Functional role of mitochondrial respiratory supercomplexes
Open accessAbstract
Recent experimental evidence has replaced the random diffusion model of electron transfer with a model of supramolecular organisation based upon specific interactions between individual respiratory complexes. These supercomplexes were found to be functionally relevant by flux control analysis and to confer a kinetic advantage to NAD-linked respiration (channelling). However, the Coenzyme Q pool is still required for FAD-linked oxidations and for the proper equilibrium with Coenzyme Q bound in the supercomplex. Channelling in the cytochrome c region probably also occurs but does not seem to confer a particular kinetic advantage. The supramolecular association of individual complexes strongly depends on membrane lipid amount and composition and is affected by lipid peroxidation; it also seems to be modulated by membrane potential and protein phosphorylation. Additional properties of supercomplexes are stabilisation of Complex I, as evidenced by the destabilising effect on Complex I of mutations in either Complex III or IV, and prevention of excessive generation of reactive oxygen species. The dynamic character of the supercomplexes allows their involvement in metabolic adaptations and in control of cellular signalling pathways. This article is part of a Special Issue entitled: Dynamic and ultrastructure of bioenergetic membranes and their components.
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The oxidative phosphorylation complexes associate in supercomplexes of the three proton-translocating units: Complex I, Complex III, and Complex IV.
“Numerous studies utilizing blue native gel electrophoresis, preserving the fidelity of weakly associated members of protein complexes (22), have repeatedly shown that the oxidative phosphorylation complexes associate in supercomplexes of the three proton-translocating units: Complex I, Complex III, and Complex IV (19, 23, 24).”
From Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies (2016) · cites this paper as [24]
CYP11A1-FDXR electron transport occurs in a physically associated metabolon, much like the electron transport of respirasomes.
“Taken together, these findings support a model for CYP11A1–FDXR electron transport occurring in a physically associated metabolon, much akin to the electron transport of the respirasomes discussed above (24).”
From Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies (2016) · cites this paper as [24]
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Multifunctional Cytochrome c : Learning New Tricks from an Old Dog
Álvarez-Paggi, D., Hannibal, L., Castro, M. A., Rouco, S. O., Demicheli, V., Tórtora, V., Tomasina, F., Radí, R., & Murgida, D. H. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00257 · Cited by 253 · see citing works
Cytonuclear integration and coevolution
Sloan, D. B., Warren, J., Williams, A. M., Wu, Z.-Q., Abdel-Ghany, S., Chicco, A., & Havird, J. C. (2018) · Nature reviews genetics · doi:10.1038/s41576-018-0035-9 · Cited by 205 · see citing works
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The subunit composition and function of mammalian cytochrome c oxidase
Kadenbach, B., & Hüttemann, M. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.07.002 · Cited by 244 · see citing works
Structure and mechanism of mitochondrial electron transport chain
Guo, R., Gu, J., Zong, S., Wu, M., & Yang, M. (2018) · Biomedical Journal · doi:10.1016/j.bj.2017.12.001 · Cited by 238 · see citing works
Complex IV – The regulatory center of mitochondrial oxidative phosphorylation
Kadenbach, B. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.10.004 · Cited by 212 · see citing works
A radical shift in perspective: mitochondria as regulators of reactive oxygen species
Munro, D., & Treberg, J. R. (2017) · Journal of Experimental Biology · doi:10.1242/jeb.132142 · Cited by 207 · see citing works
“For example, macromolecular supercomplexes have been implicated in altering the production of superoxide (Genova and Lenaz, 2014), which – alongside modifications such as glutathionylation – could influence mitochondrial H2O2 production (Mailloux and Treberg, 2016).”
BackgroundVial, G., Chauvin, M., Bendridi, N., Durand, A., Meugnier, E., Madec, A., Bernoud‐Hubac, N., de Barros, J.-P. P., Fontaine, E. M., Acquaviva, C., et al. (2014) · Diabetes · doi:10.2337/db14-1220 · Cited by 194 · see citing works
“Moreover, because cardiolipins modulate the interactions and activities of mitochondrial complexes (32,33), regulate OXPHOS chain efficacy, and reduce ROS production (34), we propose that the imeglimin-induced increase in cardiolipins could participate in inducing CIII activity and reducing ROS production by liver mit…”
BackgroundBlaza, J. N., Serreli, R., Jones, A. J. Y., Mohammed, K., & Hirst, J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1413855111 · Cited by 181 · see citing works
“It is difficult to envisage mechanistically how supercomplexes could exert primary effects on the formation of reactive oxygen species, and only limited circumstantial evidence has been presented to support this proposal (33).”
