron cells has the potential to damage cellular mitochondria.
“Conversely, the accumulation of ROS in the muscle and neuron cells has the potential to damage cellular mitochondria (46).”
From From mitochondria to sarcopenia: role of 17β-estradiol and testosterone (2023) · cites this paper as [46]
Accumulation of excessive ROS contributes to damaged and dysfunctional mitochondria in muscle and neural cells.
“it is clear that accumulation of excessive ROS contributes to damaged and dysfunctional mitochondria in muscle and neural cells.”
From Mitochondria initiate and regulate sarcopenia (2017) · cites this paper as [15]

The Hallmarks of Aging
López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982 · see citing works
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827 · see citing works
The Pathobiology of Diabetic Complications
Brownlee, M. (2005) · Diabetes · doi:10.2337/diabetes.54.6.1615 · Cited by 5,339 · see citing works
Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084 · see citing works
Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587 · see citing works
Mitochondria, Oxidants, and Aging
Balaban, R. S., Nemoto, S., & Finkel, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.001 · Cited by 4,388 · see citing works
Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
Ray, P. D., Huang, B.-W., & Tsuji, Y. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.01.008 · Cited by 4,373 · see citing works
Reactive oxygen species, cellular redox systems, and apoptosis
Circu, M. L., & Aw, T. Y. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.022 · Cited by 3,340 · see citing works
Mitochondrial free radical generation, oxidative stress, and aging
Cadenas, E., & Davies, K. J. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00317-8 · Cited by 3,010 · see citing works
Ischaemic accumulation of succinate controls reperfusion injury through mitochondrial ROS
Chouchani, E. T., Pell, V. R., Gaude, E., Aksentijević, D., Sundier, S. Y., Robb, E. L., Logan, A., Nadtochiy, S. M., Ord, E. N. J., Smith, A. C., et al. (2014) · Nature · doi:10.1038/nature13909 · Cited by 2,907 · see citing works
Physiological Roles of Mitochondrial Reactive Oxygen Species
Sena, L. A., & Chandel, N. S. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.025 · Cited by 2,632 · see citing works
The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
Boveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626 · see citing works
Calcium, ATP, and ROS: a mitochondrial love-hate triangle
Brookes, P. S., Yoon, Y., Robotham, J. L., Anders, M. W., & Sheu, S.-S. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00139.2004 · Cited by 2,575 · see citing works
Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production
Powers, S. K., & Jackson, M. J. (2008) · Physiological Reviews · doi:10.1152/physrev.00031.2007 · Cited by 2,459 · see citing works
Assessing mitochondrial dysfunction in cells
Brand, M. D., & Nicholls, D. G. (2011) · Biochemical Journal · doi:10.1042/bj20110162 · Cited by 2,436 · see citing works
Self-citation
Cellular mechanisms and physiological consequences of redox-dependent signalling
Holmström, K. M., & Finkel, T. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3801 · Cited by 2,093 · see citing works
Mitochondrial dysfunction and type 2 diabetes
Lowell, B. B., & Shulman, G. I. (2005) · Science · doi:10.1126/science.1104343 · Cited by 2,070 · see citing works
Reactive oxygen species generated at mitochondrial complex III stabilize hypoxia-inducible factor-1α during hypoxia
Chandel, N. S., McClintock, D. S., Feliciano, C. E., Wood, T. M., Melendez, J. A., Rodriguez, A. M., & Schumacker, P. T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001914200 · Cited by 2,000 · see citing works
Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
Li, Y., Huang, T.-T., Carlson, E. J., Melov, S., Ursell, P. C., Olson, J. L., Noble, L. J., Yoshimura, M. P., Berger, C., Chan, P. H., et al. (1995) · Nature Genetics · doi:10.1038/ng1295-376 · Cited by 1,789 · see citing works
Mitochondrial metabolism and ROS generation are essential for Kras-mediated tumorigenicity
Weinberg, F., Hamanaka, R., Wheaton, W. W., Weinberg, S., Joseph, J., Lopez, M., Kalyanaraman, B., Mutlu, G. M., Budinger, G. R. S., & Chandel, N. S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003428107 · Cited by 1,742 · see citing works
High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
Korshunov, S. S., Skulachev, V. P., & Starkov, A. A. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01159-9 · Cited by 1,727 · see citing works
Tlr signalling augments macrophage bactericidal activity through mitochondrial ros
West, A. P., Brodsky, I. E., Rahner, C., Woo, D. K., Erdjument-Bromage, H., Tempst, P., Walsh, M. C., Choi, Y., Shadel, G. S., & Ghosh, S. (2011) · Nature · doi:10.1038/nature09973 · Cited by 1,659 · see citing works
Mitochondrial ROS in cancer: initiators, amplifiers or an Achilles' heel?
