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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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“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]
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“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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“[1] N,N’-bis(3-cyano-5,6-dihydro-4H-cyclopenta[b]thiophen-2-yl)nonanediamide 480.”
BackgroundRapid Electron Transfer within the III-IV Supercomplex in Corynebacterium glutamicum
Graf, S., Fedotovskaya, O. N., Kao, W., Hunte, C., Ädelroth, P., Bott, M. H., von Ballmoos, C., & Brzezinski, P. (2016) · Scientific Reports · doi:10.1038/srep34098 · Cited by 21
Chen, C., Yu, Q., Han, L., Zhang, J., & Guo, Z. (2018) · Animal Science Journal · doi:10.1111/asj.12993 · Cited by 21
Ogunbona, O. B., & Claypool, S. M. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00003 · Cited by 21
“, 2013) whose structures have since provided novel insight into the potential benefits that they may confer (Schäfer et al., 2007; Althoff et al., 2011; Dudkina et al., 2011; Genova and Lenaz, 2014; Gu et al., 2016; Letts et al., 2016; Wu et al., 2016).”
BackgroundKobayashi, A., Takeiwa, T., Ikeda, K., & Inoue, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119414 · Cited by 23
Different Functions of Phylogenetically Distinct Bacterial Complex I Isozymes
Spero, M. A., Brickner, J. R., Mollet, J. T., Pisithkul, T., Amador‐Noguez, D., & Donohue, T. J. (2016) · Journal of Bacteriology · doi:10.1128/jb.01025-15 · Cited by 19
Andjelković, A., Oliveira, M. T., Cannino, G., Yalgin, C., Dhandapani, P. K., Dufour, É., Rustin, P., Szibor, M., & Jacobs, H. T. (2015) · Scientific Reports · doi:10.1038/srep18295 · Cited by 20
“The limit could be dictated by the constraints of membrane architecture, for example, if much of the ubiquinone pool is channelled directly from complex I to complex III via respiratory supercomplexes, such that it equilibrates only slowly with free ubiquinones available to AOX 36 .”
Regulation of Cytochrome c Oxidase by Natural Compounds Resveratrol, (–)-Epicatechin, and Betaine
Lee, I. (2021) · Cells · doi:10.3390/cells10061346 · Cited by 20
“The significance of these supramolecular structures has been suggested to be functionally relevant to ETC activity by increasing the efficiency of NAD-linked respiration and by reducing ROS production [3].”
BackgroundCasuso, R. A., Fazazi, S. A., Hidalgo‐Gutiérrez, A., López, L. C., Plaza‐Díaz, J., Rueda‐Robles, A., & Huertas, J. R. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.01.027 · Cited by 20
Martínez-Bernabé, T., Sastre‐Serra, J., Ciobu, N., Oliver, J., Pons, D. G., & Roca, P. (2021) · Antioxidants · doi:10.3390/antiox10091371 · Cited by 20
“In the MCF7 cell line, where ERα predominates, the protein levels of the OXPHOS system are decreased after ELIT treatment, as well as the amount of inner mitochondrial membrane (cardiolipin levels), required for the activity of complexes I, III, and IV, and plays an important role in mitochondrial biogenesis [51,52].”
BackgroundHormone deprivation alters mitochondrial function and lipid profile in the hippocampus
Zárate, S., Astiz, M., Magnani, N., Imsen, M., Merino, F., Álvarez, S., Reinés, A. G., & Seilicovich, A. (2017) · Journal of Endocrinology · doi:10.1530/joe-16-0451 · Cited by 19
“507 Moreover, it has been reported that the stability of complex I is highly dependent on its assembly 508 within the respiratory supercomplex (Genova & Lenaz 2014).”
InfluentialThe 1.3-Å resolution structure of bovine cytochrome c oxidase suggests a dimerization mechanism
Shinzawa‐Itoh, K., Hatanaka, M., Fujita, K., Yano, N., Ogasawara, Y., Iwata, J., Yamashita, E., Tomitake Tsukihara, A., Yoshikawa, S., & Muramoto, K. (2021) · BBA Advances · doi:10.1016/j.bbadva.2021.100009 · Cited by 19
Influence of anaerobic and aerobic exercise on age-related pathways in skeletal muscle
Navas‐Enamorado, I., Bernier, M., Brea‐Calvo, G., & de Cabo, R. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.04.005 · Cited by 21
“energy dependent tissues like skeletal muscle (Genova and Lenaz, 2014).”
BackgroundMcCullough, D. J., Kue, N. R., Mancini, T. J., Vang, A., Clements, R., & Choudhary, G. (2020) · Pulmonary Circulation · doi:10.1177/2045894020925762 · Cited by 17
“Mitochondrial SCs are dynamic assemblies of individual ETC complexes consisting of complex I and varying copies of complexes III and IV in physical association to form discrete functional respiratory units.(17) SCs are thought to provide more efficient respiration which should be capable of improving mitochondrial fun…”
BackgroundThe Interplay between Dysregulated Metabolism and Epigenetics in Cancer
Bassal, M. A. (2023) · Biomolecules · doi:10.3390/biom13060944 · Cited by 19
Coi1 is a novel assembly factor of the yeast complex III–complex IV supercomplex
Singhal, R. K., Kruse, C., Heidler, J., Strecker, V., Zwicker, K., Düsterwald, L., Westermann, B., Herrmann, J. M., Wittig, I., & Rapaport, D. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-02-0093 · Cited by 18
“The composition of the various supercomplexes might change depending on cell types and their physiological needs (Genova and Lenaz, 2014; Greggio et al., 2017).”