BackgroundCoenzyme Q biosynthesis and its role in the respiratory chain structure
Alcázar‐Fabra, M., Navas, P., & Brea‐Calvo, G. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.03.010 · Cited by 173 · see citing works
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Mitochondria: Are they causal players in cellular senescence?
Correia-Melo, C., & Passos, J. F. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.05.017 · Cited by 160 · see citing works
“During oxidative phosphorylation, organic molecules are oxidised in reactions that are coupled to the reduction of electron carriers such as the nicotinamide adenine dinucleotide (NAD+) [31].”
BackgroundInfluentialThe mechanism of cyclic electron flow
Nawrocki, W. J., Bailleul, B., Picot, D., Cardol, P., Rappaport, F., Wollman, F.-A., & Joliot, P. A. (2019) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.12.005 · Cited by 160 · see citing works
Mitochondria as a Target for Mitigating Sarcopenia
Coen, P. M., Musci, R., Hinkley, J., & Miller, B. F. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2018.01883 · Cited by 140 · see citing works
Paradies, G., Paradies, V., Ruggiero, F. M., & Petrosillo, G. (2018) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00028.2018 · Cited by 143 · see citing works
“Studies from our and other laboratories have shown alterations in bioenergetic parameters, such as decreased rate of mitochondrial oxygen consumption, reduced activity of complexes I, III, and IV, and increased basal rate of H2O2 production in mitochondria isolated from Langendorff-perfused rat heart subjected to glob…”
BackgroundWang, Y., Palmfeldt, J., Gregersen, N., Makhov, A. M., Conway, J. F., Wang, M., McCalley, S., Basu, S., Alharbi, H., Croix, C. M. S., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008680 · Cited by 133 · see citing works
The mitochondrial permeability transition pore in AD 2016: An update
Biasutto, L., Azzolini, M., Szabó, I., & Zoratti, M. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.02.012 · Cited by 128 · 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
“Indeed, several studies in vitro support the view that electron transfer in the respiratory chain can occur in absence of SCs, though with lower efficiency (122).”
Self-citationCannabinoid-induced changes in respiration of brain mitochondria
Fišar, Z., Singh, N., & Hroudová, J. (2014) · Toxicology Letters · doi:10.1016/j.toxlet.2014.09.002 · Cited by 124 · see citing works
Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies
Midzak, A., & Papadopoulos, V. (2016) · Frontiers in Endocrinology · doi:10.3389/fendo.2016.00106 · Cited by 114 · see citing works
“Taken together, these findings support a model for CYP11A1–FDXR electron transport occurring in a physically associated metabolon, much akin to the electron transport of the respirasomes discussed above (24).”
BackgroundCyclophilin D, Somehow a Master Regulator of Mitochondrial Function
Porter, G. A., & Beutner, G. (2018) · Biomolecules · doi:10.3390/biom8040176 · Cited by 114 · see citing works
“translocation into the cytoplasm (Figure 1b) [10-15].”
Complex I function in mitochondrial supercomplexes
Lenaz, G., Tioli, G., Falasca, A. I., & Genova, M. L. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.01.013 · Cited by 109 · see citing works
Self-citationMembrane-bound electron transport systems of an anammox bacterium: A complexome analysis.
de Almeida, N. M., Wessels, H. C., de Graaf, R. D., Ferousi, C., Jetten, M., Keltjens, J., & Kartal, B. (2016) · Biochimica et Biophysica Acta · doi:10.1016/j.bbabio.2016.07.006 · Cited by 110 · see citing works
Exercise increases mitochondrial complex I activity and DRP1 expression in the brains of aged mice
Gusdon, A. M., Callio, J., Distéfano, G., O'Doherty, R. M., Goodpaster, B. H., Coen, P. M., & Chu, C. T. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.01.013 · Cited by 109 · see citing works
“In addition, mitochondrial function is governed by supercomplexes formed between complexes I and III and also among complexes I, III, and IV (Genova and Lenaz, 2014).”