Sabharwal, S. S., & Schumacker, P. T. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3803 · Cited by 1,643 · see citing works
Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
Turrens, J. F., & Boveris, A. (1980) · Biochemical Journal · doi:10.1042/bj1910421 · Cited by 1,601 · see citing works
Topology of superoxide production from different sites in the mitochondrial electron transport chain
St-Pierre, J., Buckingham, J. A., Roebuck, S. J., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207217200 · Cited by 1,545 · see citing works
Self-citation
Mitochondrial Complex I Inhibitor Rotenone Induces Apoptosis through Enhancing Mitochondrial Reactive Oxygen Species Production
Li, N., Ragheb, K., Lawler, G., Sturgis, J., Rajwa, B. P., Melendez, J. A., & Robinson, J. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210432200 · Cited by 1,434 · see citing works
Oxidative stress and mitochondrial dysfunction in Alzheimer’s disease
Wang, X., Wang, W., Li, L., Perry, G., Lee, H.-G., & Zhu, X. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.10.015 · Cited by 1,357 · see citing works
Mitochondrial ROS Signaling in Organismal Homeostasis
Shadel, G. S., & Horvath, T. L. (2015) · Cell · doi:10.1016/j.cell.2015.10.001 · Cited by 1,353 · see citing works
Mitochondrial metabolism of reactive oxygen species
Andreyev, A. Y., Kushnareva, Y. E., & Starkov, A. A. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0102-7 · Cited by 1,336 · see citing works
Mitochondrial Oxidative Stress: Implications for Cell Death
Orrenius, S., Gogvadze, V. G., & Zhivotovsky, B. (2006) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105122 · Cited by 1,266 · see citing works
Regulation of autophagy by ROS: physiology and pathology
Scherz-Shouval, R., & Elazar, Z. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.007 · Cited by 1,263 · see citing works
Generation of reactive oxygen species by the mitochondrial electron transport chain
Liu, Y., Fiskum, G., & Schubert, D. (2002) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2002.00744.x · Cited by 1,260 · see citing works
The sites and topology of mitochondrial superoxide production
Brand, M. D. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.01.003 · Cited by 1,217 · see citing works
Self-citation
Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
Turrens, J. F., Alexandre, A., & Lehninger, A. L. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90293-0 · Cited by 1,214 · see citing works
Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis
Giorgio, M., Migliaccio, E., Orsini, F., Paolucci, D., Moroni, M., Contursi, C., Pelliccia, G., Luzi, L., Minucci, S., Marcaccio, M., et al. (2005) · Cell · doi:10.1016/j.cell.2005.05.011 · Cited by 1,176 · see citing works
Mitochondria and reactive oxygen species
Kowaltowski, A. J., de Souza-Pinto, N. C., Castilho, R. F., & Vercesi, A. E. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.004 · Cited by 1,162 · see citing works
The role of mitochondria in aging
Bratic, A., & Larsson, N.-G. (2013) · Journal of Clinical Investigation · doi:10.1172/jci64125 · Cited by 1,087 · see citing works
Mitochondrial ROS-induced ROS release: An update and review
Zorov, D. B., Juhaszova, M., & Sollott, S. J. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.04.029 · Cited by 1,081 · see citing works
Mitochondria, oxygen free radicals, disease and ageing
Raha, S., & Robinson, B. H. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01674-1 · Cited by 1,066 · see citing works
Complex iii releases superoxide to both sides of the inner mitochondrial membrane
Muller, F. L., Liu, Y., & Van Remmen, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407715200 · Cited by 1,036 · see citing works
Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins
Brand, M. D., Affourtit, C., Esteves, T. C., Green, K., Lambert, A. J., Miwa, S., Pakay, J. L., & Parker, N. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.05.034 · Cited by 1,032 · see citing works
Self-citation
Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes
Hamanaka, R. B., & Chandel, N. S. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.002 · Cited by 1,011 · see citing works
Role of oxidative stress in the pathogenesis of nonalcoholic steatohepatitis
Rolo, A. P., Teodoro, J. S., & Palmeira, C. M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.003 · Cited by 955 · see citing works
Superoxide production by the mitochondrial respiratory chain
Turrens, J. F. (1997) · Bioscience Reports · doi:10.1023/a:1027374931887 · Cited by 903 · see citing works
Fluorescent and luminescent probes for measurement of oxidative and nitrosative species in cells and tissues: Progress, pitfalls, and prospects
Wardman, P. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.06.026 · Cited by 863 · see citing works
Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria
Cadenas, E., Boveris, A., Ragan, C. I., & Stoppani, A. O. M. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90035-2 · Cited by 855 · see citing works
The role of mitochondria in reactive oxygen species metabolism and signaling
Starkov, A. A. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.015 · Cited by 846 · 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
Mitochondrial proton and electron leaks
Jastroch, M., Divakaruni, A. S., Mookerjee, S., Treberg, J. R., & Brand, M. D. (2010) · Essays in Biochemistry · doi:10.1042/bse0470053 · Cited by 829 · see citing works
Self-citation
Crystal structure of the entire respiratory complex I
Baradaran, R., Berrisford, J. M., Minhas, G. S., & Sazanov, L. A. (2013) · Nature · doi:10.1038/nature11871 · Cited by 797 · see citing works
Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism.
