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Mitochondrial ATP synthase: architecture, function and pathology
Abstract
Human mitochondrial (mt) ATP synthase, or complex V consists of two functional domains: F 1 , situated in the mitochondrial matrix, and F o , located in the inner mitochondrial membrane. Complex V uses the energy created by the proton electrochemical gradient to phosphorylate ADP to ATP. This review covers the architecture, function and assembly of complex V. The role of complex V di‐and oligomerization and its relation with mitochondrial morphology is discussed. Finally, pathology related to complex V deficiency and current therapeutic strategies are highlighted. Despite the huge progress in this research field over the past decades, questions remain to be answered regarding the structure of subunits, the function of the rotary nanomotor at a molecular level, and the human complex V assembly process. The elucidation of more nuclear genetic defects will guide physio(patho)logical studies, paving the way for future therapeutic interventions.
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The F1Fo ATP synthase is the terminal complex in oxidative phosphorylation and converts the proton motive force generated by Complexes I, III and IV into ATP.
“The F1Fo ATP synthase is the terminal complex in the oxidative phosphorylation relay and is responsible for converting the proton motive force generated by Complexes I, III and IV into ATP.”
From Codon optimization is an essential parameter for the efficient allotopic expression of mtDNA genes (2020) · cites this paper as [84]
MT-ATP8 and MT-ATP6 are mtDNA-encoded subunits of ATP synthase, while the remaining subunits are nuclear-encoded.
“Two of the subunits of this multimeric complex are encoded by mtDNA, namely MT-ATP8 and MT-ATP6, whereas, the genes for the remaining subunits reside in the nucleus [84].”
From Codon optimization is an essential parameter for the efficient allotopic expression of mtDNA genes (2020) · cites this paper as [84]
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Metadata
- Authors
- Jonckheere, A. I., Smeitink, J. A. M., & Rodenburg, R. J. T.
- Affiliations
- Department of Pediatrics, Nijmegen Center for Mitochondrial Disorders, 656 Laboratory for Genetic, Endocrine, and Metabolic Disorders Radboud University Nijmegen Medical Center PO Box 9101 Nijmegen 6500 HB The Netherlands
- Venue
- Journal of Inherited Metabolic Disease
- Publisher
- Wiley
- Published
- 2011-08-27
- Volume
- 35
- Issue
- 2
- Pages
- 211-225
- ISSN
- 0141-8955
- 1573-2665
- PMC
- PMC3278611
- Cited by
- 605
- References
- 2
- Language
- en
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