Succinate modulation of H2O2 release at NADH:ubiquinone oxidoreductase (complex I) in brain mitochondria
Open accessAbstract
Complex I (NADH:ubiquinone oxidoreductase) is responsible for most of the mitochondrial H2O2 release, both during the oxidation of NAD-linked substrates and during succinate oxidation. The much faster succinate-dependent H2O2 production is ascribed to Complex I, being rotenone-sensitive. In the present paper, we report high-affinity succinate-supported H2O2 generation in the absence as well as in the presence of GM (glutamate/malate) (1 or 2 mM of each). In brain mitochondria, their only effect was to increase from 0.35 to 0.5 or to 0.65 mM the succinate concentration evoking the semi-maximal H2O2 release. GM are still oxidized in the presence of succinate, as indicated by the oxygen-consumption rates, which are intermediate between those of GM and of succinate alone when all substrates are present together. This effect is removed by rotenone, showing that it is not due to inhibition of succinate influx. Moreover, α-oxoglutarate production from GM, a measure of the activity of Complex I, is decreased, but not stopped, by succinate. It is concluded that succinate-induced H2O2 production occurs under conditions of regular downward electron flow in Complex I. Succinate concentration appears to modulate the rate of H2O2 release, probably by controlling the hydroquinone/quinone ratio.
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Under simultaneous NADH-generating substrate and succinate supply, electrons can flow downstream through complex I, which should attenuate RET.
“Zoccarato and colleagues have shown that under these conditions electrons can flow downstream through complex I, which should attenuate RET [21].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [21]
A high rate of ROS production is observed when NADH-generating substrates and succinate are supplied together to isolated mitochondria.
“A high rate of ROS production is also observed when NADH-generating substrates and succinate are concomitantly supplied to isolated mitochondria [21,23,34,35].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [21]
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Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178 · see citing works
Mitochondrial free radical generation, oxidative stress, and aging
Cadenas, E., & Davies, K. J. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00317-8 · Cited by 3,010 · see citing works
Korshunov, S. S., Skulachev, V. P., & Starkov, A. A. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01159-9 · Cited by 1,727 · see citing works
Extension of murine life span by overexpression of catalase targeted to mitochondria
Schriner, S. E., Linford, N. J., Martin, G. M., Treuting, P., Ogburn, C. E., Emond, M., Coskun, P. E., Ladiges, W., Wolf, N., Van Remmen, H., et al. (2005) · Science · doi:10.1126/science.1106653 · Cited by 1,724 · see citing works
Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
Turrens, J. F., & Boveris, A. (1980) · Biochemical Journal · doi:10.1042/bj1910421 · Cited by 1,601 · see citing works
Topology of superoxide production from different sites in the mitochondrial electron transport chain
St-Pierre, J., Buckingham, J. A., Roebuck, S. J., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207217200 · Cited by 1,545 · see citing works
Oxidative stress and gene regulation
Allen, R. G., & Tresini, M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00242-7 · Cited by 1,297 · see citing works
Generation of reactive oxygen species by the mitochondrial electron transport chain
Liu, Y., Fiskum, G., & Schubert, D. (2002) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2002.00744.x · Cited by 1,260 · see citing works
Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
Turrens, J. F., Alexandre, A., & Lehninger, A. L. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90293-0 · Cited by 1,214 · see citing works
Self-citationFree Radicals in Biology and Medicine
Kovacic, P. (1986) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.2600750133 · Cited by 982 · see citing works
Kushnareva, Y., Murphy, A. N., & Andreyev, A. Y. (2002) · Biochemical Journal · doi:10.1042/bj20021121 · Cited by 677 · see citing works
Votyakova, T. V., & Reynolds, I. J. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00548.x · Cited by 601 · see citing works
Mitochondrial disease in superoxide dismutase 2 mutant mice
Melov, S., Coskun, P., Patel, M., Tuinstra, R., Cottrell, B., Jun, A. S., Zastawny, T. H., Dizdaroglu, M., Goodman, S. I., Huang, T.-T., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.3.846 · Cited by 581 · see citing works
Lambert, A. J., & Brand, M. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406576200 · Cited by 480 · see citing works
LAMBERT, A. J., & BRAND, M. D. (2004) · Biochemical Journal · doi:10.1042/bj20040485 · Cited by 470 · see citing works
Insulin, ketone bodies, and mitochondrial energy transduction