Ježek, P., & Hlavatá, L. (2005) · International Journal of Biochemistry and Cell Biology · doi:10.1016/j.biocel.2005.05.013 · Cited by 771 · see citing works
Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus
Sazanov, L. A., & Hinchliffe, P. (2006) · Science · doi:10.1126/science.1123809 · Cited by 763 · see citing works
A Unifying Mechanism for Mitochondrial Superoxide Production during Ischemia-Reperfusion Injury
Chouchani, E. T., Pell, V. R., James, A. M., Work, L. M., Saeb-Parsy, K., Frezza, C., Krieg, T., & Murphy, M. P. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2015.12.009 · Cited by 752 · see citing works
Role of Metabolic H2O2 Generation
Sies, H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.544635 · Cited by 734 · see citing works
The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
Kußmaul, L., & Hirst, J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510977103 · Cited by 720 · see citing works
Extending life span by increasing oxidative stress
Ristow, M., & Schmeisser, S. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.05.010 · Cited by 718 · see citing works
Mitochondrial α-Ketoglutarate Dehydrogenase Complex Generates Reactive Oxygen Species
Starkov, A. A., Fiskum, G. M., Chinopoulos, C., Lorenzo, B. J., Browne, S. E., Patel, M. S., & Beal, M. F. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1899-04.2004 · Cited by 692 · see citing works
Mitochondrial Complex II Can Generate Reactive Oxygen Species at High Rates in Both the Forward and Reverse Reactions
Quinlan, C. L., Orr, A. L., Perevoshchikova, I. V., Treberg, J. R., Ackrell, B. A., & Brand, M. D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.374629 · Cited by 670 · see citing works
Self-citation
Mitochondrial Complex III ROS Regulate Adipocyte Differentiation
Tormos, K. V., Ansó, E., Hamanaka, R. B., Eisenbart, J. D., Joseph, J., Kalyanaraman, B., & Chandel, N. S. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.007 · Cited by 662 · see citing works
The Role of Reactive Oxygen Species in Mesenchymal Stem Cell Adipogenic and Osteogenic Differentiation: A Review
Atashi, F., Modarressi, A., & Pepper, M. S. (2015) · Stem Cells and Development · doi:10.1089/scd.2014.0484 · Cited by 655 · see citing works
Molecular Mechanisms of Ischemia–Reperfusion Injury in Brain: Pivotal Role of the Mitochondrial Membrane Potential in Reactive Oxygen Species Generation
Sanderson, T. H., Reynolds, C. A., Kumar, R., Przyklenk, K., & Hüttemann, M. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8344-z · Cited by 641 · see citing works
Superoxide radicals as precursors of mitochondrial hydrogen peroxide
Loschen, G., Azzi, A., Richter, C., & Flohé, L. (1974) · FEBS Letters · doi:10.1016/0014-5793(74)80281-4 · Cited by 634 · see citing works
Cardiac Mitochondria and Reactive Oxygen Species Generation
Chen, Y., & Zweier, J. L. (2014) · Circulation Research · doi:10.1161/circresaha.114.300559 · Cited by 606 · see citing works
ΔΨ m ‐Dependent and ‐independent production of reactive oxygen species by rat brain mitochondria
Votyakova, T. V., & Reynolds, I. J. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00548.x · Cited by 601 · see citing works
Sites of reactive oxygen species generation by mitochondria oxidizing different substrates
Quinlan, C. L., Perevoshchikova, I. V., Hey‐Mogensen, M., Orr, A. L., & Brand, M. D. (2013) · Redox Biology · doi:10.1016/j.redox.2013.04.005 · Cited by 595 · see citing works
Self-citation
The Mitochondrial Production of Reactive Oxygen Species: Mechanisms and Implications in Human Pathology
Lenaz, G. (2001) · IUBMB Life · doi:10.1080/15216540152845957 · Cited by 585 · see citing works
Function and Structure of Complex II of the Respiratory Chain
Cecchini, G. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161700 · Cited by 556 · see citing works
Respiratory chain linked H2O2 production in pigeon heart mitochondria
Loschen, G., & Flohé, L. (1971) · FEBS Letters · doi:10.1016/0014-5793(71)80459-3 · Cited by 552 · see citing works
Oxidants in mitochondria: from physiology to diseases
Richter, C., Gogvadze, V. G., Laffranchi, R., Schlapbach, R., Schweizer, M., Suter, M., Walter, P. B., & Yaffee, M. (1995) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(95)00012-s · Cited by 543 · see citing works
Molecular Mechanisms of Superoxide Production by the Mitochondrial Respiratory Chain
Dröse, S., & Brandt, U. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3573-0_6 · Cited by 519 · see citing works
Oxidative stress, cardiolipin and mitochondrial dysfunction in nonalcoholic fatty liver disease
Paradies, G. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i39.14205 · Cited by 508 · see citing works
Characterization of Superoxide-producing Sites in Isolated Brain Mitochondria
Kudin, A. P., Bimpong‐Buta, N., Vielhaber, S., Elger, C. E., & Kunz, W. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310341200 · Cited by 505 · see citing works
Mitochondrial Oxygen Radical Generation and Leak: Sites of Production in States 4 and 3, Organ Specificity, and Relation to Aging and Longevity
Barja, G. (1999) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005427919188 · Cited by 494 · see citing works
Relationship between mitochondrial superoxide and hydrogen peroxide production and longevity of mammalian species
Ku, H., Brunk, U. T., & Sohal, R. S. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90165-q · Cited by 488 · see citing works
Mitochondrial oxidative stress in aging and healthspan
Dai, D., Chiao, Y. A., Marcinek, D. J., Szeto, H. H., & Rabinovitch, P. S. (2014) · Longevity & Healthspan · doi:10.1186/2046-2395-3-6 · Cited by 481 · see citing works
Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial nadh:Ubiquinone oxidoreductase (complex i)
Lambert, A. J., & Brand, M. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406576200 · Cited by 480 · see citing works
Self-citation
Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation
Tahara, E. B., Navarete, F. D. T., & Kowaltowski, A. J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.02.008 · Cited by 479 · see citing works
The Cytochrome bc1 Complex: Function in the Context of Structure
Crofts, A. R. (2004) · Annual Review of Physiology · doi:10.1146/annurev.physiol.66.032102.150251 · Cited by 474 · see citing works
Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane
LAMBERT, A. J., & BRAND, M. D. (2004) · Biochemical Journal · doi:10.1042/bj20040485 · Cited by 470 · see citing works
Self-citation
Mitochondrial Dysfunction in Parkinson’s Disease
Moon, H. E., & Paek, S. H. (2015) · Experimental Neurobiology · doi:10.5607/en.2015.24.2.103 · Cited by 455 · see citing works
Generation of Reactive Oxygen Species in the Reaction Catalyzed by α-Ketoglutarate Dehydrogenase
Tretter, L., & Ádám‐Vizi, V. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1842-04.2004 · Cited by 455 · see citing works
Mitochondrial H + Leak and ROS Generation: An Odd Couple
Brookes, P. S. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.10.016 · Cited by 447 · see citing works
Dependence of H2O2 formation by rat heart mitochondria on substrate availability and donor age
Hansford, R. G., Hogue, B. A., & Mildaziene, V. (1997) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1022420007908 · Cited by 447 · see citing works
Production of Reactive Oxygen Species in Brain Mitochondria: Contribution by Electron Transport Chain and Non–Electron Transport Chain Sources
Adam-Vizi, V. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.1140 · Cited by 439 · see citing works
Mitochondrial complex III regulates hypoxic activation of HIF
Klimova, T., & Chandel, N. S. (2008) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402307 · Cited by 433 · see citing works
Mitochondrial free radical production and cell signaling
Cadenas, E. (2004) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2004.02.005 · Cited by 430 · see citing works
Mitochondrial Diseases of the Brain
Chaturvedi, R. K., & Beal, M. F. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.03.018 · Cited by 416 · see citing works
Mechanistic insight from the crystal structure of mitochondrial complex I
Zickermann, V., Wirth, C., Nasiri, H. R., Siegmund, K., Schwalbe, H., Hunte, C., & Brandt, U. (2015) · Science · doi:10.1126/science.1259859 · Cited by 405 · see citing works
Mitochondrial production of superoxide anions and its relationship to the antimycin insensitive respiration
Boveris, A., & Cadenas, E. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80928-8 · Cited by 401 · see citing works
Mitochondrial ROS Generation and Its Regulation: Mechanisms Involved in H 2 O 2 Signaling
Rigoulet, M., Yoboue, E. D., & Devin, A. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3363 · Cited by 394 · see citing works
The mechanism of mitochondrial superoxide production by the cytochrome bc1 complex
Dröse, S., & Brandt, U. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803236200 · Cited by 386 · see citing works
Titrating the Effects of Mitochondrial Complex I Impairment in the Cell Physiology
Barrientos, A., & Moraes, C. T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.23.16188 · Cited by 382 · see citing works
Reactive Oxygen Species Production by Mitochondria
Lambert, A. J., & Brand, M. D. (2009) · Methods in molecular biology · doi:10.1007/978-1-59745-521-3_11 · Cited by 374 · see citing works
Self-citation
The rate of free radical production as a determinant of the rate of aging: evidence from the comparative approach
Pérez‐Campo, R., Lopez‐Torres, M., Cadenas, S., Rojas, C., & Barja, G. (1998) · Journal of Comparative Physiology B · doi:10.1007/s003600050131 · Cited by 356 · see citing works
Oxidative damage to macromolecules in human Parkinson disease and the rotenone model
Sanders, L. H., & Greenamyre, J. T. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.01.003 · Cited by 347 · see citing works
Sites of superoxide and hydrogen peroxide production by muscle mitochondria assessed ex vivo under conditions mimicking rest and exercise
Goncalves, R. L. S., Quinlan, C. L., Perevoshchikova, I. V., Hey-Mogensen, M., & Brand, M. D. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.619072 · Cited by 329 · see citing works
The 2-oxoacid dehydrogenase complexes in mitochondria can produce superoxide/hydrogen peroxide at much higher rates than complex I
Quinlan, C. L., Goncalves, R. L. S., Hey-Mogensen, M., Yadava, N., Bunik, V. I., & Brand, M. D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.545301 · Cited by 310 · see citing works
Self-citation
Mitochondrial superoxide production in kainate-induced hippocampal damage
Liang, L., Ho, Y.-S., & Patel, M. (2000) · Neuroscience · doi:10.1016/s0306-4522(00)00397-3 · Cited by 309 · see citing works
Oxidants and aging
Beckman, K. B., & Ames, B. N. (2000) · Elsevier eBooks · doi:10.1016/b978-044482650-3/50027-4 · Cited by 307 · see citing works
Functional role of mitochondrial respiratory supercomplexes
Genova, M. L., & Lenaz, G. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.11.002 · Cited by 306 · see citing works
Contribution of mitochondria to oxidative stress associated with alcoholic liver disease1 1This article is part of a series of reviews on “Alcohol, Oxidative Stress and Cell Injury”. The full list of papers may be found on the homepage of the journal.