BackgroundGuerra‐Castellano, A., Dı́az-Quintana, A., Pérez‐Mejías, G., Elena‐Real, C. A., González‐Arzola, K., García‐Mauriño, S. M., la Rosa, M. Á. D., & Díaz‐Moreno, I. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1806833115 · Cited by 105 · see citing works
“Respiratory supercomplexes provide higher efficiency to the electron transport during OxPhos, thereby minimizing the generation of ROS (12).”
The Paradox of Mitochondrial Dysfunction and Extended Longevity
Munkácsy, E., & Rea, S. L. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.03.016 · Cited by 101 · see citing works
“…has more in common with these other matrix-localized enzymes than with the other canonical ETC complexes: It does not pump protons, it is comprised exclusively of nuclear-encoded subunits, and it is not integral to supercomplex formation (Genova and Lenaz 2013; Schagger and Pfeiffer 2001).”
BackgroundCardiolipin, the Mitochondrial Signature Lipid: Implication in Cancer
Pour, S. T. A., Mahéo, K., Servais, S., Brisson, L., & Dumas, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218031 · Cited by 102 · see citing works
“ETC protein complexes are organized into the higher organized structures known as supercomplexes or « respirasome » in order to improve the electron transfer efficiency [48,49].”
BackgroundSullivan, E. M., Pennington, E. R., Green, W. D., Beck, M. A., Brown, D. A., & Shaikh, S. R. (2018) · Advances in Nutrition · doi:10.1093/advances/nmy007 · Cited by 104 · see citing works
The Respiratory Chain Supercomplex Organization Is Independent of COX7a2l Isoforms
Mourier, A., Matic, S., Ruzzenente, B., Larsson, N., & Milenkovic, D. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.11.005 · Cited by 95 · see citing works
Plant Mitochondrial Inner Membrane Protein Insertion
Kolli, R., Soll, J., & Carrie, C. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020641 · Cited by 98 · see citing works
Altered mitochondrial metabolism in the insulin‐resistant heart
Makrecka‐Kuka, M., Liepinsh, E., Murray, A. J., Lemieux, H., Dambrova, M., Tepp, K., Puurand, M., Käämbre, T., Han, W. H., de Goede, P., et al. (2019) · Acta Physiologica · doi:10.1111/apha.13430 · Cited by 93 · see citing works
He, C. H., Xie, L. X., Allan, C. M., Tran, U. C., & Clarke, C. F. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.12.017 · Cited by 95 · see citing works
“It is tempting to speculate that Coq10 may function to chaperone the “inactive” pool of Q (depicted as residing at the midplane of the bilayer [80, 81]) to form an “active” pool of Q, consistent with a dedicated subset of Q molecules performing electron transport within the respirasomes [82, 83].”
BackgroundStructure and Mechanism of Respiratory III–IV Supercomplexes in Bioenergetic Membranes
Brzezinski, P., Moe, A., & Ädelroth, P. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00140 · Cited by 93 · see citing works
Cyclophilin D regulates the dynamic assembly of mitochondrial ATP synthase into synthasomes
Beutner, G., Alanzalon, R. E., & Porter, G. A., Jr. (2017) · Scientific Reports · doi:10.1038/s41598-017-14795-x · Cited by 95 · see citing works
Molecular mechanism of cardiolipin-mediated assembly of respiratory chain supercomplexes
Arnarez, C., Marrink, . J., & Périole, X. (2016) · Chemical Science · doi:10.1039/c5sc04664e · Cited by 94 · see citing works
Mitochondrial Redox Dysfunction and Environmental Exposures
Caito, S. W., & Aschner, M. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6289 · Cited by 94 · see citing works
“A variety of supercomplexes have been purified, consisting of complex I + complex III, complex III + complex IV, complex II + complex IV, or complex I + complex III + complex IV (55), giving rise to a ‘‘plastic’’ model for the organization.”