Sato, K., Kashiwaya, Y., Keon, C. A., Tsuchiya, N., King, M. T., Radda, G. K., Chance, B., Clarke, K., & Veech, R. L. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.8.7768357 · Cited by 455 · see citing works
McCORMACK, J. G., & Denton, R. M. (1979) · Biochemical Journal · doi:10.1042/bj1800533 · Cited by 453 · see citing works
Dependence of H2O2 formation by rat heart mitochondria on substrate availability and donor age
Hansford, R. G., Hogue, B. A., & Mildaziene, V. (1997) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1022420007908 · Cited by 447 · see citing works
Mason, M. G., Nicholls, P., Wilson, M. T., & Cooper, C. E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506562103 · Cited by 233 · see citing works
Han, D., Canali, R., Rettori, D., & Kaplowitz, N. (2003) · Molecular Pharmacology · doi:10.1124/mol.64.5.1136 · Cited by 212 · see citing works
On the mechanism and biology of cytochrome oxidase inhibition by nitric oxide
Antunes, F., Boveris, A., & Cadenas, E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405368101 · Cited by 189 · see citing works
Respiration-dependent Removal of Exogenous H2O2 in Brain Mitochondria
Zoccarato, F., Cavallini, L., & Alexandre, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308143200 · Cited by 130 · see citing works
Self-citationDopamine-derived Dopaminochrome Promotes H2O2 Release at Mitochondrial Complex I
Zoccarato, F., Toscano, P., & Alexandre, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500657200 · Cited by 95 · see citing works
Self-citation[11] α-ketoglutarate dehydrogenase from pig heart
Sanadi, D. R. (1969) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(69)13015-3 · Cited by 48 · see citing works
GOODALL, A. A., & MARSHALL, R. D. (1980) · Biochemical Journal · doi:10.1042/bj1890533 · Cited by 36 · see citing works
Flagged first, then by citations
1 of the 26 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
The role of mitochondria in reactive oxygen species metabolism and signaling
Starkov, A. A. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.015 · Cited by 846 · see citing works
Reactive Oxygen Species in the Regulation of Synaptic Plasticity and Memory
Massaad, C. A., & Klann, E. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3208 · Cited by 635 · see citing works
Sites of reactive oxygen species generation by mitochondria oxidizing different substrates
Quinlan, C. L., Perevoshchikova, I. V., Hey‐Mogensen, M., Orr, A. L., & Brand, M. D. (2013) · Redox Biology · doi:10.1016/j.redox.2013.04.005 · Cited by 595 · see citing works
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
Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471 · see citing works
Beckhauser, T. F., Francis-Oliveira, J., & De Pasquale, R. (2016) · Journal of Experimental Neuroscience · doi:10.4137/jen.s39887 · Cited by 301 · see citing works
Superoxide Is Produced by the Reduced Flavin in Mitochondrial Complex I
Pryde, K. R., & Hirst, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.186841 · Cited by 301 · see citing works
Shandilya, S., Kumar, S., Jha, N. K., Kesari, K. K., & Ruokolainen, J. (2021) · Journal of Advanced Research · doi:10.1016/j.jare.2021.09.005 · Cited by 300 · see citing works
Heavy metals induced mitochondrial dysfunction in animals: Molecular mechanism of toxicity
Sun, Q., Li, Y., Shi, L., Hussain, R., Mehmood, K., Tang, Z., & Zhang, H. (2022) · Toxicology · doi:10.1016/j.tox.2022.153136 · Cited by 262 · see citing works
Calcium and Mitochondrial Reactive Oxygen Species Generation: How to Read the Facts
Ádám‐Vizi, V., & Starkov, A. A. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100465 · Cited by 250 · 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
Potential Therapeutic Benefits of Strategies Directed to Mitochondria
Camara, A. K. S., Lesnefsky, E. J., & Stowe, D. F. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2788 · Cited by 195 · see citing works
The mitochondrial free radical theory of ageing - Where do we stand?
Gruber, J. (2008) · Frontiers in bioscience · doi:10.2741/3174 · Cited by 168 · see citing works
Dambrova, M., Zuurbier, C. J., Borutaitė, V., Liepinsh, E., & Makrecka‐Kuka, M. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.01.036 · Cited by 165 · see citing works
Muller, F. L., Liu, Y., Abdul-Ghani, M. A., Lustgarten, M. S., Bhattacharya, A., Jang, Y. C., & Van Remmen, H. (2008) · Biochemical Journal · doi:10.1042/bj20071162 · Cited by 150 · see citing works
Mitochondrial Approaches to Protect Against Cardiac Ischemia and Reperfusion Injury
Camara, A. K. S., Bienengraeber, M., & Stowe, D. F. (2011) · Frontiers in Physiology · doi:10.3389/fphys.2011.00013 · Cited by 150 · see citing works
Jurcău, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111847 · Cited by 150 · 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
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
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
Mitochondrial (‘mild’) uncoupling and ROS production: Physiologically relevant or not?