Bailey, S. M., & CUNNINGHAM, C. C. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00769-9 · Cited by 301 · see citing works
Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase
Messner, K. R., & Imlay, J. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204958200 · Cited by 301 · see citing works
Superoxide Is Produced by the Reduced Flavin in Mitochondrial Complex I
Pryde, K. R., & Hirst, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.186841 · Cited by 301 · see citing works
Superoxide and hydrogen peroxide production by Drosophila mitochondria
Miwa, S., St‐Pierre, J., Partridge, L., & Brand, M. D. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00464-7 · Cited by 298 · see citing works
Self-citation
A mitochondrial etiology of Alzheimer and Parkinson disease
Coskun, P. E., Wyrembak, J., Schriner, S. E., Chen, H.-W., Marciniack, C., LaFerla, F. M., & Wallace, D. C. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.08.008 · Cited by 297 · see citing works
Hydrogen peroxide release by mitochondria increases during aging
Sohal, R. S., & Sohal, B. H. (1991) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(91)90034-w · Cited by 296 · see citing works
Starvation-induced autophagy is regulated by mitochondrial reactive oxygen species leading to AMPK activation
Li, L., Chen, Y., & Gibson, S. B. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.09.020 · Cited by 292 · see citing works
The role of mitochondrial function and cellular bioenergetics in ageing and disease
Brand, M. D., Orr, A. L., Perevoshchikova, I. V., & Quinlan, C. L. (2013) · British Journal of Dermatology · doi:10.1111/bjd.12208 · Cited by 292 · see citing works
Self-citation
There is no evidence that mitochondria are the main source of reactive oxygen species in mammalian cells
Brown, G. C., & Borutaitė, V. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.02.001 · Cited by 280 · see citing works
Electron Transport Chain-dependent and -independent Mechanisms of Mitochondrial H2O2 Emission during Long-chain Fatty Acid Oxidation
Seifert, E. L., Estey, C., Xuan, J. Y., & Harper, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.026203 · Cited by 278 · see citing works
Low rates of hydrogen peroxide production by isolated heart mitochondria associate with long maximum lifespan in vertebrate homeotherms
Lambert, A. J., Boysen, H. M., Buckingham, J. A., Yang, T., Podlutsky, A. J., Austad, S. N., Kunz, T., Buffenstein, R., & Brand, M. D. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00312.x · Cited by 264 · see citing works
Self-citation
Macrophage Mitochondrial Oxidative Stress Promotes Atherosclerosis and Nuclear Factor-κB–Mediated Inflammation in Macrophages
Wang, Y., Wang, G. Z., Rabinovitch, P. S., & Tabas, I. A. (2013) · Circulation Research · doi:10.1161/circresaha.114.302153 · Cited by 264 · see citing works
Mitochondrial involvement and oxidative stress in temporal lobe epilepsy
Rowley, S. D., & Patel, M. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.02.002 · Cited by 257 · see citing works
[47] Mammalian succinate dehydrogenase
Ackrell, B. A. C., Kearney, E. B., & Singer, T. P. (1978) · Methods in Enzymology · doi:10.1016/s0076-6879(78)53050-4 · Cited by 255 · see citing works
Reduction in mitochondrial superoxide dismutase modulates Alzheimer’s disease-like pathology and accelerates the onset of behavioral changes in human amyloid precursor protein transgenic mice
Esposito, L., Raber, J., Kekonius, L., Yan, F., Yu, G.-Q., Bien-Ly, N., Puoliväli, J., Scearce-Levie, K., Masliah, E., & Mucke, L. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.0482-06.2006 · Cited by 254 · see citing works
Generation of Superoxide Anion by Succinate-Cytochromec Reductase from Bovine Heart Mitochondria
Zhang, L., Yu, L. P. C., & Yu, C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.51.33972 · Cited by 253 · see citing works
Mitochondrial ROS generation for regulation of autophagic pathways in cancer
Li, Z., Yu, Y., Ming, M., & Liu, B. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.09.046 · Cited by 235 · see citing works
Overexpression of mitochondrial superoxide dismutase in mice protects the retina from diabetes-induced oxidative stress
Kowluru, R. A., Kowluru, V., Xiong, Y., & Ho, Y.-S. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.01.012 · Cited by 233 · see citing works
Stable Overexpression of Manganese Superoxide Dismutase in Mitochondria Identifies Hydrogen Peroxide as a Major Oxidant in the AP-1-mediated Induction of Matrix-degrading Metalloprotease-1
Wenk, J., Brenneisen, P., Wlaschek, M., Poswig, A., Briviba, K., Oberley, T. D., & Scharffetter‐Kochanek, K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25869 · Cited by 224 · see citing works
Rotenone induces cell death in primary dopaminergic culture by increasing ROS production and inhibiting mitochondrial respiration
Radad, K., Rausch, W., & Gille, G. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2006.02.003 · Cited by 220 · see citing works
Generating, Partitioning, Targeting and Functioning of Superoxide in Mitochondria
Liu, S. (1997) · Bioscience Reports · doi:10.1023/a:1027328510931 · Cited by 217 · see citing works
Evidence for two sites of superoxide production by mitochondrial NADH-ubiquinone oxidoreductase (complex I)
Treberg, J. R., Quinlan, C. L., & Brand, M. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.252502 · Cited by 212 · see citing works
Self-citation
Effect of Glutathione Depletion on Sites and Topology of Superoxide and Hydrogen Peroxide Production in Mitochondria
Han, D., Canali, R., Rettori, D., & Kaplowitz, N. (2003) · Molecular Pharmacology · doi:10.1124/mol.64.5.1136 · Cited by 212 · see citing works
Mitochondrial Aging: Open Questionsa
