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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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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 65
Therapeutic Efficacy of Molecular Hydrogen: A New Mechanistic Insight
Ishibashi, T. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666190506123038 · Cited by 60
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 55
“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 51
“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 55
“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 56
“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
Novack, G. V., Galeano, P., Castaño, E. M., & Morelli, L. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00600 · Cited by 52
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“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
“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 52
Kobayashi, A., Azuma, K., Ikeda, K., & Inoue, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186683 · Cited by 49
CoQ10 and Mitochondrial Dysfunction in Alzheimer’s Disease
Fišar, Z., & Hroudová, J. (2024) · Antioxidants · doi:10.3390/antiox13020191 · Cited by 57
“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
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“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
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 46
Disturbed Flow Induces Autophagy, but Impairs Autophagic Flux to Perturb Mitochondrial Homeostasis
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“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 46
The new role of F1Fo ATP synthase in mitochondria-mediated neurodegeneration and neuroprotection
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Distribution and dynamics of OXPHOS complexes in the bacterial cytoplasmic membrane
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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 45
“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. (2014) · The Plant Journal · doi:10.1111/tpj.12532 · Cited by 42
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 43
Azoles activate type I and type II programmed cell death pathways in crop pathogenic fungi
Schuster, M., Kilaru, S., & Steinberg, G. (2024) · Nature Communications · doi:10.1038/s41467-024-48157-9 · Cited by 44
“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 43
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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