The DOI matches its Crossref record; 187 of the 187 references it cites were found in a registry or an index.
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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Cites
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Cardiolipin Stabilizes Respiratory Chain Supercomplexes
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Placental powerhouses: Links between physical activity, tissue location and mitochondrial properties
O’Rourke, N., Everest, C., Rankin, J., Cuillerier, A., Cairns, G., Burelle, Y., Dantas, A. E., & Adamo, K. B. (2026) · Advanced Exercise and Health Science · doi:10.1016/j.aehs.2026.04.002
Pang, Y., Li, N., Ding, Y., Hou, S., Liu, J. J., Liu, X., Liu, E., & Chen, X. (2026) · Animal Models and Experimental Medicine · doi:10.1002/ame2.70241
“24 At the same time, a large accumulation of ROS also accelerates autophagy and the degeneration of skeletal muscles, 25,26 growth.”
Azarkina, N. V., Orlov, V. N., Muntyan, M. S., Chesnokov, Y. M., Nesterov, S. V., Oleynikov, I. P., & Vygodina, T. V. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27198744
Manutlak, R., Gill, S. K., Rossi, G. S., & Little, A. G. (2026) · Journal of Experimental Biology · doi:10.1242/jeb.252349
Ma, W., Owusu-Sarfo, J., Zhang, Z., Silvia, S. M., Cordeiro, B., Bazinet, L. F., Mancini, T. J., Aguocha, B. C., Aboulgheit, A., O-Uchi, J., et al. (2026) · Antioxidants · doi:10.3390/antiox15101366
“…regulation of mitochondrial volume may modulate mitochondrial structure to promote and/or preserve mitochondrial electron transport chain supercomplexes (mSCs). mSCs consist of ETC CI, III and IV in physical association and are thought to improve mitochondrial respiratory efficiency [23,24].”
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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