Beckman, K. B., & Ames, B. N. (1998) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1998.tb09897.x · Cited by 211 · see citing works
Reactive Oxygen Species, Apoptosis, and Mitochondrial Dysfunction in Hearing Loss
Kamogashira, T., Fujimoto, C., & Yamasoba, T. (2015) · BioMed Research International · doi:10.1155/2015/617207 · Cited by 210 · see citing works
Mitochondrial ROS and cancer drug resistance: Implications for therapy
Okon, I. S., & Zou, M.-H. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.06.013 · Cited by 207 · see citing works
Suppressors of superoxide production from mitochondrial complex III
Orr, A. L., Vargas, L., Turk, C. N., Baaten, J., Matzen, J., Dardov, V. J., Attle, S. J., Li, J., Quackenbush, D., Goncalves, R. L. S., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1910 · Cited by 207 · see citing works
Self-citation
Overexpression of Manganese Superoxide Dismutase Prevents Alcohol-induced Liver Injury in the Rat
Wheeler, M. D., Nakagami, M., Bradford, B. U., Uesugi, T., Mason, R. P., Connor, H. D., Dikalova, A., Kadiiska, M. B., & Thurman, R. G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105352200 · Cited by 207 · see citing works
Mitochondrial and Cytoplasmic ROS Have Opposing Effects on Lifespan
Schaar, C. E., Dues, D. J., Spielbauer, K. K., Machiela, E., Cooper, J. F., Senchuk, M., Hekimi, S., & Van Raamsdonk, J. M. (2015) · PLOS Genetics · doi:10.1371/journal.pgen.1004972 · Cited by 203 · see citing works
The mechanism of superoxide production by the antimycin-inhibited mitochondrial Q-cycle
Quinlan, C. L., Gerencser, A. A., Treberg, J. R., & Brand, M. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.267898 · Cited by 200 · see citing works
Self-citation
The mitochondrion: A perpetrator of acquired hearing loss
Böttger, E. C., & Schacht, J. (2013) · Hearing Research · doi:10.1016/j.heares.2013.01.006 · Cited by 195 · see citing works
Mitochondrial ROS metabolism: 10 Years later
Andreyev, A. Y., Kushnareva, Y. E., Murphy, A. N., & Starkov, A. A. (2015) · Biochemistry (Moscow) · doi:10.1134/s0006297915050028 · Cited by 194 · see citing works
Redefining the major contributors to superoxide production in contracting skeletal muscle. The role of NAD(P)H oxidases
Sakellariou, G. K., Jackson, M. J., & Vasilaki, A. (2014) · Free Radical Research · doi:10.3109/10715762.2013.830718 · Cited by 184 · see citing works
Generator-specific targets of mitochondrial reactive oxygen species
Bleier, L., Wittig, I., Heide, H., Steger, M., Brandt, U., & Dröse, S. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.10.511 · Cited by 183 · see citing works
Oxygen Sensitivity of Mitochondrial Reactive Oxygen Species Generation Depends on Metabolic Conditions
Hoffman, D. L., & Brookes, P. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809512200 · Cited by 182 · see citing works
Mitochondrial defect drives non-autonomous tumour progression through Hippo signalling in Drosophila
Ohsawa, S., Sato, Y., Enomoto, M., Nakamura, M., Betsumiya, A., & Igaki, T. (2012) · Nature · doi:10.1038/nature11452 · Cited by 180 · see citing works
Hydrogen peroxide production by liver mitochondria in different species
Sohal, R. S., Svensson, I., & Brunk, U. T. (1990) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(90)90039-i · Cited by 174 · see citing works
JNK interaction with Sab mediates ER stress induced inhibition of mitochondrial respiration and cell death
Win, S., Than, T. A., Fernández-Checa, J. C., & Kaplowitz, N. (2014) · Cell Death and Disease · doi:10.1038/cddis.2013.522 · Cited by 174 · see citing works
Zinc Is a Potent Inhibitor of Thiol Oxidoreductase Activity and Stimulates Reactive Oxygen Species Production by Lipoamide Dehydrogenase
Gazaryan, I. G., Krasnikov, B. F., ASHBY, G. A., THORNELEY, R. N. F., Kristal, B. S., & Brown, A. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108264200 · Cited by 174 · see citing works
H2O2 production of heart mitochondria and aging rate are slower in canaries and parakeets than in mice: sites of free radical generation and mechanisms involved
Herrero, A., & Barja, G. (1998) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(98)00035-9 · Cited by 168 · see citing works
Response of mitochondrial reactive oxygen species generation to steady-state oxygen tension: implications for hypoxic cell signaling
Hoffman, D. L., Salter, J. D., & Brookes, P. S. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00699.2006 · Cited by 167 · see citing works
A Refined Analysis of Superoxide Production by Mitochondrial sn-Glycerol 3-Phosphate Dehydrogenase
Orr, A. L., Quinlan, C. L., Perevoshchikova, I. V., & Brand, M. D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.397828 · Cited by 167 · see citing works
Self-citation
Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism
Yeh, J. I., Chinte, U., & Du, S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712331105 · Cited by 164 · see citing works
Native rates of superoxide production from multiple sites in isolated mitochondria measured using endogenous reporters
Quinlan, C. L., Treberg, J. R., Perevoshchikova, I. V., Orr, A. L., & Brand, M. D. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.08.015 · Cited by 151 · see citing works
Self-citation
High rates of superoxide production in skeletal-muscle mitochondria respiring on both complex I- and complex II-linked substrates
Muller, F. L., Liu, Y., Abdul-Ghani, M. A., Lustgarten, M. S., Bhattacharya, A., Jang, Y. C., & Van Remmen, H. (2008) · Biochemical Journal · doi:10.1042/bj20071162 · Cited by 150 · see citing works
Thioredoxin-2 Inhibits Mitochondrial ROS Generation and ASK1 Activity to Maintain Cardiac Function
