Cited by 394Redox biology and oxidative stressMitochondrial Function and PathologyCancer and biochemical research

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Mitochondrial ROS Generation and Its Regulation: Mechanisms Involved in H 2 O 2 Signaling

Rigoulet, Michel, Yoboue, Edgar D., Devin, Anne·2011·Antioxidants & Redox Signaling

DOI 10.1089/ars.2010.3363

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Abstract

Mitochondria are the main source of reactive oxygen species in the cell. These reactive oxygen species have long been known as being involved in oxidative stress. This is a review of the mechanisms involved in reactive oxygen species generation by the respiratory chain and some of the dehydrogenases and the control by thermodynamic and kinetic constraints. Mitochondrial ROS produced at the level of the bc1 complex as well at the level of complex I are discussed. It was recognized more than a decade ago that they can also function as signaling molecules. This signaling role will be developed both in terms of mechanism and in terms of mitochondrial ROS signaling. The notion that hydrogen peroxide acts not only as a damaging oxidant but also as a signaling molecule was proposed more than a decade ago. Hydrogen peroxide signaling can be either direct (oxidation of its target) or indirect (involving peroxiredoxins, for example). The consequences of ROS signaling on crucial biologic processes such as cell proliferation and differentiation are discussed. Antioxid. Redox Signal. 14, 459—468.

