The mechanism of mitochondrial superoxide production by the cytochrome bc1 complex
Open accessAbstract
Production of reactive oxygen species (ROS) by the mitochondrial respiratory chain is considered to be one of the major causes of degenerative processes associated with oxidative stress. Mitochondrial ROS has also been shown to be involved in cellular signaling. It is generally assumed that ubisemiquinone formed at the ubiquinol oxidation center of the cytochrome bc(1) complex is one of two sources of electrons for superoxide formation in mitochondria. Here we show that superoxide formation at the ubiquinol oxidation center of the membrane-bound or purified cytochrome bc(1) complex is stimulated by the presence of oxidized ubiquinone indicating that in a reverse reaction the electron is transferred onto oxygen from reduced cytochrome b(L) via ubiquinone rather than during the forward ubiquinone cycle reaction. In fact, from mechanistic studies it seems unlikely that during normal catalysis the ubisemiquinone intermediate reaches significant occupancies at the ubiquinol oxidation site. We conclude that cytochrome bc(1) complex-linked ROS production is primarily promoted by a partially oxidized rather than by a fully reduced ubiquinone pool. The resulting mechanism of ROS production offers a straightforward explanation of how the redox state of the ubiquinone pool could play a central role in mitochondrial redox signaling.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In coupled mitochondria and submitochondrial particles, high ROS production with saturating succinate is largely attributable to complex I via reverse electron transfer from complex II, because it is sensitive to complex I inhibitors, requires high membrane potential, and does not occur in uncoupled submitochondrial particles.
“In coupled mitochondria and SMP, high ROS production is observed under these conditions, but this can be largely attributed to complex I due to reverse electron transfer from complex II, since (i) it is sensitive to complex I inhibitors like rotenone [18][19][20]24,91,92], (ii) requires a high membrane potential, i.e. is sensitive to uncouplers and ionophores [15,[18][19][20]91] or ADP (that”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [32]
The ROS-promoting effect of complex II inhibitors can be explained by a partially oxidized Q-pool that maximizes complex III ROS production during antimycin inhibition.
“This ROS-promoting effect of complex II inhibitors can be related to a partially oxidized Q-pool that maximizes ROS production by complex III upon antimycin inhibition [25,32,33].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [32]
Increased oxidation of the Q-pool explains the increased ROS generation by antimycin A-inhibited complex III, because superoxide generation at the Qo site is maximal at intermediate reduction states of the ubiquinone pool when the Qi site is blocked.
“This can be explained by an increased oxidation of the Q-pool, since it was shown that the superoxide generation at the Q o site is maximal at intermediate reduction states of the ubiquinone pool if the Q i site is blocked by antimycin A [25,32,33].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [32]
Under these specific conditions, an intermediate succinate concentration/complex II activity results in an intermediate reduction of the Q-pool that favors superoxide production by complex III.
“Under these specific conditions, an intermediate succinate concentration/complex II activity results in an intermediate reduction of the Q-pool that favors superoxide production by complex III [32].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [32]
Mitochondrial cytochrome bc1 (complex III) inhibition is a major source of intracellular ROS generation.
“Mitochondrial cytochrome bc1 (complex III) inhibition is a major source of intracellular ROS generation [59].”
From Lansoprazole interferes with fungal respiration and acts synergistically with amphotericin B against multidrug-resistant <i>Candida auris</i> (2024) · cites this paper as [59]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Fridovich (1978) · doi:10.1126/science.210504 · Cited by 3,329 · see citing works
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
Production of Reactive Oxygen Species by Mitochondria
Chen, Q., Vazquez, E. J., Moghaddas, S., Hoppel, C. L., & Lesnefsky, E. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304854200 · Cited by 1,616 · see citing works
Neurodegenerative diseases and oxidative stress
Emerit, J., Edeas, M. A., & Bricaire, F. (2003) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2003.11.004 · Cited by 1,031 · see citing works
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
Vanden Hoek, T. L., Becker, L. B., Shao, Z., Li, C., & Schumacker, P. T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.29.18092 · Cited by 721 · see citing works
Kußmaul, L., & Hirst, J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510977103 · Cited by 720 · see citing works
Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
Boveris, A., Cadenas, E., & Stoppani, A. O. M. (1976) · Biochemical Journal · doi:10.1042/bj1560435 · Cited by 655 · see citing works
Bell, E. L., Klimova, T. A., Eisenbart, J., Moraes, C. T., Murphy, M. P., Budinger, G. R. S., & Chandel, N. S. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200609074 · Cited by 568 · see citing works
Are reactive oxygen species involved in Alzheimer's disease?