BackgroundCoQ10 a super-vitamin: review on application and biosynthesis
Shukla, S., & Dubey, K. K. (2018) · 3 Biotech · doi:10.1007/s13205-018-1271-6 · Cited by 85 · see citing works
New and revisited approaches to preserving the reperfused myocardium
Kloner, R. A., Brown, D. A., CSETE, M. E., Dai, W., Downey, J. M., Gottlieb, R. A., Hale, S. L., & Shi, J. (2017) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2017.102 · Cited by 83 · see citing works
Mechanistic Details of Early Steps in Coenzyme Q Biosynthesis Pathway in Yeast
Payet, L.-A., Leroux, M., Willison, J. C., Kihara, A., Pélosi, L., & Pierrel, F. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.08.008 · Cited by 82 · see citing works
“The electrochemical gradient used for ATP synthesis is generated by the respiratory chain in which the redox lipid coenzyme Q (Q) transfers electrons between membrane-embedded multiprotein complexes responsible for proton pumping (Genova and Lenaz, 2014; Wang and Hekimi, 2016).”
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
“Respiratory SCs have been described and characterized in the mitochondria of several mammalian tissues and in many other organisms, also including plants, fungi and bacteria [42].”
BackgroundInfluentialSelf-citationWang, Y., Lilienfeldt, N., & Hekimi, S. (2024) · Physiological Reviews · doi:10.1152/physrev.00040.2023 · Cited by 83 · see citing works
Protective role of melatonin in mitochondrial dysfunction and related disorders
Paradies, G., Paradies, V., Ruggiero, F. M., & Petrosillo, G. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1475-z · Cited by 79 · see citing works
Miller, V. J., LaFountain, R. A., Barnhart, E. C., Sapper, T. N., Short, J. A., Arnold, W. D., Hyde, P. N., Crabtree, C. D., Kackley, M. L., Kraemer, W. J., et al. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00305.2020 · Cited by 81 · see citing works
Tomková, V., Sandoval-Acuña, C., Torrealba, N., & Truksa, J. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.09.004 · Cited by 76 · see citing works
Sex differences in brain mitochondrial metabolism: influence of endogenous steroids and stroke
Gaignard, P., Fréchou, M., Lière, P., Thérond, P., Schumacher, M., Slama, A., & Guennoun, R. (2017) · Journal of Neuroendocrinology · doi:10.1111/jne.12497 · Cited by 76 · see citing works
Huang, Y., Sarkhel, S., Roy, A., & Mohan, A. (2023) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2023.2245029 · Cited by 74 · see citing works
“This pathway primarily consists of four enzyme complexes (complexes I (NADH), II, III, and IV), two mobile electron carriers (coenzyme Q and cytochrome C), and the involvement of cytochrome C in the electronic respiratory chain (Genova and Lenaz 2014).”
Winter, L., Wittig, I., Peeva, V., Eggers, B., Heidler, J., Chevessier, F., Kley, R. A., Barkovits, K., Strecker, V., Berwanger, C., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1592-7 · Cited by 74 · see citing works
“The formation of supercomplexes is thought to be essential for the stability of the individual complexes [1, 10, 21], efficient substrate channeling [27], and for the prevention of reactive oxygen species generation [49].”
BackgroundMüller, C. S., Bildl, W., Haupt, A., Ellenrieder, L., Becker, T., Hunte, C., Fakler, B., & Schulte, U. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.054080 · Cited by 73 · see citing works
“organization and function of the dynamic entity (31, 32).”
BackgroundCarden, T., Singh, B. P., Mooga, V. P., Bajpai, P., & Singh, K. K. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.797001 · Cited by 71 · see citing works
“The expression of OXPHOS subunits, their assembly factor– mediated construction into larger complexes, and the stability of those complexes determine, in part, the enzymatic activity of each complex (34).”
BackgroundMitochondrial Membrane Dynamics—Functional Positioning of OPA1
Lee, H., & Yoon, Y. (2018) · Antioxidants · doi:10.3390/antiox7120186 · Cited by 70 · see citing works
“The supercomplex assembly of the ETC complexes is thought to promote efficient electron transport [10,11].”