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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
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
A Mitochondrial Paradigm of Metabolic and Degenerative Diseases, Aging, and Cancer: A Dawn for Evolutionary Medicine
Wallace, D. C. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.39.110304.095751 · Cited by 3,185
NOX enzymes and the biology of reactive oxygen
Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125
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
Requirement for Generation of H 2 O 2 for Platelet-Derived Growth Factor Signal Transduction
Sundaresan, M., Yu, Z.-X., Ferrans, V. J., Irani, K., & Finkel, T. (1995) · Science · doi:10.1126/science.270.5234.296 · Cited by 2,520
Reactive Species and Antioxidants. Redox Biology Is a Fundamental Theme of Aerobic Life
Halliwell, B. B. (2006) · PLANT PHYSIOLOGY · doi:10.1104/pp.106.077073 · Cited by 2,402
H 2 O 2 , a Necessary Evil for Cell Signaling
Rhee, S. G. (2006) · Science · doi:10.1126/science.1130481 · Cited by 2,160
Mitochondrial Overload and Incomplete Fatty Acid Oxidation Contribute to Skeletal Muscle Insulin Resistance
Koves, T. R., Ussher, J. R., Noland, R. C., Slentz, D., Mosedale, M., Ilkayeva, O., Bain, J., Stevens, R., Dyck, J. R. B., Newgard, C. B., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.013 · Cited by 1,990
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
The cellular production of hydrogen peroxide
Boveris, A., Oshino, N., & Chance, B. (1972) · Biochemical Journal · doi:10.1042/bj1280617 · Cited by 1,549
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
Superoxide activates mitochondrial uncoupling proteins
Echtay, K. S., Roussel, D., St-Pierre, J., Jekabsons, M. B., Cadenas, S., Stuart, J. A., Harper, J. A., Roebuck, S. J., Morrison, A., Pickering, S., et al. (2002) · Nature · doi:10.1038/415096a · Cited by 1,382
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
Mitochondrial H2O2 emission and cellular redox state link excess fat intake to insulin resistance in both rodents and humans
Anderson, E. J., Lustig, M. E., Boyle, K. E., Woodlief, T. L., Kane, D. A., Lin, C.-T., Price, J. W., Kang, L., Rabinovitch, P. S., Szeto, H. H., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37048 · Cited by 1,253
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
Epidermal Growth Factor (EGF)-induced Generation of Hydrogen Peroxide
Bae, Y. S., Kang, S. W., Seo, M. S., Baines, I., Tekle, E., Chock, P. B., & Rhee, S. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.217 · Cited by 1,208
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
Hydrogen Peroxide: A Signaling Messenger
Stone, J. R., & Yang, S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.243 · Cited by 1,193
ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin
Biteau, B., Labarre, J., & Tolédano, M. B. (2003) · Nature · doi:10.1038/nature02075 · Cited by 970
A Thiol Peroxidase Is an H2O2 Receptor and Redox-Transducer in Gene Activation
Delaunay, A., Pflieger, D., Barrault, M., Vinh, J., & Tolédano, M. B. (2002) · Cell · doi:10.1016/s0092-8674(02)01048-6 · Cited by 902
Uncoupling: new approaches to an old problem of bioenergetics
Skulachev, V. P. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(97)00091-1 · Cited by 893
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
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
Activation of molecular oxygen by flavins and flavoproteins.
Massey, V. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31664-2 · Cited by 823
Mitochondrial dysfunction results from oxidative stress in the skeletal muscle of diet-induced insulin-resistant mice
Bonnard, C., Durand, A., Peyrol, S., Chanseaume, E., Chauvin, M.-A., Morio, B., Vidal, H., & Rieusset, J. (2008) · Journal of Clinical Investigation · doi:10.1172/jci32601 · Cited by 819
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 745
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 711
Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation–reduction state
Kushnareva, Y., Murphy, A. N., & Andreyev, A. Y. (2002) · Biochemical Journal · doi:10.1042/bj20021121 · Cited by 696
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
Inactivation of Peroxiredoxin I by Phosphorylation Allows Localized H2O2 Accumulation for Cell Signaling
Woo, H. A., Yim, S. H., Shin, D. H., Kang, D., Yu, D., & Rhee, S. G. (2010) · Cell · doi:10.1016/j.cell.2010.01.009 · Cited by 632
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
Plasma Acylcarnitine Profiles Suggest Incomplete Long-Chain Fatty Acid β-Oxidation and Altered Tricarboxylic Acid Cycle Activity in Type 2 Diabetic African-American Women
Adams, S. H., Hoppel, C. L., Lok, K. H., Zhao, L., Wong, S. W., Minkler, P. E., Hwang, D. H., Newman, J. W., & Garvey, W. T. (2009) · The Journal of Nutrition · doi:10.3945/jn.108.103754 · Cited by 598
A signalling role for 4‐hydroxy‐2‐nonenal in regulation of mitochondrial uncoupling
Echtay, K. S., Esteves, T. C., Pakay, J. L., Jekabsons, M. B., Lambert, A. J., Portero‐Otín, M., Pamplona, R., Vidal‐Puig, A. J., Wang, S., Roebuck, S. J., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg412 · Cited by 597
Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol—disulfide status
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
Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation
Woo, H. A., Chae, H. Z., Hwang, S. C., Yang, K., Kang, S. W., Kim, K., & Rhee, S. G. (2003) · Science · doi:10.1126/science.1080273 · Cited by 558
H2O2 sensing through oxidation of the Yap1 transcription factor
Delaunay, A., Isnard, A., & Tolédano, M. B. (2000) · The EMBO Journal · doi:10.1093/emboj/19.19.5157 · Cited by 540
High-fat diets cause insulin resistance despite an increase in muscle mitochondria