Benzi, G. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00066-n · Cited by 365 · see citing works
The Protonmotive Q Cycle in Mitochondria and Bacteria
Brandt, U., & Trumpower, B. L. (1994) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239409086800 · Cited by 354 · see citing works
Self-citationDistribution and redox state of ubiquinones in rat and human tissues
Åberg, F. O., Appelkvist, E., Dallner, G., & Ernster, L. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90511-t · Cited by 315 · see citing works
Okun, J. G., Lümmen, P., & Brandt, U. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.5.2625 · Cited by 308 · see citing works
Self-citationOxidoreduction of cytochrome b in the presence of antimycin
Wikström, M. K. F., & BERDEN, J. A. (1972) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(72)90258-7 · Cited by 280 · see citing works
Reversible redox energy coupling in electron transfer chains
Osyczka, A., Moser, C. C., Daldal, F., & Dutton, P. L. (2004) · Nature · doi:10.1038/nature02242 · Cited by 266 · see citing works
Osyczka, A., Moser, C. C., & Dutton, P. L. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.02.001 · Cited by 217 · see citing works
Cape, J. L., Bowman, M. K., & Kramer, D. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702621104 · Cited by 172 · see citing works
Muller, F., Crofts, A. R., & Kramer, D. M. (2002) · Biochemistry · doi:10.1021/bi025581e · Cited by 163 · see citing works
Galkin, A. S., & Brandt, U. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504709200 · Cited by 162 · see citing works
Self-citationSuperoxide anion generation by the cytochrome bc1 complex
Sun, J. L., & Trumpower, B. L. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.08.028 · Cited by 159 · see citing works
A new species of bound ubisemiquinone anion in QH2: cytochrome c oxidoreductase.
de Vries, S., Albracht, S. P. J., BERDEN, J. A., & Slater, E. C. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43222-x · Cited by 132 · see citing works
Architecture of the QoSite of the Cytochromebc1Complex Probed by Superoxide Production
Müller, F. L., Roberts, A. G., Bowman, M. K., & Kramer, D. (2003) · Biochemistry · doi:10.1021/bi0342160 · Cited by 132 · see citing works
Dröse, S., Brandt, U., & Hanley, P. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602570200 · Cited by 105 · see citing works
Self-citationCrofts, A. R. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2003.10.012 · Cited by 104 · see citing works
Evidence for a Concerted Mechanism of Ubiquinol Oxidation by the Cytochrome bc 1 Complex
Snyder, C. H., Gutiérrez-Cirlos, E. B., & Trumpower, B. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.18.13535 · Cited by 101 · see citing works
Exposing the Complex III Qo semiquinone radical
Zhang, H., Osyczka, A., Dutton, P. L., & Moser, C. C. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.04.004 · Cited by 95 · see citing works
Horvat, S., Beyer, C., & Arnold, S. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04134.x · Cited by 90 · see citing works
Wan, Y., Williams, R. H., Folkers, K., Leung, K. H., & Racker, E. (1975) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(75)80003-9 · Cited by 87 · see citing works
Kudin, A. P., Dębska–Vielhaber, G., & Kunz, W. S. (2005) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2005.03.012 · Cited by 78 · see citing works
Forquer, I., Covián, R., Bowman, M. K., Trumpower, B. L., & Kramer, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605119200 · Cited by 77 · see citing works
Brandt, U. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00078-4 · Cited by 61 · see citing works
Self-citationGalinier, A., Carrière, A., Fernandez, Y., Bessac, A. M., Caspar‐Bauguil, S., Périquet, B., Comtat, M., Thouvenot, J. P., & Casteilla, L. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.10.067 · Cited by 49 · see citing works
Erecińska, M., & Wilson, D. F. (1976) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(76)90333-7 · Cited by 41 · see citing works
Engel, W. D., Schägger, H., & von JAGOW, G. (1983) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1983.364.2.1753 · Cited by 34 · see citing works
Cape, J. L., Strahan, J. R., Lenaeus, M. J., Yuknis, B., Le, T. T., Shepherd, J. N., Bowman, M. K., & Kramer, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507616200 · Cited by 32 · see citing works
Flagged first, then by citations
Research works printed but not linked: 2
- Kussmaul, L., and Hirst, J. (2006) Proc. Natl. Acad. Sci. U. S. A. 103, 7607-7612
- Cape, J. L., Bowman, M. K., and Kramer, D. M. (2007) Proc. Natl. Acad. Sci.
