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The Role of Mitochondria in Reactive Oxygen Species Metabolism and Signaling
Open accessAbstract
Oxidative stress is considered a major contributor to the etiology of both “normal” senescence and severe pathologies with serious public health implications. Several cellular sources, including mitochondria, are known to produce significant amounts of reactive oxygen species (ROS) that may contribute to intracellular oxidative stress. Mitochondria possess at least 10 known sites that are capable of generating ROS, but they also feature a sophisticated multilayered ROS defense system that is much less studied. This review summarizes the current knowledge about major components involved in mitochondrial ROS metabolism and factors that regulate ROS generation and removal at the level of mitochondria. An integrative systemic approach is applied to analysis of mitochondrial ROS metabolism, which is “dissected” into ROS generation, ROS emission, and ROS scavenging. The in vitro ROS‐producing capacity of several mitochondrial sites is compared in the metabolic context and the role of mitochondria in ROS‐dependent intracellular signaling is discussed.
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“The succinate concentration in different tissues and mitochondria is in the submillimolar range under aerobic conditions [22,72,73], indicating that complex II is not working at maximal velocity under 'standard conditions'.”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [22]
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“The highly effective mitochondrial antioxidative defense system encompasses the thioredoxin/peroxiredoxin system as well as the glutathione/glutathione peroxidase system (overview in [22,117]).”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [22]
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Citations
Cites
Free radicals and antioxidants in normal physiological functions and human disease
Valko, M., Leibfritz, D., Moncol, J., Cronin, M. T. D., Mazur, M., & Telser, J. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.07.001 · Cited by 14,269
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827
Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084
Boveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626
Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
Turrens, J. F., & Boveris, A. (1980) · Biochemical Journal · doi:10.1042/bj1910421 · Cited by 1,601
Role of reactive oxygen species in the pathophysiology of human reproduction.
Agarwal, A., Saleh, R., & Bedaiwy, M. (2003) · Fertility and Sterility · doi:10.1016/s0015-0282(02)04948-8 · Cited by 1,578
Oxygen, oxidative stress, hypoxia, and heart failure
Giordano, F. J. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24408 · Cited by 1,515
Research works printed but not linked: 2
- 10.1172/JCI200524408 · DOI
- 10.1111/j.1469-7793.2003.00335.x · DOI · Paper page
Cited by
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Items 801–847 of 847
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Chandran, A., Kumar, T. S., Halikar, A. M., & Kumar, T. R. S. (2024) · Springer eBooks · doi:10.1007/978-981-99-6263-1_40
Devaux, J. B. L., McArley, T. J., Herbert, N. A., & H, A. J. R. (2024) · Research Square · doi:10.21203/rs.3.rs-4722244/v1
Tan, A. D. Y., Li, R., & Li, J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.13.632863
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Güç, İ. (2025) · Osmaniye Korkut Ata Üniversitesi Fen Bilimleri Enstitüsü Dergisi · doi:10.47495/okufbed.1550868
Schantz, S. L., LePage, T. H., Dubrof, S., Sneed, S. E., Cheek, S. R., Park, H., Barany, D. A., Kinder, H. A., Duberstein, K., DeWahl, D. A., et al. (2025) · Journal of Neurotrauma · doi:10.1177/08977151251363584
Gao, Z., Liu, L., Xu, Y., Zhao, C., Zhao, X., Zhao, T., Che, Y., & Zhao, W. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110694
Targeting reactive oxygen species signaling pathways for cancer metabolic reprogramming
Kar, S. S., Mishra, H., Barik, C. S., Kar, B., Ghosh, G., & Rath, G. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-33459-7.00014-4
Tetteh, P. A., Kalvani, Z., Stevens, D., Sappal, R., & Kamunde, C. (2025) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2025.110417
Das, K., Pramanik, S., Biswas, G., Rajak, P., Nanda, S., Ganguly, A., & Mandi, M. (2025) · Journal of Applied Toxicology · doi:10.1002/jat.4986 · Cited by 1
He, W., Liu, X., Feng, Y., Ding, H., Sun, H., Li, Z., & Baoming, S. (2024) · Figshare · doi:10.6084/m9.figshare.25560887
King, D. E., Sparling, A. C., Joyce, A. S., Ryde, I. T., deSouza, B., Ferguson, P. L., Murphy, S. K., & Meyer, J. N. (2024) · Figshare · doi:10.6084/m9.figshare.25698146
Krupenko, N. I., Sharma, J., Pediaditakis, P., Helke, K. L., Hall, M. S., Du, X., Sumner, S., & Krupenko, S. A. (2020) · Figshare · doi:10.6084/m9.figshare.13212581
Krupenko, N. I., Sharma, J., Pediaditakis, P., Helke, K. L., Hall, M. S., Du, X., Sumner, S., & Krupenko, S. A. (2020) · Figshare · doi:10.6084/m9.figshare.13212557
Raafat, M. A., Al-Hasnaawei, S., Mousa, H. M., Malathi, H., Sahu, S., Prathiba, S., Singh, G., & Sinha, A. (2026) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.70673
Devaux, J. B. L., McArley, T. J., Herbert, N. A., & Hickey, A. J. (2026) · Scientific Reports · doi:10.1038/s41598-025-30078-2
ROS and Inflammation in Mitochondrial Disorders
Bishal, A., Bandyopadhyay, B., Mondal, M., & Dewan, D. (2026) · Springer eBooks · doi:10.1007/978-3-032-11752-6_15
Roy, D., Bose, S., Das, A., Manna, R., Roy, D., Verma, S. S., Bhattacharjee, J., Das, S., Tudu, S., Steiner, R. E., et al. (2026) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.5c00493
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Benyamina, S. M. (2012) · theses.fr (ABES) · doi:10.70675/aafc7ab4z1251z44d8zbdaez0661f78121c0
Coevolution of sociality and ageing in animal societies
Quque, M. (2020) · theses.fr (ABES) · doi:10.70675/6bc5d1cdz71abz4041z846bzdf36af17baa8
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Fouché, G. (2021) · theses.fr (ABES) · doi:10.70675/b2bddc22z76f0z4d08z950cz2b03da999efa
Benssouina, F.-Z. (2022) · theses.fr (ABES) · doi:10.70675/276c5067zc483z4f95zb64bz7585a1ebc1e6
Same mitochondria, different longevities : what do ants tell us about metabolic ageing ?