Hancock, C. R., Han, D.-H., Chen, M., Terada, S., Yasuda, T., Wright, D. C., & Holloszy, J. O. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802057105 · Cited by 538
Superoxide Dismutase Activity Is Essential for Stationary Phase Survival in Saccharomyces cerevisiae
Longo, V. D., Gralla, E. B., & Valentine, J. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.21.12275 · Cited by 531
Excess Lipid Availability Increases Mitochondrial Fatty Acid Oxidative Capacity in Muscle
Turner, N., Bruce, C. R., Beale, S. M., Hoehn, K. L., So, T., Rolph, M. S., & Cooney, G. J. (2007) · Diabetes · doi:10.2337/db07-0093 · Cited by 520
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 514
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
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
Evolution of Catalases from Bacteria to Humans
Zámocký, M., Furtmüller, P. G., & Obinger, C. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2046 · Cited by 467
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 · cited 1×
“More realistic predictions estimate that, under physiologic conditions, the superoxide production is around 0.1% of the respiratory rate (48, 95).”
Influential
Regulation of yAP‐1 nuclear localization in response to oxidative stress
Kuge, S., Jones, N., & Nomoto, A. (1997) · The EMBO Journal · doi:10.1093/emboj/16.7.1710 · Cited by 445
Localizing NADPH Oxidase–Derived ROS
Ushio‐Fukai, M. (2006) · Science s STKE · doi:10.1126/stke.3492006re8 · Cited by 397
Free Radicals in Medicine. I. Chemical Nature and Biologic Reactions
Southorn, P. A., & Powis, G. (1988) · Mayo Clinic Proceedings · doi:10.1016/s0025-6196(12)64861-7 · Cited by 391
Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin
Chae, H. Z., Kim, H. J., Kang, S. W., & Rhee, S. G. (1999) · Diabetes Research and Clinical Practice · doi:10.1016/s0168-8227(99)00037-6 · Cited by 390
Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: A mechanism for differential promoter selection
Tolédano, 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
The Interaction of Energy and Electron Transfer Reactions in Mitochondria
Chance, B., & Hollunger, G. (1961) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64210-3 · Cited by 364
Reactive oxygen species signaling in vascular smooth muscle cells
Clempus, R. E., & Griendling, K. K. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.02.033 · Cited by 362
Coenzyme Q is an obligatory cofactor for uncoupling protein function
Echtay, K. S., Winkler, E., & Klingenberg, M. (2000) · Nature · doi:10.1038/35046114 · Cited by 334
Uncoupling proteins 2 and 3 are highly active H + transporters and highly nucleotide sensitive when activated by coenzyme Q (ubiquinone)
Echtay, K. S., Winkler, E., Frischmuth, K., & Klingenberg, M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1416 · Cited by 313
Role of UCP homologues in skeletal muscles and brown adipose tissue: mediators of thermogenesis or regulators of lipids as fuel substrate?
Samec, S., Seydoux, J., & Dulloo, A. G. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.9.715 · Cited by 304
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 303
The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron–sulfur cluster N2
Genova, M. L., Ventura, B., Giuliano, G., Bovina, C., Formiggini, G., Castelli, G. P., & Lenaz, G. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02850-2 · Cited by 301
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 289
Localization of the Glycerol‐Phosphate Dehydrogenase in the Outer Phase of the Mitochondrial Inner Membrane
Klingenberg, M. (1970) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1970.tb00924.x · Cited by 287
Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path
Lee, C., Lee, S. M., Mukhopadhyay, P., Kim, S. J., Lee, S. C., Ahn, W.-S., Yu, M., Storz, G., & Ryu, S. E. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb856 · Cited by 281
The ROS production induced by a reverse-electron flux at respiratory-chain complex 1 is hampered by metformin
Batandier, C., Guigas, B., Detaille, D., El-Mir, M., Fontaine, E., Rigoulet, M., & Leverve, X. M. (2006) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-006-9003-8 · Cited by 279
Self-citation
Enhancement of hydrogen peroxide formation by protophores and ionophores in antimycin-supplemented mitochondria
Cadenas, E., & Boveris, A. (1980) · Biochemical Journal · doi:10.1042/bj1880031 · Cited by 275
Superoxide Radical and Hydrogen Peroxide in Mitochondria
Forman, H. J., & Boveris, A. (1982) · Elsevier eBooks · doi:10.1016/b978-0-12-566505-6.50010-7 · Cited by 270
Substrate and Site Specificity of Hydrogen Peroxide Generation in Mouse Mitochondria
Kwong, L. K., & Sohal, R. S. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0489 · Cited by 242
Nox2 and Rac1 Regulate H2O2-Dependent Recruitment of TRAF6 to Endosomal Interleukin-1 Receptor Complexes
Li, Q., Harraz, M. M., Zhou, W., Zhang, L. N., Ding, W., Zhang, Y., Eggleston, T., Yeaman, C. A., Bánfi, B., & Engelhardt, J. F. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.140-154.2006 · Cited by 233
Mitochondrial Reactive Oxygen Species Control the Transcription Factor CHOP-10/GADD153 and Adipocyte Differentiation
Carrière, A., Carmona, M.-C., Fernandez, Y., Rigoulet, M., Wenger, R. H., Pénicaud, L., & Casteilla, L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407258200 · Cited by 230
Self-citation
UCP2 and UCP3 rise in starved rat skeletal muscle but mitochondrial proton conductance is unchanged
Cadenas, S., Buckingham, J. A., Samec, S., Seydoux, J., Din, N., Dulloo, A. G., & Brand, M. D. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01540-9 · Cited by 227
Signaling Components of Redox Active Endosomes: The Redoxosomes
Oakley, F. D., Abbott, D., Li, Q., & Engelhardt, J. F. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2363 · Cited by 217
