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

Rigoulet, Michel; Yoboue, Edgar D.; Devin, Anne

doi:10.1089/ars.2010.3363

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

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 produce reactive oxygen species as a consequence of electron leak during respiration.
“It is well established that mitochondria produce ROS as a consequence of electron leak during respiration (223, 349).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [349]
There is a threshold range of ROS concentrations beyond which ROS become harmful, although some increases in ROS can stimulate essential pathways.
“Although some increases in ROS can stimulate these essential pathways, there is a threshold range of concentrations beyond which ROS become harmful (83, 206, 349).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [349]

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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 · see citing works
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 · see citing works
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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 69 · see citing works
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 · see citing works
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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 · see citing works
The yeast cAMP protein kinase Tpk3p is involved in the regulation of mitochondrial enzymatic content during growth
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pH-dependent Substrate Preference of Pig Heart Lipoamide Dehydrogenase Varies with Oligomeric State
Klyachko, N. L., Shchedrina, V. A., Efimov, A. V., Kazakov, S. V., Gazaryan, I. G., Kristal, B. S., & Brown, A. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414285200 · Cited by 60 · see citing works
Inhibition of the alpha‐ketoglutarate dehydrogenase‐mediated reactive oxygen species generation by lipoic acid
Ambrus, A., Tretter, L., & Ádám‐Vizi, V. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05942.x · Cited by 58 · see citing works
Reaction of electron-transfer flavoprotein with electron transfer flavoprotein-ubiquinone oxidoreductase
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Competition of Electrons to Enter the Respiratory Chain
Bunoust, O., Devin, A., Avéret, N., Camougrand, N. M., & Rigoulet, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407746200 · Cited by 55 · see citing works
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Kinetic Regulation of the Mitochondrial Glycerol-3-phosphate Dehydrogenase by the External NADH Dehydrogenase in Saccharomyces cerevisiae
Påhlman, I.-L., Larsson, C., Avéret, N., Bunoust, O., Boubekeur, S., Gustafsson, L., & Rigoulet, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204079200 · Cited by 49 · see citing works
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In vivo oxidation‐reduction kinetics of OxyR, the transcriptional activator for an oxidative stress‐inducible regulon in Escherichia coli
Tao, K. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01013-3 · Cited by 49 · see citing works
Pathways of hydrogen peroxide generation in guinea pig cerebral cortex mitochondria
Zoccarato, F., Cavallini, L., Deana, R., & Alexandre, A. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(88)90200-8 · Cited by 43 · see citing works
Quantitative analysis of some mechanisms affecting the yield of oxidative phosphorylation: dependence upon both fluxes and forces.
Rigoulet, M., Leverve, X. M., Fontaine, E. M., Ouhabi, R., & Guérin, B. (1998) · PubMed · Cited by 38 · see citing works
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Respiration in non-phosphorylating yeast mitochondria. Roles of non-ohmic proton conductance and intrinsic uncoupling
Ouhabi, R., Rigoulet, M., Lavie, J.-L., & Guérin, B. (1991) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(05)80319-6 · Cited by 38 · see citing works
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cAMP-induced modulation of the growth yield of Saccharomyces cerevisiae during respiratory and respiro-fermentative metabolism
Dejean, L. M., Beauvoit, B. P., Alonso, A. P., Bunoust, O., Guérin, B., & Rigoulet, M. (2002) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(02)00240-2 · Cited by 36 · see citing works