BackgroundSirey, T., Roberts, K., Haerty, W., Bedoya-Reina, O. C., Rogatti, S., Tan, J. Y., Li, N., Heather, L. C., Carter, R. N., Cooper, S., et al. (2019) · eLife · doi:10.7554/elife.45051 · Cited by 68 · see citing works
“Our observation of increased enzymatic activity may relate to the formation, by the complexes of the respiratory chain, of higher order supercomplexes ( Scha¨gger and Pfeiffer, 2000 ; Genova and Lenaz, 2014 ).”
Zhou, X., Zhang, Z., Liu, X., Wu, D., Ding, Y., Li, G., & Wu, Y. (2020) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12535 · Cited by 69 · see citing works
Moe, A., Trani, J. M. D., Rubinstein, J. L., & Brzezinski, P. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2021157118 · Cited by 68 · see citing works
Control of mitochondrial function and cell growth by the atypical cadherin Fat1
Cao, L. L., Riascos‐Bernal, D. F., Chinnasamy, P., Dunaway, C. M., Hou, R., Pujato, M. A., O'Rourke, B. P., Miskolci, V., Guo, L., Hodgson, L., et al. (2016) · Nature · doi:10.1038/nature20170 · Cited by 67 · see citing works
Mitochondrial bioenergetics decay in aging: beneficial effect of melatonin
Paradies, G., Paradies, V., Ruggiero, F. M., & Petrosillo, G. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2619-5 · Cited by 64 · see citing works
“In addition, the supercomplex organization of the ETC, seems to minimize the production of reactive oxygen species [110].”
BackgroundMitochondrial Actions of Thyroid Hormone
Lanni, A., Moreno, M., & Goglia, F. (2016) · Comprehensive physiology · doi:10.1002/cphy.c150019 · Cited by 64 · see citing works
Desmurs, M., Foti, M., Raemy, E., Vaz, F. M., Martinou, J., Bairoch, A., & Lane, L. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.01047-14 · Cited by 61 · see citing works
“The functional role of these SC is still under debate, but recent studies have proposed that they can participate in electron transfer and substrate channeling (14), reduce oxidative damage by decreasing the generation of reactive oxygen species by complex I (15), and confer structural stability on respiratory enzymes…”
BackgroundKôrge, P., John, S., Calmettes, G., & Weiss, J. N. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.768325 · Cited by 63 · see citing works
Antioxidant effect of exercise: Exploring the role of the mitochondrial complex I superassembly
Huertas, J. R., Fazazi, S. A., Hidalgo‐Gutiérrez, A., López, L. C., & Casuso, R. A. (2017) · Redox Biology · doi:10.1016/j.redox.2017.07.009 · Cited by 60 · see citing works
Coenzyme Q10 effects in neurological diseases
Rauchová, H. (2021) · Physiological Research · doi:10.33549/physiolres.934712 · Cited by 63 · see citing works
Wang, L., Duan, Q., Wang, T., Ahmed, M., Zhang, N., Li, Y., Li, L., & Yao, X. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/217670 · Cited by 59 · see citing works
Therapeutic Efficacy of Molecular Hydrogen: A New Mechanistic Insight
Ishibashi, T. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666190506123038 · Cited by 58 · see citing works
Amazing structure of respirasome: unveiling the secrets of cell respiration
Guo, R., Gu, J., Wu, M., & Yang, M. (2016) · Protein & Cell · doi:10.1007/s13238-016-0329-7 · Cited by 54 · see citing works
“The electron delivered to heme bL was further 1900 Janus Green B was found to serve as mitochondria specific stain 1912 Mitochondria were coarsely extracted from hepatocyte 1920s~1930s Cytochrome system was associated with cellular structures 1940s Well-preserved mitochondria were extracted 1980s Entensive study of ce…”
BackgroundInfluentialWelchen, E., & González, D. H. (2016) · Physiologia Plantarum · doi:10.1111/ppl.12449 · Cited by 53 · see citing works
“In plants, supercomplexes conformed by complexes I, III and IV, adopting the stoichiometry I:III2:IV in a configuration that may allow CYTc binding, were described (Eubel et al. 2004, Dudkina et al. 2006, Genova and Lenaz 2014).”