Huang, Q.-H., Zhou, H., Zhang, H.-F., Huang, Y., Hinojosa-Kirschenbaum, F., Fan, P., Yao, L., Belardinelli, L., Tellides, G., Giordano, F. J., et al. (2015) · Circulation · doi:10.1161/circulationaha.114.012725 · Cited by 149 · see citing works
Generation of hydrogen peroxide by brain mitochondria: The effect of reoxygenation following postdecapitative ischemia
Cino, M., & Maestro, R. F. D. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90148-3 · Cited by 148 · see citing works
Manganese Superoxide Dismutase Overexpression Attenuates MPTP Toxicity
Klivenyi, P., St. Clair, D., Wermer, M., Yen, H.-C., Oberley, T., Yang, L., & Beal, M. F. (1998) · Neurobiology of Disease · doi:10.1006/nbdi.1998.0191 · Cited by 142 · see citing works
Purification of Mitochondrial Thioredoxin Reductase and Its Involvement in the Redox Regulation of Membrane Permeability
Rigobello, M. P., Callegaro, M. T., Barzon, E., Benetti, M., & Bindoli, A. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00216-5 · Cited by 138 · see citing works
Reactive Oxygen-Related Diseases: Therapeutic Targets and Emerging Clinical Indications
Casas, A. I., Dao, V. T.-V., Daiber, A., Maghzal, G. J., Di Lisa, F., Kaludercic, N., Leach, S., Cuadrado, A., Jaquet, V., Seredenina, T., et al. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2015.6433 · Cited by 136 · see citing works
The role of complex II in disease
Hoekstra, A. S., & Bayley, J. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.11.005 · Cited by 136 · see citing works
Inactivation of the 2‐oxo acid dehydrogenase complexes upon generation of intrinsic radical species
Bunik, V. I., & Sievers, C. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03204.x · Cited by 134 · see citing works
Mitochondrial Reactive Oxygen Species and Risk of Atherosclerosis
Hulsmans, M., Dooren, E. V., & Holvoet, P. (2012) · Current Atherosclerosis Reports · doi:10.1007/s11883-012-0237-0 · Cited by 132 · see citing works
Q-site inhibitor induced ROS production of mitochondrial complex II is attenuated by TCA cycle dicarboxylates
Siebels, I., & Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.06.005 · Cited by 130 · see citing works
2‐Oxo acid dehydrogenase complexes in redox regulation
Bunik, V. I. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03470.x · Cited by 125 · see citing works
Endogenous and endobiotic induced reactive oxygen species formation by isolated hepatocytes
Siraki, A. G., Pourahmad, J., Chan, T. S., Khan, S., & O'Brien, P. J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00764-x · Cited by 122 · see citing works
Sites of superoxide and hydrogen peroxide production during fatty acid oxidation in rat skeletal muscle mitochondria
Perevoshchikova, I. V., Quinlan, C. L., Orr, A. L., Gerencser, A. A., & Brand, M. D. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.04.006 · Cited by 120 · see citing works
Self-citation
The mitochondria-targeted anti-oxidant MitoQ decreases ischemia-reperfusion injury in a murine syngeneic heart transplant model
Dare, A. J., Logan, A., Prime, T. A., Rogatti, S., Goddard, M., Bolton, E. M., Bradley, J. A., Pettigrew, G. J., Murphy, M. P., & Saeb-Parsy, K. (2015) · The Journal of Heart and Lung Transplantation · doi:10.1016/j.healun.2015.05.007 · Cited by 119 · see citing works
Diphenyleneiodonium acutely inhibits reactive oxygen species production by mitochondrial complex I during reverse, but not forward electron transport
Lambert, A. J., Buckingham, J. A., Boysen, H. M., & Brand, M. D. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.03.005 · Cited by 118 · see citing works
Self-citation
Superoxide production and electron transport in mitochondrial oxidation of dihydroorotic acid
Forman, H. J., & Kennedy, J. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41421-x · Cited by 115 · see citing works
Mitochondrial glutathione depletion reveals a novel role for the pyruvate dehydrogenase complex as a key H2O2-emitting source under conditions of nutrient overload
Fisher‐Wellman, K. H., Gilliam, L. A. A., Lin, C., Cathey, B. L., Lark, D. S., & Neufer, P. D. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.09.008 · Cited by 115 · see citing works
The topology of superoxide production by complex III and glycerol 3-phosphate dehydrogenase in Drosophila mitochondria
Miwa, S., & Brand, M. D. (2005) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2005.08.003 · Cited by 114 · see citing works
Self-citation
Reactive oxygen species mediate cognitive deficits in experimental temporal lobe epilepsy
Pearson-Smith, J. N., Rowley, S. D., Liang, L., White, A. M., Day, B. J., & Patel, M. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.07.005 · Cited by 112 · see citing works
Characteristics of α‐glycerophosphate‐evoked H2O2 generation in brain mitochondria
Tretter, L., Takacs, K., Hegedus, V., & Ádám‐Vizi, V. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04223.x · Cited by 109 · see citing works
Glycerophosphate-Dependent Hydrogen Peroxide Production by Brown Adipose Tissue Mitochondria and Its Activation by Ferricyanide
Drahota, Z., Chowdhury, S. R., Floryk, D., Mráček, T., Wilhelm, J., Rauchová, H., Lenaz, G., & Houštěk, J. (2002) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1015123908918 · Cited by 106 · see citing works
Induction of mitochondrial manganese superoxide dismutase in macrophages by oxidized LDL: its relevance in atherosclerosis of humans and heritable hyperlipidemic rabbits
Kinscherf, R., Deigner, H., Usinger, C., Pill, J., Wagner, M., Kamencic, H., Hou, D., Chen, M., Schmiedt, W., Schrader, M., et al. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.14.9409551 · Cited by 105 · see citing works
The ubiquinone-binding site of the Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase is a source of superoxide.