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Quantitative analysis of some mechanisms affecting the yield of oxidative phosphorylation: Dependence upon both fluxes and forces
Rigoulet, M., Leverve, X. M., Fontaine, E. M., Ouhabi, R., & Guérin, B. (1998) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006858104988 · Cited by 34 · see citing works
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Active proton leak in mitochondria: A new way to regulate substrate oxidation
Mourier, A., Devin, A., & Rigoulet, M. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.10.011 · Cited by 32 · see citing works
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Growth Yield Homeostasis in Respiring Yeast Is Due to a Strict Mitochondrial Content Adjustment
Devin, A., Dejean, L. M., Beauvoit, B. P., Chevtzoff, C., Avéret, N., Bunoust, O., & Rigoulet, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604800200 · Cited by 31 · see citing works
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α-Ketoglutarate dehydrogenase complex may be heterogeneous in quaternary structure
Wagenknecht, T., Francis, N. R., & DeRosier, D. J. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80217-4 · Cited by 27 · see citing works
NADH-Ubiquinone oxidoreductase: substrate-dependent oxygen turnover to superoxide anion as a function of flavin mononucleotide
Johnson, J. E., Choksi, K. B., & Widger, W. R. (2003) · Mitochondrion · doi:10.1016/s1567-7249(03)00084-9 · Cited by 21 · see citing works
Activation of mitochondrial glycerophosphate cytochrome c reductase in regenerating rat liver by triiodothyronine
Lotková, H., Rauchová, H., & Drahota, Z. (2001) · Physiological Research · doi:10.33549/physiolres.930064 · Cited by 4 · see citing works

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Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling
Brand, M. D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.001 · Cited by 1,063 · see citing works
Oxidative stress mitigation by antioxidants - An overview on their chemistry and influences on health status
Pisoschi, A. M., Pop, A., Iordache, F., Stanca, L., Predoi, G., & Șerban, A. I. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112891 · Cited by 849 · see citing works
Role of peroxisomes in ros/rns-metabolism: Implications for human disease
Fransen, M., Nordgren, M., Wang, B., & Apanasets, O. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.001 · Cited by 644 · see citing works
Nanocatalytic Tumor Therapy by Biomimetic Dual Inorganic Nanozyme‐Catalyzed Cascade Reaction
Gao, S., Lin, H., Zhang, H., Yao, H., Chen, Y., & Shi, J. (2018) · Advanced Science · doi:10.1002/advs.201801733 · Cited by 645 · see citing works
Redox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works
“Within the mitochondria, the enzymes of the TCA cycle supply reducing equivalents (NADH and FADH2) for ETC-mediated oxidative phosphorylation and production of ATP.”
BackgroundInfluential
Mitochondria as playmakers of apoptosis, autophagy and senescence
Abate, M., Festa, A., Falco, M., Lombardi, A., Luce, A., Grimaldi, A., Zappavigna, S., Sperlongano, P., Irace, C., Caraglia, M., et al. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.022 · Cited by 543 · see citing works
MitoNEET-driven alterations in adipocyte mitochondrial activity reveal a crucial adaptive process that preserves insulin sensitivity in obesity
Kusminski, C. M., Holland, W. L., Sun, K., Park, J., Spurgin, S. B., Lin, Y., Askew, G. R., Simcox, J., McClain, D. A., Li, C., et al. (2012) · Nature Medicine · doi:10.1038/nm.2899 · Cited by 466 · see citing works
Synthetic Oleanane Triterpenoids: Multifunctional Drugs with a Broad Range of Applications for Prevention and Treatment of Chronic Disease
Liby, K. T., & Sporn, M. B. (2012) · Pharmacological Reviews · doi:10.1124/pr.111.004846 · Cited by 410 · see citing works
“Furthermore, the production of mitochondrial reactive oxygen species (Rigoulet et al., 2011) in parenchymal cells in turn drives the production and activation of proinflammatory cytokines, further enhancing this vicious circle.”
Background
Reactive Oxygen Species: A Key Hallmark of Cardiovascular Disease
Panth, N., Paudel, K. R., & Parajuli, K. (2016) · Advances in Medicine · doi:10.1155/2016/9152732 · Cited by 405 · see citing works
“triphosphate sensitive potassium channel in mitochondria [45].”