Mitochondrial Superoxide Decreases Yeast Survival in Stationary Phase
Longo, V. D., Liou, L.-L., Valentine, J. S., & Gralla, E. B. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1158 · Cited by 215
Partial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation
Hinkle, P. C., Butow, R. A., Racker, E., & Chance, B. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99410-x · Cited by 195
Mitochondrial ROS Metabolism: Modulation by Uncoupling Proteins
Casteilla, L., Rigoulet, M., & Pénicaud, L. (2001) · IUBMB Life · doi:10.1080/15216540152845984 · Cited by 173
Self-citation
Fatty acids decrease mitochondrial generation of reactive oxygen species at the reverse electron transport but increase it at the forward transport
Schönfeld, P., & Wojtczak, L. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.04.005 · Cited by 167
The composition of the ketoglutarate dehydrogenase complex
Massey, V. (1960) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(60)91280-4 · Cited by 166
Dating the cyanobacterial ancestor of the chloroplast
Falcón, L. I., Magallón, S., & Castillo, A. (2010) · The ISME Journal · doi:10.1038/ismej.2010.2 · Cited by 159
Localization of the Site of Oxygen Radical Generation inside the Complex I of Heart and Nonsynaptic Brain Mammalian Mitochondria
Herrero, A., & Barja, G. (2000) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005626712319 · Cited by 149
Oxidants Painting the Cysteine Chapel
Xu, D. L., Rovira, I. I., & Finkel, T. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00132-6 · Cited by 148
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
Uncoupling of oxidative phosphorylation in rat liver mitochondria by general anesthetics.
Rottenberg, H. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.11.3313 · Cited by 128
The α‐Ketoglutarate Dehydrogenase Complex
Sheu, K. R., & Blass, J. P. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb07818.x · Cited by 125
Role of thioredoxin reductase in the Yap1p‐dependent response to oxidative stress in Saccharomyces cerevisiae
Carmel‐Harel, O., Stearman, R. S., Gasch, A. P., Botstein, D., Brown, P. O., & Storz, G. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02255.x · Cited by 122
Intrinsic uncoupling of mitochondrial proton pumps. 1. Nonohmic conductance cannot account for the nonlinear dependence of static head respiration on .DELTA.~.mu.H
Zoratti, M., Favaron, M., Pietrobon, D., & AZZONE, G. F. (1986) · Biochemistry · doi:10.1021/bi00352a004 · Cited by 118
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 116
Inhibition of preadipocyte proliferation by mitochondrial reactive oxygen species
Carrière, A., Fernandez, Y., Rigoulet, M., Pénicaud, L., & Casteilla, L. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00862-7 · Cited by 114
Self-citation
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 113
The Interaction of Energy and Electron Transfer Reactions in Mitochondria
Chance, B., & Hollunger, G. (1961) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64213-9 · Cited by 103
Electron transfer flavoprotein-ubiquinone oxidoreductase from pig liver: purification and molecular, redox, and catalytic properties
Beckmann, J. D., & Frerman, F. E. (1985) · Biochemistry · doi:10.1021/bi00336a016 · Cited by 92
Mechanisms of mitochondrial response to variations in energy demand in eukaryotic cells
Devin, A., & Rigoulet, M. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00208.2006 · Cited by 92
Self-citation
Life at Extreme Limits
Mesbah, N. M., & Wiegel, J. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1419.028 · Cited by 88
Shift in the localization of sites of hydrogen peroxide production in brain mitochondria by mitochondrial stress
Gyulkhandanyan, A. V., & Pennefather, P. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02489.x · Cited by 87
High activity of mitochondrial glycerophosphate dehydrogenase and glycerophosphate-dependent ROS production in prostate cancer cell lines
Chowdhury, S. K. R., Gemin, A., & Singh, G. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.06.017 · Cited by 83
Ergosteroids: induction of thermogenic enzymes in liver of rats treated with steroids derived from dehydroepiandrosterone.
Lardy, H. A., Partridge, B., Kneer, N. M., & Wei, Y. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.14.6617 · Cited by 76
Reactive Oxygen Species-mediated Regulation of Mitochondrial Biogenesis in the Yeast Saccharomyces cerevisiae
Chevtzoff, C., Yoboue, E. D., Galinier, A., Casteilla, L., Daignan‐Fornier, B., Rigoulet, M., & Devin, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.019570 · Cited by 72
Self-citation
Reactions of electron-transfer flavoprotein and electron-transfer flavoprotein: ubiquinone oxidoreductase
Ramsay, R. R., Steenkamp, D. J., & Husain, M. (1987) · Biochemical Journal · doi:10.1042/bj2410883 · Cited by 68
Activation of Ras cascade increases the mitochondrial enzyme content of respiratory competent yeast
Dejean, L. M., Beauvoit, B. P., Bunoust, O., Guérin, B., & Rigoulet, M. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00391-1 · Cited by 65
Self-citation
The Mitochondrial Complex I: Progress in Understanding of Catalytic Properties
Vinogradov, A. D., & Grivennikova, V. G. (2001) · IUBMB Life · doi:10.1080/15216540152845920 · Cited by 65
The yeast cAMP protein kinase Tpk3p is involved in the regulation of mitochondrial enzymatic content during growth
Chevtzoff, C., Vallortigara, J., Avéret, N., Rigoulet, M., & Devin, A. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.10.001 · Cited by 64
Self-citation
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Rigoulet M, , Mourier A, , Galinier A, , Casteilla L, , Devin A. Electron competition process in respiratory chain: regulatory mechanisms and physiological functions. Biochim Biophys Acta, 1797; 671–677. 2010.