Cited by
Sorted by citations
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
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
Brand, M. D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.001 · Cited by 1,063 · see citing works
Scharping, N. E., Rivadeneira, D. B., Menk, A. V., Vignali, P. D. A., Ford, B. R., Rittenhouse, N. L., Peralta, R., Wang, Y., Wang, Y., DePeaux, K., et al. (2021) · Nature Immunology · doi:10.1038/s41590-020-00834-9 · Cited by 897 · see citing works
Oxidative stress in the aging substantia nigra and the etiology of Parkinson's disease
Trist, B. G., Hare, D. J., & Double, K. L. (2019) · Aging Cell · doi:10.1111/acel.13031 · Cited by 778 · see citing works
Sivitz, W. I., & Yorek, M. A. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2531 · Cited by 742 · see citing works
Hypoxic Pulmonary Vasoconstriction
Sylvester, J. T., Shimoda, L. A., Aaronson, P. I., & Ward, J. P. T. (2012) · Physiological Reviews · doi:10.1152/physrev.00041.2010 · Cited by 727 · 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
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
Mitochondria-Ros Crosstalk in the Control of Cell Death and Aging
Marchi, S., Giorgi, C., Suski, J. M., Agnoletto, C., Bononi, A., Bonora, M., Marchi, E. D., Missiroli, S., Patergnani, S., Poletti, F., et al. (2011) · Journal of Signal Transduction · doi:10.1155/2012/329635 · Cited by 639 · see citing works
Bactericidal Antibiotics Induce Mitochondrial Dysfunction and Oxidative Damage in Mammalian Cells
Kalghatgi, S., Spina, C. S., Costello, J. C., Liesa, M., Morones‐Ramírez, J. R., Slomovic, S., Molina, A. J. A., Shirihai, O. S., & Collins, J. J. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3006055 · Cited by 565 · 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
Self-citationOxidative stress and cellular pathologies in Parkinson’s disease
Puspita, L., Chung, S. Y., & Shim, J. (2017) · Molecular Brain · doi:10.1186/s13041-017-0340-9 · Cited by 486 · see citing works
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
Figueira, T. R., de Barros, M. H., Camargo, A. A., Castilho, R. F., Ferreira, J. C. B., Kowaltowski, A. J., Sluse, F. E., de Souza-Pinto, N. C., & Vercesi, A. E. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4729 · Cited by 417 · see citing works
Generation of Reactive Oxygen Species by Mitochondria
Hernansanz‐Agustín, P., & Enrı́quez, J. A. (2021) · Antioxidants · doi:10.3390/antiox10030415 · Cited by 414 · see citing works
Kellner, M., Noonepalle, S. K. R., Lü, Q., Srivastava, A., Zemskov, E. A., & Black, S. M. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-63245-2_8 · Cited by 411 · see citing works
Superoxide generation by complex III: From mechanistic rationales to functional consequences
Bleier, L., & Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.12.002 · Cited by 369 · see citing works
Self-citationKausar, S., Wang, F., & Cui, H. (2018) · Cells · doi:10.3390/cells7120274 · Cited by 315 · see citing works
Rutherford, A. W., Osyczka, A., & Rappaport, F. (2012) · FEBS Letters · doi:10.1016/j.febslet.2011.12.039 · Cited by 272 · see citing works
Daiber, A., Lisa, F. D., Oelze, M. W., Kröller‐Schön, S., Steven, S., Schulz, E., & Münzel, T. F. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13403 · Cited by 271 · see citing works
OXPHOS mutations and neurodegeneration
Koopman, W. J. H., Distelmaier, F., Smeitink, J. A. M., & Willems, P. H. G. M. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.300 · Cited by 254 · see citing works
Rekatsina, M., Paladini, A., Piroli, A., Zis, P., Pergolizzi, J. V., & Varrassi, G. (2019) · Advances in Therapy · doi:10.1007/s12325-019-01148-5 · Cited by 254 · see citing works