Dysregulation of Glutathione Homeostasis in Neurodegenerative Diseases
Johnson, W. M., Wilson‐Delfosse, A. L., & Mieyal, J. J. (2012) · Nutrients · doi:10.3390/nu4101399 · Cited by 354 · see citing works
Regulation of Pichia pastoris promoters and its consequences for protein production
Vogl, T. J., & Glieder, A. (2012) · New Biotechnology · doi:10.1016/j.nbt.2012.11.010 · Cited by 333 · see citing works
Oxidative stress, inflamm-aging and immunosenescence
Cannizzo, E. S., Clement, C. C., Sahu, R. K., Follo, C., & Santambrogio, L. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.06.005 · Cited by 303 · see citing works
“[9] Rigoulet M, Yoboue ED, Devin A.”
BackgroundInfluential
Melatonin Alleviates Intracerebral Hemorrhage-Induced Secondary Brain Injury in Rats via Suppressing Apoptosis, Inflammation, Oxidative Stress, DNA Damage, and Mitochondria Injury
Wang, Z., Zhou, F., Dou, Y., Tian, X., Liu, C., Li, H., Shen, H., & Chen, G. (2017) · Translational Stroke Research · doi:10.1007/s12975-017-0559-x · Cited by 292 · see citing works
Regulation of protein tyrosine phosphatases by reversible oxidation
Östman, A., Frijhoff, J., Sandin, Å., & Böhmer, F. (2011) · The Journal of Biochemistry · doi:10.1093/jb/mvr104 · Cited by 288 · see citing works
“Mitochondrial respiration is an important source of ROS production (50).”
Background
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
Mitochondria and Reactive Oxygen Species: Physiology and Pathophysiology
Bolisetty, S., & Jaimes, E. A. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14036306 · Cited by 274 · see citing works
Protein sulfenic acid formation: From cellular damage to redox regulation
Roos, G., & Messens, J. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.031 · Cited by 274 · see citing works
Cell Signaling through Protein Kinase C Oxidation and Activation
Cosentino-Gomes, D., Rocco-Machado, N., & Meyer-Fernandes, J. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms130910697 · Cited by 256 · see citing works
“For a complete review, see Rigoulet et al. 2011 [45].”
Background
T cells and reactive oxygen species
Belikov, A. V., Schraven, B., & Simeoni, L. (2015) · Journal of Biomedical Science · doi:10.1186/s12929-015-0194-3 · Cited by 264 · see citing works
The role of mitochondrial DNA mutations and free radicals in disease and ageing
Lagouge, M., & Larsson, N. (2013) · Journal of Internal Medicine · doi:10.1111/joim.12055 · Cited by 270 · see citing works
Mitochondrial Dysfunction in Parkinson’s Disease—Cause or Consequence?
Chen, C., Turnbull, D. M., & Reeve, A. K. (2019) · Biology · doi:10.3390/biology8020038 · Cited by 253 · see citing works
“The increase in numbers of electrons being transferred would increase the probability of electron capture by O2 to generate superoxide before they reach COX [36].”
Background
Mitochondrial Redox Signaling: Interaction of Mitochondrial Reactive Oxygen Species with Other Sources of Oxidative Stress
Schulz, E., Wenzel, P., Münzel, T. F., & Daiber, A. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4609 · Cited by 253 · see citing works
“…in redox signaling events, such as the regulation of redox-sensitive transcription factors ( e.g., OxyR or Yap1 by H 2 O 2 via disulﬁde bridge formation) or processes mediated by redox-sensitive protein tyrosine phosphatases/kinases as well as the glutaredoxin and peroxiredoxin systems (106).”
Mitochondrial Energy Metabolism and Redox Signaling in Brain Aging and Neurodegeneration
Yin, F., Boveris, A., & Cadenas, E. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4774 · Cited by 246 · see citing works
“Mitochondrial H2O2 is implicated in the regulation of the cellular redox status, thus transducing redox signals into a wide variety of responses, such as proliferation, adaptation, differentiation, and cellular death pathways (199).”
Background
Redox Roles of Reactive Oxygen Species in Cardiovascular Diseases
He, F. J., & Zuo, L. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161126059 · Cited by 240 · see citing works
“For example, about 1%–3% of oxygen is converted to O2‚´ via oxidative phosphorylation in mitochondrial complexes I and III [23,24].”