Kervella, M. (2023) · theses.fr (ABES) · doi:10.70675/7b57ef70z057dz4435za749zb0c6dcd534e4
Nunes, Á. M., & Falagan-Lotsch, P. (2026) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6c00848
Tian, X., Kong, Y., Ma, S., Xu, C., Zhang, R., Deng, H., & Lan, H. (2026) · Toxicology · doi:10.1016/j.tox.2026.154479
Enumerating the Role of Oxidative Stress in Cancer Progression
Tandon, R., Karankar, V. S., & Srivastava, N. (2026) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-3-032-19837-2_6
Clioquinol inactivates thiamine pyrophosphate by increasing cellular oxidative stress
Fan, Z., Yan, X., Zheng, Q., Zhu, Z., Song, B., Feng, X., Pan, S., Lv, C., & Shi, P. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104258
Macrophage-mediated antibiotic evasion and competitive dominance of mcr-3-carrying Escherichia coli
Tan, S., Yin, W., Sun, J., Xiong, W., An, Y., Qiao, L., Zhang, P., Sun, S., Li, Q., Fu, L., et al. (2026) · PLoS Pathogens · doi:10.1371/journal.ppat.1014427
Cell-specific effects of methoxy-substituted iron(III) salophene complexes
Bernkop-Schnürch, A. D., Hermann, M., Strich, S. L., Raffeiner, A., Hanifle, S., Torres‐Quesada, O., Hofmann, J., Martowicz, A., Seidl, M., Gust, R., et al. (2026) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2026.110257
Nanomaterials in Healthcare: Regulatory Aspects and Safety Perspectives
Rajchal, B., Thapa, Y. N., Karki, D., Katiyar, V., & Adhikari, R. (2026) · Springer eBooks · doi:10.1007/978-981-95-9386-6_17
Decoding Molecular Mechanisms of Pongamia pinnata Phytochemicals in Cancer Therapy
Dhar, R., & Subramaniyan, V. (2026) · Medicine Advances · doi:10.1002/med4.70076
Badawi, K., Mujalli, A., Owaydhah, W., Sharazly, B. M. E., Chen, P., Sun, K.-T., Negm, O. H., Khan, R., & Carter, W. G. (2026) · Brain Sciences · doi:10.3390/brainsci16080889
Pavlova, S. I., Samartsev, V. N., Kuzmina, E. I., Zainutdinova, G. I., & Dubinin, M. V. (2026) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-026-10129-7
Sai‐Ut, S., Indriani, S., Srisakultiew, N., Thumanu, K., Kingwascharapong, P., Phongthai, S., Chaikham, P., Rawdkuen, S., & Pongsetkul, J. (2026) · LWT · doi:10.1016/j.lwt.2026.119968
Ai, M., Liao, Y., Jiang, T., Huo, T., Wu, L., Xiao, L., Liu, J., & Song, K. (2026) · International Dental Journal · doi:10.1016/j.identj.2026.111244
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Xie, Q., Walker, H. E., Minczuk, M. A., Chiaratti, M. R., & Chinnery, P. F. (2026) · Nature Reviews Genetics · doi:10.1038/s41576-026-01019-0
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Tan, A. D. Y., Li, R., & Li, J. (2026) · Research Square · doi:10.21203/rs.3.rs-11188068/v1
Phosphate and induction of the mitochondrial permeability transition
Bernardi, P., & Carraro, M. (2026) · Mitochondrial Communications · doi:10.1016/j.mitoco.2026.10.001
Aliberti, A., Coppola, N., Gasparro, R., Trosino, O., Sammartino, J. C., & Sammartino, G. (2026) · Frontiers in Oral Health · doi:10.3389/froh.2026.1976898
Reilly, B. (2015) · The University of Queensland · doi:10.14264/uql.2015.587
Metadata
- Authors
- Starkov, A. A.
- Affiliations
- Cornell University (US)
- Corresponding author
- Starkov, Anatoly A.
- ORCID
- Starkov, Anatoly A.
- Venue
- Annals of the New York Academy of Sciences
- Publisher
- Wiley
- Published
- 2008-12
- Volume
- 1147
- Issue
- 1
- Pages
- 37-52
- ISSN
- 0077-8923 (ISSN-L)
- 1749-6632
- PMC
- PMC2869479
- OpenAlex
- W2053022803
- Cited by
- 846
- References
- 86
- Citations by year
- 2026: 39 · 2025: 39 · 2024: 42 · 2023: 66 · 2022: 67 · 2021: 78 · 2020: 74 · 2019: 55 · 2018: 42 · 2017: 46 · 2016: 50 · 2015: 39 · 2014: 38 · 2013: 41 · 2012: 39
- FWCI
- 2.32
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Annals of the New York Academy of Sciences (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (AG014930, P01AG014930)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- mitochondria, reactive oxygen species, oxidative stress, ROS signaling, reactive oxygen species scavenging, aging, cellular senescence
- MeSH terms
- Humans, Mitochondria, Signal Transduction, Reactive Oxygen Species, Oxidative Stress
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