BackgroundMolecular aspects of β, β-carotene-9′, 10′-oxygenase 2 in carotenoid metabolism and diseases
Wu, L., Guo, X., Wang, W., Medeiros, D. M., Clarke, S. L., Lucas, E. A., Smith, B. J., & Lin, D. (2016) · Experimental Biology and Medicine · doi:10.1177/1535370216657900 · Cited by 53 · see citing works
“Recent evidence supports the function of these supercomplexes, including: (1) the formation of mitochondrial respiratory chain supercomplexes could minimize the production of ROS which is generated from complex I,(81) (2) the mitochondrial respiratory chain supercomplexes may intergrate the cytochrome c and coenzyme Q…”
BackgroundBioenergetic Aspects of Mitochondrial Actions of Thyroid Hormones
Cioffi, F., Giacco, A., Goglia, F., & Silvestri, E. (2022) · Cells · doi:10.3390/cells11060997 · Cited by 55 · see citing works
“Functionally, the assembly of SCs has been proposed to have several biological significances, among which are: reduction of ROS generation [162,163]; optimization of the catalytic activity of the individual complexes [164]; boost of the efficiency of electron transfer through substrate channeling [145,149,165]; stabil…”
BackgroundKuter, K. Z., Kratochwil, M., Berghauzen-Maciejewska, K., Głowacka, U., Sugawa, M. D., Ossowska, K., & Dencher, N. A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.01.022 · Cited by 52 · see citing works
Novack, G. V., Galeano, P., Castaño, E. M., & Morelli, L. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00600 · Cited by 52 · see citing works
Beutner, G., Eliseev, R. A., & Porter, G. A., Jr. (2014) · PLoS ONE · doi:10.1371/journal.pone.0113330 · Cited by 51 · see citing works
“The formation of respiratory supercomplexes To increase the efficiency of the ETC in some tissues including the heart, Cx-1 is thought to form ‘‘solid state’’ supercomplexes with Cx-3, Cx-4, ubiquinone, and cytochrome c (8,10,30) Therefore, as our data suggests that the efficiency of electron transfer from Cx-1 to Cx-…”
BackgroundIsolation of yeast complex IV in native lipid nanodiscs
Smirnova, I. A., Sjöstrand, D., Li, F., Björck, M. L., Schäfer, J., Østbye, H., Högbom, M., von Ballmoos, C., Lander, G. C., Ädelroth, P., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2016.09.004 · Cited by 51 · see citing works
“bc1 and that the Rcf proteins are presumably weakly bound [23-25, 40-49].”
BackgroundMass-spectrometry-based proteomics reveals mitochondrial supercomplexome plasticity
González-Franquesa, A., Stocks, B., Chubanava, S., Hattel, H. B., Moreno‐Justicia, R., Peijs, L., Treebak, J. T., Zierath, J. R., & Deshmukh, A. S. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109180 · Cited by 51 · see citing works
Kobayashi, A., Azuma, K., Ikeda, K., & Inoue, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186683 · Cited by 50 · see citing works
CoQ10 and Mitochondrial Dysfunction in Alzheimer’s Disease
Fišar, Z., & Hroudová, J. (2024) · Antioxidants · doi:10.3390/antiox13020191 · Cited by 55 · see citing works
“The efficiency of the OXPHOS system, especially the transfer of electrons by means of CoQ 10 and the Q-cycle, is influenced by the existence and organization of respiratory supercomplexes [106,107].”
BackgroundAcute RyR1 Ca2+ leak enhances NADH-linked mitochondrial respiratory capacity
Zanou, N., Dridi, H., Reiken, S. R., de Lima, T. I., Donnelly, C., Marchi, U. D., Ferrini, M., Vidal, J., Sittenfeld, L. R., Feige, J. N., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27422-1 · Cited by 46 · see citing works
Caza, M., Hu, G., Price, M., Perfect, J. R., & Kronstad, J. W. (2016) · mSphere · doi:10.1128/msphere.00080-15 · Cited by 48 · see citing works
“This process occurs in mitochondrial cristae and includes the four complexes (I to IV) of the electron transport chain (ETC) that shuttle electrons from NADH and succinate to generate a proton gradient to ultimately produce ATP and reduce oxygen to water (21, 22).”