Calcium, Bioenergetics, and Neuronal Vulnerability in Parkinson's Disease
Surmeier, D. J., & Schumacker, P. T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.410530 · Cited by 233 · 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
Oxidative Stress, Inflammaging, and Immunosenescence
Bauer, M. E., & la Fuente, M. D. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-397803-5.00004-6 · Cited by 229 · see citing works
ROS-Scavenging Therapeutic Hydrogels for Modulation of the Inflammatory Response
Kim, Y. E., & Kim, J. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c18261 · Cited by 229 · see citing works
Mitochondrial Biogenesis and Mitochondrial Reactive Oxygen Species (ROS): A Complex Relationship Regulated by the cAMP/PKA Signaling Pathway
Bouchez, C. L., & Devin, A. (2019) · Cells · doi:10.3390/cells8040287 · Cited by 226 · see citing works
Self-citation
Mitochondria and Brain Disease: A Comprehensive Review of Pathological Mechanisms and Therapeutic Opportunities
Clemente‐Suárez, V. J., Redondo-Flórez, L., Beltrán-Velasco, A. I., Ramos‐Campo, D. J., Belinchón-deMiguel, P., Martínez‐Guardado, I., Dalamitros, A. A., Sepulveda, R. A. Y., Martín-Rodríguez, A., & Tornero-Aguilera, J. F. (2023) · Biomedicines · doi:10.3390/biomedicines11092488 · Cited by 241 · see citing works
Ablation of Ceramide Synthase 2 Causes Chronic Oxidative Stress Due to Disruption of the Mitochondrial Respiratory Chain
Zigdon, H., Kogot‐Levin, A., Park, J., Goldschmidt, R., Kelly, S. L., Merrill, A. H., Scherz, A. J., Pewzner‐Jung, Y., Saada, A., & Futerman, A. H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.402719 · Cited by 207 · see citing works
Elamipretide (SS-31) improves mitochondrial dysfunction, synaptic and memory impairment induced by lipopolysaccharide in mice
Zhao, W., Xu, Z., Cao, J., Fu, Q., Wu, Y., Zhang, X., Yue, L., Zhang, X., Yang, Y., Li, Y., et al. (2019) · Journal of Neuroinflammation · doi:10.1186/s12974-019-1627-9 · Cited by 207 · see citing works
Ubiad1 Is an Antioxidant Enzyme that Regulates eNOS Activity by CoQ10 Synthesis
Mugoni, V., Postel, R., Catanzaro, V., Luca, E. D., Turco, E., Digilio, G., Silengo, L., Murphy, M. P., Medana, C., Stainier, D. Y. R., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.013 · Cited by 205 · see citing works
“If the ETC is disturbed, such as in the absence of UBIAD1/CoQ10, the ferrous-dioxygen complex dissociates, and O 2 is generated from the FMN oxygenase domain (Liu et al., 2002; Rigoulet et al., 2011).”
Nutritional Ketosis and Mitohormesis: Potential Implications for Mitochondrial Function and Human Health
Miller, V. J., Villamena, F. A., & Volek, J. S. (2018) · Journal of Nutrition and Metabolism · doi:10.1155/2018/5157645 · Cited by 200 · see citing works
Protective Effect of Glutathione against Oxidative Stress-induced Cytotoxicity in RAW 264.7 Macrophages through Activating the Nuclear Factor Erythroid 2-Related Factor-2/Heme Oxygenase-1 Pathway
Kwon, D. H., Cha, H., Lee, H., Hong, S. H., Park, C., Park, S., Kim, G., Kim, S., Kim, H., Hwang, H., et al. (2019) · Antioxidants · doi:10.3390/antiox8040082 · Cited by 197 · see citing works
“Moreover, the accumulation of ROS beyond the antioxidant function of cells could reduce the mitochondrial membrane potential (MMP), an index of the electron transport chain performance, resulting in a compromised adenosine triphosphate (ATP) production [4,7].”