Loss of Mitochondrial Function Impairs Lysosomes
Demers-Lamarche, J., Guillebaud, G., Tlili, M., Todkar, K. J., Bélanger, N., Grondin, M., Nguyen, A., Michel, J. J. C., & Germain, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.695825 · Cited by 242 · see citing works
Mitochondrial Respiratory Chain Complexes
Sousa, J. S., D’Imprima, E., & Vonck, J. (2018) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-10-7757-9_7 · Cited by 239 · see citing works
Hazan, R., Que, Y., Maura, D., Strobel, B., Majcherczyk, P. A., Hopper, L. R., Wilbur, D. J., Hreha, T. N., Barquera, B., & Rahme, L. G. (2016) · Current Biology · doi:10.1016/j.cub.2015.11.056 · Cited by 226 · see citing works
Oxidative stress factors in Parkinson’s disease
Dorszewska, J., Kowalska, M., Prendecki, M., Piekut, T., Kozłowska, J., & Kozubski, W. P. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.300980 · Cited by 211 · see citing works
Origin and Consequences of Necroinflammation
Sarhan, M., Land, W. G., Tonnus, W., Hugo, C., & Linkermann, A. (2018) · Physiological Reviews · doi:10.1152/physrev.00041.2016 · Cited by 210 · see citing works
Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.01.004 · Cited by 201 · see citing works
Self-citationThe 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
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
Self-citationSanchez, V., Feinstein, S. D., Lunardi, N., Joksovic, P. M., Boscolo, A., Todorovic, S. M., & Jevtović‐Todorović, V. (2011) · Anesthesiology · doi:10.1097/aln.0b013e3182303a63 · Cited by 180 · see citing works
Modelling mitochondrial ROS production by the respiratory chain
Mazat, J., Devin, A., & Ransac, S. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03381-1 · Cited by 180 · see citing works
Antimicrobial-associated harm in critical care: a narrative review
Arulkumaran, N., Routledge, M., Schlebusch, S., Lipman, J., & Conway Morris, A. (2020) · Intensive Care Medicine · doi:10.1007/s00134-020-05929-3 · Cited by 175 · see citing works
Belyaeva, E. A., Соколова, Т. В., Emelyanova, L. V., & Zakharova, I. O. (2012) · The Scientific World JOURNAL · doi:10.1100/2012/136063 · Cited by 173 · see citing works
Sarewicz, M., & Osyczka, A. (2014) · Physiological Reviews · doi:10.1152/physrev.00006.2014 · Cited by 173 · see citing works
OXPHOS gene expression and control in mitochondrial disorders
Reinecke, F., Smeitink, J. A. M., & van der Westhuizen, F. H. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.04.003 · Cited by 170 · see citing works
Transplantation and Damage-Associated Molecular Patterns (DAMPs)
Land, W. G., Agostinis, P., Gasser, S., Garg, A. D., & Linkermann, A. (2016) · American Journal of Transplantation · doi:10.1111/ajt.13963 · Cited by 166 · see citing works
Barjaktarović, Ž., Schmaltz, D., Shyla, A., Azimzadeh, O., Schulz, S., Haagen, J., Dörr, W., Sarioglu, H., Schäfer, A., Atkinson, M. J., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027811 · Cited by 163 · see citing works
Toxicity of depleted uranium on isolated rat kidney mitochondria
Shaki, F., Hosseini, M., Ghazi‐Khansari, M., & Pourahmad, J. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.08.015 · Cited by 156 · see citing works
The Role of Mitochondria-Derived Reactive Oxygen Species in Hyperthermia-Induced Platelet Apoptosis
Wang, Z., Cai, F., Chen, X., Luo, M., Hu, L., & Lu, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075044 · Cited by 155 · see citing works
“As a positive control, washed platelets were incubated with antimycin A, which is known to increase mitochondrial ROS production [35].”