Shabalina, I. G., & Nedergaard, J. (2011) · Biochemical Society Transactions · doi:10.1042/bst0391305 · Cited by 110 · see citing works
Neuronal and Vascular Oxidative Stress in Alzheimers Disease
Massaad, C. A. (2011) · Current Neuropharmacology · doi:10.2174/157015911798376244 · Cited by 102 · see citing works
Moreno‐Sánchez, R., Hernández‐Esquivel, L., Rivero‐Segura, N. A., Marín‐Hernández, A., Neuzil, J., Ralph, S. J., & Rodríguez‐Enríquez, S. (2013) · The FEBS Journal · doi:10.1111/febs.12086 · Cited by 100 · see citing works
Schönfeld, P., Wieckowski, M. R., Lebiedzińska, M., & Wojtczak, L. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.01.010 · Cited by 100 · see citing works
Hickey, A. J., Renshaw, G. M. C., Speers‐Roesch, B., Richards, J. G., Wang, Y., Farrell, A. P., & Brauner, C. J. (2011) · Journal of Comparative Physiology B · doi:10.1007/s00360-011-0599-6 · Cited by 90 · see citing works
Lambert, A. J., Buckingham, J. A., Boysen, H. M., & Brand, M. D. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00538.x · Cited by 70 · see citing works
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Goncalves, R. L. S., Bunik, V. I., & Brand, M. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.12.020 · Cited by 70 · see citing works
Lee, J., Go, Y., Kim, D. Y., Lee, S. H., Kim, O., Jeon, Y. H., Kwon, T. K., Bae, J., Song, D., Rhyu, I. J., et al. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-0379-z · Cited by 67 · see citing works
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Chinta, S. J., Rane, A., Yadava, N., Andersen, J. K., Nicholls, D. G., & Polster, B. M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.01.010 · Cited by 62 · see citing works
Martínez-Moya, P., Niehaus, K., Alcaı́no, J., Baeza, M., & Cifuentes, V. (2015) · BMC Genomics · doi:10.1186/s12864-015-1484-6 · Cited by 62 · see citing works
Panov, A. V., Schönfeld, P., Dikalov, S., Hemendinger, R. A., Bonkovsky, H. L., & Brooks, B. R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900985200 · Cited by 62 · see citing works
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Weissman, D., & Maack, C. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.05.013 · Cited by 59 · see citing works
Dey, S. K., Bose, D., Hazra, A., Naskar, S., Nandy, A., Munda, R. N., Das, S., Chatterjee, N., Mondal, N. B., Banerjee, S., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058055 · Cited by 54 · see citing works
Thirupathi, A., Freitas, S., Sorato, H. R., Pedroso, G. S., Effting, P. S., Damiani, A. P., de Andrade, V. M., Nesi, R. T., Gupta, R. C., Muller, A. P., et al. (2018) · Nutrition · doi:10.1016/j.nut.2018.03.058 · Cited by 39 · see citing works
Ghosh, R., Hwang, S. M., Cui, Z., Gilda, J. E., & Gomes, A. V. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.03.016 · Cited by 37 · see citing works
Ouyang, Y., Chen, Z., Tan, M., Liu, A., Chen, M., Liu, J., Pi, R., & Fang, J. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.10.160 · Cited by 36 · see citing works
Sanz, A., Stefanatos, R. K. A., & Mcilroy, G. D. (2010) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-010-9281-z · Cited by 36 · see citing works
Wang, L., Wang, R., Jin, M., Huang, Y., Liu, A., Qin, J., Chen, M., Wen, S., Pi, R., & Shen, W. (2014) · Neurochemical Research · doi:10.1007/s11064-014-1367-2 · Cited by 36 · see citing works
Hickey, A. J., Chai, C. C., Choong, S. Y., Costa, S. D. F., Skea, G. L., Phillips, A. R. J., & Cooper, G. J. S. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00111.2009 · Cited by 35 · see citing works
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Self-citationLaure, L., Long, R., Lizano, P. L., Zini, R., Berdeaux, A., Depré, C., & Morin, D. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.03.001 · Cited by 26 · see citing works
Luo, L., Chen, J., Su, D., Chen, M., Luo, B., Pi, R., Wang, L., Shen, W., & Wang, R. (2017) · Neurochemical Research · doi:10.1007/s11064-016-2117-4 · Cited by 23 · see citing works
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Strutynska, N. A., Strutynskyi, R. B., Chorna, S. V., Semenykhina, O. M., Mys', L., Moibenko, O. O., & Sahach, V. F. (2014) · Fìzìologìčnij žurnal · doi:10.15407/fz59.06.003 · Cited by 6 · see citing works
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三上, 貴. (2016) · Institutional Repositories DataBase (IRDB) · doi:10.15083/00073664
- Authors
- Zoccarato, F., Cavallini, L., Bortolami, S., & Alexandre, A.
- Affiliations
- University of Padua (IT)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2007-07-26
- Volume
- 406
- Issue
- 1
- Pages
- 125-129
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1948981
- OpenAlex
- W2044707953
- Cited by
- 66
- References
- 26
- Citations by year
- 2025: 2 · 2022: 1 · 2021: 6 · 2020: 2 · 2018: 2 · 2017: 1 · 2016: 4 · 2015: 3 · 2014: 3 · 2013: 7 · 2012: 7
- FWCI
- 2.51
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion, other-oa)
- Padua Research Archive (University of Padova) (submittedVersion)
- 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 › Redox biology and oxidative stress
- Keywords
- succinic acid, hydrogen peroxide release, complex I, brain mitochondria, glutamate-malate, rotenone sensitivity, alpha-oxoglutarate, electron flow, oxygen consumption, NAD-linked substrates
- MeSH terms
- Animals, Electron Transport, Hydrogen Peroxide, Hydrogen-Ion Concentration, Ketoglutaric Acids, Malates, Mitochondria, Oxidation-Reduction, Oxygen Consumption, Substrate Specificity, Succinates, Titrimetry, Glutamic Acid, Electron Transport Complex I, Rats
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