Guo, J., & Lemire, B. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306312200 · Cited by 103 · see citing works
Metallothionein isoform 2A expression is inducible and protects against ROS-mediated cell death in rotenone-treated HeLa cells
Reinecke, F., Levanets, O., Olivier, Y., et al. (2006) · Biochemical Journal · doi:10.1042/bj20051253 · Cited by 102 · see citing works
The Determination and Analysis of Site-Specific Rates of Mitochondrial Reactive Oxygen Species Production
Quinlan, C. L., Perevoschikova, I. V., Goncalves, R. L. S., Hey‐Mogensen, M., & Brand, M. D. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-405883-5.00012-0 · Cited by 98 · see citing works
Self-citation
Tetrahydrobiopterin Scavenges Superoxide in Dopaminergic Neurons
Nakamura, K., Bindokas, V. P., Kowlessur, D., Elas, M., Milstien, S., Marks, J. D., Halpern, H. J., & Kang, U. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103766200 · Cited by 95 · see citing works
External alternative NADH dehydrogenase of Saccharomyces cerevisiae: a potential source of superoxide
Fang, J. S., & Beattie, D. S. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01328-x · Cited by 94 · see citing works
Cytopathies involving mitochondrial complex II
Ackrell, B. A. C. (2002) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(02)00012-2 · Cited by 86 · see citing works
Hydrogen peroxide efflux from muscle mitochondria underestimates matrix superoxide production – a correction using glutathione depletion
Treberg, J. R., Quinlan, C. L., & Brand, M. D. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07693.x · Cited by 85 · see citing works
Self-citation
Production of superoxide/H2O2 by dihydroorotate dehydrogenase in rat skeletal muscle mitochondria
Hey‐Mogensen, M., Goncalves, R. L. S., Orr, A. L., & Brand, M. D. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.04.007 · Cited by 84 · see citing works
Self-citation
Inhibitors of ros production by the ubiquinone-binding site of mitochondrial complex i identified by chemical screening
Orr, A. L., Ashok, D., Sarantos, M. R., Shi, T., Hughes, R. E., & Brand, M. D. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.08.170 · Cited by 80 · see citing works
Self-citation
High efficiency of ROS production by glycerophosphate dehydrogenase in mammalian mitochondria
Mráček, T., Pecinová, A., Vrbacký, M., et al. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.10.011 · Cited by 79 · see citing works
Sources of superoxide/H2O2 during mitochondrial proline oxidation
Goncalves, R. L. S., Rothschild, D. E., Quinlan, C. L., Scott, G. K., Benz, C. C., & Brand, M. D. (2014) · Redox Biology · doi:10.1016/j.redox.2014.07.003 · Cited by 79 · see citing works
Self-citation
Scavenging of H2O2 by mouse brain mitochondria
Starkov, A. A., Andreyev, A. Y., Zhang, S. F., Starkova, N. N., Korneeva, M., Syromyatnikov, M., & Popov, V. N. (2014) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-014-9581-9 · Cited by 78 · see citing works
Low complex I content explains the low hydrogen peroxide production rate of heart mitochondria from the long‐lived pigeon,Columba livia
Lambert, A. J., Buckingham, J. A., Boysen, H. M., & Brand, M. D. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00538.x · Cited by 70 · see citing works
Self-citation
Role of Mitochondria in Alcoholic Liver Disease
García‐Ruiz, C., Kaplowitz, N., & Fernández-Checa, J. C. (2013) · Current Pathobiology Reports · doi:10.1007/s40139-013-0021-z · Cited by 70 · see citing works
Production of superoxide/hydrogen peroxide by the mitochondrial 2-oxoadipate dehydrogenase complex
Goncalves, R. L. S., Bunik, V. I., & Brand, M. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.12.020 · Cited by 70 · see citing works
Self-citation
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Moruzzi, N., Valladolid-Acebes, I., Kannabiran, S. A., Bulgaro, S., Burtscher, I., Leibiger, B., Leibiger, I. B., Berggren, P.-O., & Brismar, K. (2022) · Life Science Alliance · doi:10.26508/lsa.202201505 · Cited by 27 · see citing works
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Hancock, J. T. (2021) · Oxygen · doi:10.3390/oxygen1010002 · Cited by 24 · see citing works
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Valentine, J. M., Li, M. E., Shoelson, S. E., Zhang, N., Reddick, R. L., & Musi, N. (2020) · The Journals of Gerontology: Series A · doi:10.1093/gerona/gly262 · Cited by 23 · see citing works

Regulation of Superoxide Anion Production by NADPH Oxidase in Monocytes/Macrophages
Cathcart, M. K. (2003) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000097769.47306.12 · Cited by 365 · see citing works
Bowman-Birk Inhibitor Suppresses Production of Superoxide Anion Radicals in Differentiated HL-60 Cells
Ware, J. H., Wan, X. S., & Kennedy, A. R. (1999) · Nutrition and Cancer · doi:10.1207/s15327914nc330209 · Cited by 24 · see citing works
Activation and Activity of the Superoxide-Generating System of Neutophils from Human Infants
Strauss, R. G., & Snyder, E. L. (1983) · Pediatric Research · doi:10.1203/00006450-198308000-00011 · Cited by 30 · see citing works
Brain Superoxide Anion Generation in Asphyxiated Piglets and the Effect of Indomethacin at Therapeutic Dose
Pourcyrous, M., Leffler, C. W., Bada, H. S., et al. (1993) · Pediatric Research · doi:10.1203/00006450-199309000-00025 · Cited by 83 · see citing works
[The changes in superoxide anion production in neutrophils on ischemia-reperfusion].
Midorikawa, Y., & Ogata, H. (1994) · PubMed

Authors: Brand, M. D.
Affiliations: Buck Institute for Research on Aging (US)
Corresponding author: Brand, Martin D.
ORCID: Brand, Martin D.
Venue: Free Radical Biology and Medicine
Publisher: Elsevier BV
Published: 2016-11
Volume: 100
Pages: 14-31
ISSN: 0891-5849 (ISSN-L)
DOI: 10.1016/j.freeradbiomed.2016.04.001
OpenAlex: W2336416528
Cited by: 1,063
References: 199
Citations by year: 2026: 106 · 2025: 109 · 2024: 104 · 2023: 93 · 2022: 125 · 2021: 156 · 2020: 126 · 2019: 98 · 2018: 75 · 2017: 54 · 2016: 15 · 2013: 1
FWCI: 7.30
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Free Radical Biology and Medicine (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
Keywords: mitochondrial superoxide, hydrogen peroxide, mitochondrial redox signaling, reactive oxygen species, electron leak, complex I, cytochrome bc1 complex, complex II, glycerol-3-phosphate dehydrogenase, reverse electron transfer, hypoxia signaling, endoplasmic reticulum stress, oxidative damage, skeletal muscle mitochondria, antioxidant defense
MeSH terms: Animals, Hydrogen Peroxide, Mitochondria, Oxidation-Reduction, Superoxides, Signal Transduction, Rats

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Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling

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