Regulatory role of the respiratory supercomplex factors in Saccharomyces cerevisiae
Lundin, C. R., von Ballmoos, C., Ott, M., Ädelroth, P., & Brzezinski, P. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1601196113 · Cited by 47 · see citing works
Nitrite Protects Mitochondrial Structure and Function under Hypoxia
Gupta, K. J., Lee, C. P., & Ratcliffe, R. G. (2016) · Plant and Cell Physiology · doi:10.1093/pcp/pcw174 · Cited by 47 · see citing works
Disturbed Flow Induces Autophagy, but Impairs Autophagic Flux to Perturb Mitochondrial Homeostasis
Li, R., Jen, N., Wu, L., Lee, J., Fang, K., Quigley, K., Lee, K. J., Wang, S., Zhou, B., Vergnes, L., et al. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5896 · Cited by 46 · see citing works
“coupled with respiratory chain complexes I to II, III, and IV (23, 30).”
Degradation of the mitochondrial complex I assembly factor TMEM126B under chronic hypoxia
Fuhrmann, D. C., Wittig, I., Dröse, S., Schmid, T., Dehne, N., & Brüne, B. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2779-y · Cited by 45 · see citing works
The new role of F1Fo ATP synthase in mitochondria-mediated neurodegeneration and neuroprotection
Mnatsakanyan, N., & Jonas, E. A. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113400 · Cited by 43 · see citing works
Distribution and dynamics of OXPHOS complexes in the bacterial cytoplasmic membrane
Magalon, A., & Alberge, F. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.10.015 · Cited by 45 · see citing works
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“It is believed that both protein and phospholipid components of the mitochondrial inner membrane (IMM) may contribute to the pH-driven regulation [24].”
BackgroundAssociation between ROS production, swelling and the respirasome integrity in cardiac mitochondria
Jang, S., & Javadov, S. A. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.07.009 · Cited by 44 · see citing works
“283 Notably, growing number of studies demonstrate interdependence between ETC individual 284 complexes involved in SCs (Reviewed in [38,39]).”
Pan, R., Kaur, N., & Hu, J.-P. (2014) · The Plant Journal · doi:10.1111/tpj.12532 · Cited by 40 · see citing works
Cytochrome c : Surfing Off of the Mitochondrial Membrane on the Tops of Complexes III and IV
Pérez‐Mejías, G., Guerra‐Castellano, A., Dı́az-Quintana, A., la Rosa, M. Á. D., & Díaz‐Moreno, I. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.05.002 · Cited by 42 · see citing works
Azoles activate type I and type II programmed cell death pathways in crop pathogenic fungi
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“This conclusion was agreed with the editor of this submission.”
Shinzawa‐Itoh, K., Shimomura, H., Yanagisawa, S., Shimada, S., Takahashi, R., Oosaki, M., Ogura, T., & Tomitake Tsukihara, A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.680553 · Cited by 41 · see citing works
- Authors
- Genova, M. L., & Lenaz, G.
- Affiliations
- University of Bologna (IT)
- Corresponding author
- Genova, Maria Luisa
- ORCID
- Genova, Maria Luisa
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 2014-04
- Volume
- 1837
- Issue
- 4
- Pages
- 427-443
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W2006849545
- Cited by
- 306
- References
- 187
- Citations by year
- 2026: 10 · 2025: 8 · 2024: 15 · 2023: 17 · 2022: 17 · 2021: 24 · 2020: 30 · 2019: 27 · 2018: 32 · 2017: 34 · 2016: 43 · 2015: 31 · 2014: 15 · 2013: 2
- FWCI
- 2.85
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- Archivio istituzionale della ricerca (Alma Mater Studiorum Università di Bologna) (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 › ATP Synthase and ATPases Research
- Keywords
- electron transfer, supramolecular organization, flux control, channeling, coenzyme Q10, cytochrome c, membrane lipid composition, lipid peroxidation, membrane potential, protein phosphorylation, reactive oxygen species, metabolic adaptation, signal transduction
- MeSH terms
- Kinetics, Membrane Lipids, Mitochondria, Models, Biological, Multienzyme Complexes, Oxidation-Reduction, Oxidative Phosphorylation, Ubiquinone, Cell Respiration, Mitochondrial Membranes
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