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“Within the mitochondria, the enzymes of the TCA cycle supply reducing equivalents (NADH and FADH2) for ETC-mediated oxidative phosphorylation and production of ATP.”
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Authors: Rigoulet, M., Yoboue, E. D., & Devin, A.
Affiliations: Centre National de la Recherche Scientifique (FR)
ORCID: Yoboue, Edgar D.
Devin, Anne
Venue: Antioxidants & Redox Signaling
Publisher: SAGE Publications
Published: 2011-02
Volume: 14
Issue: 3
Pages: 459-468
ISSN: 1523-0864 (ISSN-L)
1557-7716
DOI: 10.1089/ars.2010.3363
OpenAlex: W1985730402
Semantic Scholar: 72f038ebb891d7e56acea1d3220662223a95864f
Cited by: 394
References: 112
Citations by year: 2026: 6 · 2025: 8 · 2024: 13 · 2023: 24 · 2022: 25 · 2021: 41 · 2020: 23 · 2019: 24 · 2018: 26 · 2017: 25 · 2016: 19 · 2015: 31 · 2014: 25 · 2013: 37 · 2012: 44
FWCI: 2.91
Type: journal article
Language: en
Open access: closed
Licence: journals.sagepub.com/page/policies/text-and-data-mining-license (tdm)
Locations: Antioxidants and Redox Signaling (publishedVersion)
PubMed (publishedVersion)
Funders: Agence Nationale de la Recherche
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer and biochemical research
Keywords: mitochondrial reactive oxygen species, hydrogen peroxide signaling, oxidative stress, electron transport chain, bc1 complex, complex I, dehydrogenase, peroxiredoxin, cell proliferation, cell differentiation
MeSH terms: Animals, Electron Transport, Hydrogen Peroxide, Mitochondria, Models, Molecular, Oxygen, Protein Conformation, Signal Transduction, Oxidants, Reactive Oxygen Species, Oxidative Stress, Cell Proliferation

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Mitochondrial ROS Generation and Its Regulation: Mechanisms Involved in H 2 O 2 Signaling

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