Epigenetics and Oxidative Stress in Aging
Guillaumet-Adkins, A., Yáñez, Y., Peris‐Díaz, M. D., Calabria, I., Palanca-Ballester, C., & Sandoval, J. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/9175806 · Cited by 194 · see citing works
“The mitochondria are the main intracellular source of ROS generation, as a consequence of electron transfer during ATP production [22, 23].”
Background
Targeting Mitochondrial Biogenesis with Polyphenol Compounds
Chodari, L., Aytemir, M. D., Vahedi, P., Alipour, M., Vahed, S. Z., Khatibi, S. M. H., Ahmadian, E., Ardalan, M., & Eftekhari, A. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/4946711 · Cited by 194 · see citing works
“Additionally, inside the cells, mitochondria serve as the ROS’s prime source [19].”
Background
Principles in Redox Signaling: From Chemistry to Functional Significance
Bindoli, A., & Rigobello, M. P. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4655 · Cited by 189 · see citing works
“signaling molecules able to communicate to cells or to the subcellular micro-environment any alterations in redox conditions in order to transmit specific messages (54, 88, 103, 108, 111, 286, 287, 298, 314, 332, 372).”
Is Mitochondrial Dysfunction a Common Root of Noncommunicable Chronic Diseases?
Díaz‐Vegas, A., Sánchez-Aguilera, P., Krycer, J. R., Morales, P. E., Monsalves‐Álvarez, M., Cifuentes, M., Rothermel, B. A., & Lavandero, S. (2020) · Endocrine Reviews · doi:10.1210/endrev/bnaa005 · Cited by 174 · see citing works
Natural Compounds Modulating Mitochondrial Functions
Gibellini, L., Bianchini, E., Biasi, S. D., Nasi, M., Cossarizza, A., & Pinti, M. (2015) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2015/527209 · Cited by 158 · see citing works
“Furthermore, mitochondria are the main intracellular source of reactive oxygen species (ROS) [5].”
Background
Mitochondrial Dysfunction and Ovarian Aging
Kasapoğlu, I., & Seli, E. U. (2020) · Endocrinology · doi:10.1210/endocr/bqaa001 · Cited by 156 · see citing works
The two faces of reactive oxygen species (ROS) in adipocyte function and dysfunction
Castro, J. P., Grune, T., & Speckmann, B. (2016) · Biological Chemistry · doi:10.1515/hsz-2015-0305 · Cited by 152 · see citing works
Reactive oxygen species and ovarian diseases: Antioxidant strategies
Liang, J., Gao, Y., Feng, Z., Zhang, B., Na, Z., & Li, D. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102659 · Cited by 149 · see citing works
“Mitochondria are the most abundant organelles in oocytes [11], and the respiratory electron transfer systems for aerobic metabolism are the primary sources of ROS production [12] (Fig.”
Background
MXenes-based nanomaterials for biosensing and biomedicine
Yang, G., Liu, F., Zhao, J., Fu, L., Gu, Y., Qu, L., Zhu, C., Zhu, J., & Lin, Y. (2023) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2022.215002 · Cited by 144 · see citing works
Remnant nephron physiology and the progression of chronic kidney disease
Schnaper, H. W. (2013) · Pediatric Nephrology · doi:10.1007/s00467-013-2494-8 · Cited by 138 · see citing works
“Among these, non-hypoxic forms of stress are prominent [52] and may be self-propagating [53].”
H 2 O 2
Rice, M. E. (2011) · The Neuroscientist · doi:10.1177/1073858411404531 · Cited by 133 · see citing works
Oxidative Stress in Cardiovascular Diseases and Obesity: Role of p66Shc and Protein Kinase C
Marchi, E. D., Baldassari, F., Bononi, A., Wieckowski, M. R., & Pinton, P. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/564961 · Cited by 132 · see citing works
“While O2 ∙− mediates its effects within a short range of its production, H 2 O 2 is more stable and can diffuse throughout the cell; hence, despite the compartmentalization of ROS production, electrons generated by excess mitochondrial metabolism can be used to regulate intracellular signalling through the production…”
Background
Iron uptake controls the generation of Leishmania infective forms through regulation of ROS levels
Mittra, B., Cortéz, M., Haydock, A. K., Ramasamy, G., Myler, P. J., & Andrews, N. W. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20121368 · Cited by 130 · 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
“However, there is a threshold above which ROS become harmful and induce oxidative stress (331).”