Fišar, Z., Hroudová, J., Singh, N., Kopřivová, A., & Maceckova, D. (2016) · Folia Biologica · doi:10.14712/fb2016062020053 · Cited by 18
“The respiratory complexes are thought to be both in their free enzyme forms and associated in supercomplexes within the inner mito chondrial membrane (Genova and Lenaz, 2014).”
BackgroundGoswami, D., Ghosh, S., Dutta, R., Ghatak, D., Ranjit, D., & De, R. (2025) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-025-01857-5 · Cited by 18
Cardiolipin alterations and mitochondrial dysfunction in heart ischemia/reperfusion injury
Paradies, G., Paradies, V., Ruggiero, F. M., & Petrosillo, G. (2015) · Clinical Lipidology · doi:10.2217/clp.15.31 · Cited by 18
Miranda‐Astudillo, H., Colina-Tenorio, L., Jiménez-Suárez, A., Vázquez‐Acevedo, M., Salin, B., Giraud, M., Remacle, C., Cardol, P., & González‐Halphen, D. (2018) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.03.004 · Cited by 17
Asencio, C., Hernández, M., Briones, P., Montoya, J., Cortés, A., Emperador, S., Gavilán, Á., Ruiz‐Pesini, E., Yubero, D., Montero, R., et al. (2015) · European Journal of Human Genetics · doi:10.1038/ejhg.2015.112 · Cited by 16
Kuter, K. Z., Olech, Ł., & Dencher, N. A. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.12.002 · Cited by 16
Clarke, C. F., Rowat, A. C., & Gober, J. W. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1478 · Cited by 16
Ferguson, M. A., Sutton, R. M., Karlsson, M., Sjövall, F., Becker, L. B., Berg, R. A., Margulies, S. S., & Kilbaugh, T. J. (2016) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-016-9657-9 · Cited by 16
Haroon, S., Yoon, H., Seiler, C., Osei-Frimpong, B., He, J., Nair, R. M., Mathew, N. D., Burg, L., Köse, M., Venkata, C. R. M., et al. (2023) · Human Molecular Genetics · doi:10.1093/hmg/ddad031 · Cited by 15
Dudkina, N. V., Folea, I. M., & Boekema, E. J. (2015) · Micron · doi:10.1016/j.micron.2015.03.002 · Cited by 16
Tempelhagen, L., Ayer, A., Culham, D. E., Stocker, R., & Wood, J. M. (2020) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)49909-1 · Cited by 15
Kuter, K. Z., Kratochwil, M., Marx, S.-H., Hartwig, S., Lehr, S., Sugawa, M. D., & Dencher, N. A. (2016) · Archives of Physiology and Biochemistry · doi:10.1080/13813455.2016.1197948 · Cited by 15
“…in process of dopaminergic neurons degeneration Higher organisation of mitochondrial OxPhos Cxs into SCxs improves effectiveness of particular Cxs (Genova & Lenaz, 2014; Maranzana et al., 2013; Schäfer et al., 2006; Schon & Dencher, 2009) and our previous studies corroborated it, with individual…”
BackgroundResultBeutner, G., & Porter, G. A. (2017) · Journal of Visualized Experiments · doi:10.3791/55738 · Cited by 16
Goyani, S., Shinde, A., Shukla, S., Saranga, M. V., Currim, F., Mane, M., Singh, J., Roy, M., Gohel, D., Chandak, N., et al. (2024) · FEBS Journal · doi:10.1111/febs.17065 · Cited by 14
“These individual complexes assemble to form super-complexes or respirasomes, which maintain flux of electrons through OXPHOS and determine functional capacity of mitochondria [58].”
BackgroundTargeting Mitochondrial Dysfunction in Cerebral Ischemia: Advances in Pharmacological Interventions
Belenichev, I. F., Popazova, O., Bukhtiyarova, N. V., Ryzhenko, V. P., Pavlov, S. V., Suprun, E. V., Oksenych, V., & Kamyshnyi, O. (2025) · Antioxidants · doi:10.3390/antiox14010108 · Cited by 25
Peloso, E. D. F., Dias, L., Queiroz, R. M. L., Leme, A. F. P., Pereira, C. N., Carnielli, C. M., WERNECK, C. C., de Sousa, M. V., Ricart, C. A. O., & Gadelha, F. R. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.10.005 · Cited by 14
Bacterial Electron Transfer Chains Primed by Proteomics
Wessels, H. J. C. T., de Almeida, N. M., Kartal, B., & Keltjens, J. T. (2016) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2016.02.006 · Cited by 14
Kahl, A., Anderson, C. J., Qian, L., Voss, H. U., Manfredi, G., Iadecola, C., & Zhou, P. (2017) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x17720371 · Cited by 14
“Recently, the classical paradigm of mitochondrial respiratory chain complexes acting as individual functional entities in the inner mitochondrial membrane has been complemented by a dynamic supramolecular interaction model.(55,56) In this solid structural organization model, mitochondrial respiratory complexes associa…”
BackgroundChapa‐Dubocq, X. R., Rodríguez‐Graciani, K. M., Guzman‐Hernandez, R. A., Jang, S., Brookes, P. S., & Javadov, S. A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051555 · Cited by 14
“On the contrary, a study using flux control analysis found evidence that respirasome does provide a kinetic advantage in electron channeling [41,42].”
BackgroundDrummond, F. R., Leite, L. B., de Miranda, D. C., Drummond, L. R., Lavorato, V. N., Soares, L. L., Neves, C. A., & Natali, A. J. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1148146 · Cited by 13
“Mitochondrial supercomplexes are dynamic sets of individual complexes in the electron transport chain that can lead to more efficient respiration (Genova and Lenaz, 2014).”
Background
Metadata
- 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
- 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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