Redox Control of the Survival of Healthy and Diseased Cells
Zhang, Y., Du, Y., Le, W., Wang, K., Kieffer, N., & Zhang, J. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3685 · Cited by 156 · see citing works
Leuner, K., Müller, W. E., & Reichert, A. S. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8307-4 · Cited by 155 · see citing works
Role of phospholipids in respiratory cytochrome bc1 complex catalysis and supercomplex formation
Wenz, T., Hielscher, R., Hellwig, P., Schägger, H., Richers, S., & Hunte, C. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.02.012 · Cited by 154 · see citing works
Mitochondrial respiratory chain complexes as sources and targets of thiol-based redox-regulation
Dröse, S., Brandt, U., & Wittig, I. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.02.006 · Cited by 153 · see citing works
Self-citationMitochondrial ROS and involvement of Bcl-2 as a mitochondrial ROS regulator
Chong, S. J. F., Low, I. C. C., & Pervaiz, S. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.06.002 · Cited by 142 · see citing works
Ischemic A/D transition of mitochondrial complex I and its role in ROS generation
Dröse, S., Степанова, А., & Galkin, A. S. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.12.013 · Cited by 137 · see citing works
Self-citationA Review on Oxidative Stress, Diabetic Complications, and the Roles of Honey Polyphenols
Pasupuleti, V. R., Arigela, C. S., Gan, S. H., Salam, S. K. N. M., Krishnan, K. T., Rahman, N. A., & Jeffree, M. S. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/8878172 · Cited by 135 · see citing works
Sarewicz, M., Pintscher, S., Pietras, R., Borek, A., Bujnowicz, Ł., HANKE, G. T., Cramer, W. A., Finazzi, G., & Osyczka, A. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00712 · Cited by 130 · see citing works
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
Self-citationJeong, E. M., Yoon, J., Lim, J., Shin, J., Cho, A. Y., Heo, J., Lee, K. B., Lee, J.-H., Lee, W. J., Kim, H.-J., et al. (2018) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.12.007 · Cited by 130 · see citing works
Wu, J., Sun, Y., Zhao, Y., Zhang, J., Luo, L., Li, M., Wang, J., Yu, H. J., Liu, G., Yang, L., et al. (2015) · Cell Research · doi:10.1038/cr.2015.46 · Cited by 129 · see citing works
Chowdhury, A. R., Zielonka, J., Kalyanaraman, B., Hartley, R. C., Murphy, M. P., & Avadhani, N. G. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101606 · Cited by 128 · see citing works
Kadenbach, B., Ramzan, R., Wen, L., & Vogt, S. K. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.04.019 · Cited by 128 · see citing works
Dong, L., Freeman, R., Liu, J., Zobalová, R., Marín‐Hernández, Á., Stantic, M., Rohlena, J., Vališ, K., Rodríguez‐Enríquez, S., Butcher, B., et al. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-2439 · Cited by 125 · see citing works
Ralph, S. J., Moreno-Sánchez, R., Neuzil, J., & Rodríguez-Enríquez, S. (2011) · Pharmaceutical Research · doi:10.1007/s11095-011-0566-7 · Cited by 126 · see citing works
The Interplay Between Respiratory Supercomplexes and ROS in Aging
Genova, M. L., & Lenaz, G. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6214 · Cited by 126 · see citing works
An Electronic Bus Bar Lies in the Core of Cytochrome bc 1
Świerczek, M., Cieluch, E., Sarewicz, M., Borek, A., Moser, C. C., Dutton, P. L., & Osyczka, A. (2010) · Science · doi:10.1126/science.1190899 · Cited by 122 · see citing works
Jung, H. J., Shim, J. S., Lee, J., Song, Y., Park, K. C., Choi, S. H., Kim, N. D., Yoon, J. H., Mungai, P. T., Schumacker, P. T., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.087809 · Cited by 121 · see citing works
Mitochondrial ROS and mitochondria-targeted antioxidants in the aged heart
Bou‐Teen, D., Kaludercic, N., Weissman, D., Turan, B., Maack, C., Lisa, F. D., & Ruiz‐Meana, M. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.02.043 · Cited by 119 · see citing works
Arnold, S. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.05.003 · Cited by 117 · see citing works
Martin, A., Byrne, A., Burke, C. S., Forster, R. J., & Keyes, T. E. (2014) · Journal of the American Chemical Society · doi:10.1021/ja508043q · Cited by 117 · see citing works