Riding the tiger – physiological and pathological effects of superoxide and hydrogen peroxide generated in the mitochondrial matrix
Brand, M. D. (2020) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1828258 · Cited by 123 · see citing works
Tissue‐ and Condition‐Specific Isoforms of Mammalian Cytochrome c Oxidase Subunits: From Function to Human Disease
Sinkler, C. A., Kalpage, H. A., Shay, J., Lee, I., Malek, M. H., Grossman, L. I., & Hüttemann, M. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/1534056 · Cited by 124 · see citing works
Generation of reactive oxygen species in 1-methyl-4-phenylpyridinium (MPP+) treated dopaminergic neurons occurs as an NADPH oxidase-dependent two-wave cascade
Zawada, W. M., Banninger, G. P., Thornton, J., Marriott, B., Cantu, D., Rachubinski, A. L., Das, M., Griffin, W. S. T., & Jones, S. M. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-129 · Cited by 122 · see citing works
“Reactive oxygen species (ROS) contribute to cellular signaling, affecting most aspects of cellular function including gene expression, proliferation, differentiation, and migration [1,2].”
Background
Mitochondrial dysfunction in cancer
Księżakowska‐Łakoma, K., Żyła, M. M., & Wilczyński, J. R. (2014) · Menopause Review/Przegląd Menopauzalny · doi:10.5114/pm.2014.42717 · Cited by 120 · see citing works
“For instance, one of the RS, hydrogen peroxide (H 2O2), acts as an important intracellular messenger, and regulates apoptosis and senescence [29, 30].”
Antioxidant and Hepatoprotective Effects of the Red Ginseng Essential Oil in H2O2-Treated HepG2 Cells and CCl4-Treated Mice
Bak, M.-J., Jun, M., & Jeong, W. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13022314 · Cited by 119 · see citing works
“Hydrogen peroxide (H2O2) is produced endogenously from microsomes and peroxisomes and also by several physiological processes such as inflammatory respiratory burst and oxidative phosphorylation [6,25].”
Background
Physiological Phenotype and Vulnerability in Parkinson's DiseasePreprint
Surmeier, D. J., Guzmán, J. N., Sánchez, J. A., & Schumacker, P. T. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009290 · Cited by 115 · see citing works
“In that regard, the stimulation of mitochondrial activity by high ADP production in the cell would increase the transfer of electrons down the chain, potentially increasing the likelihood that some electrons will be captured by O2 before they reach cytochrome oxidase (Lee et al. 2001; Rigoulet et al. 2011).”
Background
PGC-1α protects RPE cells of the aging retina against oxidative stress-induced degeneration through the regulation of senescence and mitochondrial quality control. The significance for AMD pathogenesis
Kaarniranta, K., Kajdanek, J., Morawiec, J., Pawlowska, E., & Blasiak, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082317 · Cited by 112 · see citing works
Antioxidant and neuroprotective effects of Dictyophora indusiata polysaccharide in Caenorhabditis elegans
Zhang, J., Shi, R., Li, H., Xiang, Y., Xiao, L., Hu, M., Ma, F., Ma, C. W., & Huang, Z. (2016) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2016.09.031 · Cited by 110 · see citing works
“Mitochondria are the main source of ROS generation which is caused by electron leakage from the oxidative phosphorylation pathway (Rigoulet et al., 2011).”
Background
Manganese Superoxide Dismutase Regulates a Redox Cycle Within the Cell Cycle
Sarsour, E. H., Kalen, A. L., & Goswami, P. C. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5303 · Cited by 109 · see citing works
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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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