El‐Khoury, R., Dufour, É., Rak, M., Ramanantsoa, N., Grandchamp, N., Csaba, Z., Duvillié, B., Bénit, P., Gallego, J., Gressèns, P., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003182 · Cited by 116 · see citing works
Salicylic Acid-Dependent Plant Stress Signaling via Mitochondrial Succinate Dehydrogenase
Belt, K., Huang, S., Thatcher, L. F., Casarotto, H. J., Singh, K. B., Aken, O. V., & Millar, A. H. (2017) · PLANT PHYSIOLOGY · doi:10.1104/pp.16.00060 · Cited by 107 · see citing works
The role of mitochondrial membrane potential in ischemic heart failure
Kadenbach, B., Ramzan, R., Moosdorf, R., & Vogt, S. K. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.06.001 · Cited by 103 · see citing works
Rottenberg, H., Covián, R., & Trumpower, B. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.017376 · Cited by 102 · see citing works
Gould, N. S., White, C. W., & Day, B. J. (2008) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.108.145037 · Cited by 101 · see citing works
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
Low-oxygen response is triggered by an ATP-dependent shift in oleoyl-CoA in Arabidopsis
Schmidt, R., Fulda, M. S., Paul, M. V., Anders, M., Plum, F., Weits, D. A., Kosmacz, M., Larson, T. R., Graham, I. A., Beemster, G. T. S., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1809429115 · Cited by 97 · see citing works
Degenerative diseases, oxidative stress and cytochrome c oxidase function
Kadenbach, B., Ramzan, R., & Vogt, S. K. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.02.004 · Cited by 97 · see citing works
Mitochondrial production of reactive oxygen species
Grivennikova, V. G., & Vinogradov, A. D. (2013) · Biochemistry (Moscow) · doi:10.1134/s0006297913130087 · Cited by 96 · see citing works
Carvalho, L., Luque-Ortega, J. R., Manzano, J. I., Castanys, S., Rivas, L., & Gamarro, F. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00790-10 · Cited by 97 · see citing works
Cela, O., Piccoli, C., Scrima, R., Quarato, G., Marolla, A., Cinnella, G., DAMBROSIO, M., & Capitanio, N. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.05.005 · Cited by 95 · see citing works
Mitochondrial superoxide production contributes to vancomycin-induced renal tubular cell apoptosis
Arimura, Y., Yano, T., Hirano, M., Sakamoto, Y., Egashira, N., & Oishi, R. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.038 · Cited by 94 · see citing works
Anticancer Drugs Targeting the Mitochondrial Electron Transport Chain
Rohlena, J., Dong, L.-F., Ralph, S. J., & Neuzil, J. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.3990 · Cited by 91 · see citing works
NLR-Dependent Regulation of Inflammation in Multiple Sclerosis
Gharagozloo, M., Gris, K. V., Mahvelati, T. M., Amrani, A., Lukens, J. R., & Gris, D. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2017.02012 · Cited by 91 · see citing works
Üremiş, N., & Üremi̇ş, M. M. (2025) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.70133 · Cited by 98 · see citing works
Wang, Z., Chen, L., Huang, Y., Luo, M., Wang, H., Jiang, Z., Zheng, J., Yang, Z., Chen, Z., Zhang, C., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102082 · Cited by 90 · see citing works
Ascochlorin is a novel, specific inhibitor of the mitochondrial cytochrome bc1 complex
Berry, E. A., Huang, L.-S., Lee, D., Daldal, F., Nagai, K., & Minagawa, N. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.12.003 · Cited by 89 · see citing works
Johnson, J. D., & Hill, G. E. (2012) · Biochimie · doi:10.1016/j.biochi.2012.10.021 · Cited by 87 · see citing works
Lozano, O., Lázaro‐Alfaro, A., Silva‐Platas, C., Oropeza‐Almazán, Y., Torres‐Quintanilla, A., Bernal‐Ramírez, J., Alves‐Figueiredo, H., & García‐Rivas, G. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/7683051 · Cited by 86 · see citing works
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
Munro, D., Banh, S., Sotiri, E., Tamanna, N., & Treberg, J. R. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.014 · Cited by 83 · see citing works
Bottani, E., Cerutti, R., Harbour, M. E., Ravaglia, S., Doğan, Ş. A., Giordano, C., Fearnley, I. M., d’Amati, G., Viscomi, C. F., Fernández‐Vizarra, E., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.001 · Cited by 82 · see citing works
Nesci, S., Trombetti, F., Pagliarani, A., Ventrella, V., Algieri, C., Tioli, G., & Lenaz, G. (2021) · Life · doi:10.3390/life11030242 · Cited by 80 · see citing works
Alpha-Synuclein and Mitochondrial Dysfunction in Parkinson’s Disease: The Emerging Role of VDAC
Risiglione, P., Zinghirino, F., Rosa, M. C. D., Magrì, A., & Messina, A. A. (2021) · Biomolecules · doi:10.3390/biom11050718 · Cited by 79 · see citing works
Lanciano, P., Khalfaoui-Hassani, B., Selamoglu, N., Ghelli, A. M., Rugolo, M., & Daldal, F. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.03.009 · Cited by 80 · see citing works
Lustgarten, M. S., Jang, Y. C., Liu, Y., Müller, F. L., Qi, W., Steinhelper, M. E., Brooks, S. V., Larkin, L. M., Shimizu, T., Shirasawa, T., et al. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00372.2009 · Cited by 78 · see citing works
Hirata, N., Shim, Y. H., Pravdić, D., Lohr, N. L., Pratt, P. F., Weihrauch, D., Kersten, J. R., Warltier, D. C., Bosnjak, Z. J., & Bienengraeber, M. (2011) · Anesthesiology · doi:10.1097/aln.0b013e31822a2316 · Cited by 78 · see citing works
Sakamoto, Y., Yano, T., Hanada, Y., Takeshita, A., Inagaki, F., Masuda, S., Matsunaga, N., Koyanagi, S., & Ohdo, S. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.02.025 · Cited by 77 · see citing works
Yonamine, R., Satoh, Y., Kodama, M., Araki, Y., & Kazama, T. (2012) · Anesthesiology · doi:10.1097/aln.0b013e318275146d · Cited by 77 · see citing works
Choi, E. M. (2011) · Food and Chemical Toxicology · doi:10.1016/j.fct.2011.04.031 · Cited by 77 · see citing works
Dibrova, D. V., Cherepanov, D. A., Galperin, M. Y., Skulachev, V. P., & Mulkidjanian, A. Y. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.07.006 · Cited by 76 · see citing works
Tikunov, A. P., Johnson, C. B., Pediaditakis, P., Markevich, N. I., Macdonald, J. M., Lemasters, J. J., & Holmuhamedov, E. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.01.008 · Cited by 74 · see citing works
Cytochrome c Oxidase and Its Role in Neurodegeneration and Neuroprotection
Arnold, S. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3573-0_13 · Cited by 75 · see citing works
What are the sources of hydrogen peroxide production by heart mitochondria?
Grivennikova, V. G., Kareyeva, A. V., & Vinogradov, A. D. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.013 · Cited by 74 · see citing works
Effects of brevetoxin exposure on the immune system of loggerhead sea turtles
Walsh, C. J., Leggett, S. R., Carter, B. J., & Colle, C. F. (2009) · Aquatic Toxicology · doi:10.1016/j.aquatox.2009.12.014 · Cited by 73 · see citing works
Baniulis, D., Hasan, S. S., Stofleth, J. T., & Cramer, W. A. (2013) · Biochemistry · doi:10.1021/bi4013534 · Cited by 73 · see citing works
Song, M., Wu, H., Wu, S., Ge, T., Wang, G., Zhou, Y., Sheng, S., & Jiang, J. (2016) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2016.10.034 · Cited by 73 · see citing works
Dröse, S., Hanley, P. J., & Brandt, U. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.01.011 · Cited by 72 · see citing works
Self-citation
- Authors
- Dröse, S., & Brandt, U.
- Affiliations
- Goethe University Frankfurt (DE)
- Corresponding author
- Brandt, Ulrich
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2008-08
- Volume
- 283
- Issue
- 31
- Pages
- 21649-21654
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1982085892
- Cited by
- 386
- References
- 35
- Citations by year
- 2026: 7 · 2025: 13 · 2024: 19 · 2023: 10 · 2022: 11 · 2021: 21 · 2020: 22 · 2019: 14 · 2018: 27 · 2017: 22 · 2016: 29 · 2015: 24 · 2014: 24 · 2013: 22 · 2012: 27
- FWCI
- 12.88
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) (submittedVersion, cc-by)
- Funders
- Deutsche Forschungsgemeinschaft ((EXC 115).)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Keywords
- cytochrome bc1 complex, mitochondrial superoxide production, reactive oxygen species, ubisemiquinone, electron transfer to oxygen, mitochondrial respiratory chain, oxidative stress, mitochondrial redox signaling
- MeSH terms
- Animals, Catalysis, Cattle, Dose-Response Relationship, Drug, Electron Transport, Mitochondria, Models, Biological, Molecular Conformation, Oxidation-Reduction, Oxidoreductases, Oxygen, Superoxides, Electron Transport Complex III, Ubiquinone, Reactive Oxygen Species
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
