Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria
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The catalytic domain of the F-ATPase in mitochondria protrudes into the matrix of the organelle, and is attached to the membrane domain by central and peripheral stalks. Energy for the synthesis of ATP from ADP and phosphate is provided by the transmembrane proton-motive-force across the inner membrane, generated by respiration. The proton-motive force is coupled mechanically to ATP synthesis by the rotation at about 100 times per second of the central stalk and an attached ring of c-subunits in the membrane domain. Each c-subunit carries a glutamate exposed around the midpoint of the membrane on the external surface of the ring. The rotation is generated by protonation and deprotonation successively of each glutamate. Each 360° rotation produces three ATP molecules, and requires the translocation of one proton per glutamate by each c-subunit in the ring. In fungi, eubacteria, and plant chloroplasts, ring sizes of c 10 –c 15 subunits have been observed, implying that these enzymes need 3.3–5 protons to make each ATP, but until now no higher eukaryote has been examined. As shown here in the structure of the bovine F 1 -c-ring complex, the c-ring has eight c-subunits. As the sequences of c-subunits are identical throughout almost all vertebrates and are highly conserved in invertebrates, their F-ATPases probably contain c 8 -rings also. Therefore, in about 50,000 vertebrate species, and probably in many or all of the two million invertebrate species, 2.7 protons are required by the F-ATPase to make each ATP molecule.
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Oxidative phosphorylation is the largest source of cellular ATP.
“Whereas oxidative phosphorylation is the largest source of cellular ATP, the potential energy generated by the ETC is also harnessed for biosynthetic purposes.”
From The multifaceted contributions of mitochondria to cellular metabolism (2018) · cites this paper as [8]
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- Authors
- Watt, I. N., Montgomery, M. G., Runswick, M. J., Leslie, A. G. W., & Walker, J. E.
- Affiliations
- MRC Mitochondrial Biology Unit (GB)
- MRC Laboratory of Molecular Biology (GB)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2010-09-16
- Volume
- 107
- Issue
- 39
- Pages
- 16823-16827
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2947889
- OpenAlex
- W2052618584
- Cited by
- 513
- References
- 31
- Citations by year
- 2026: 14 · 2025: 24 · 2024: 23 · 2023: 24 · 2022: 37 · 2021: 32 · 2020: 46 · 2019: 29 · 2018: 29 · 2017: 33 · 2016: 30 · 2015: 43 · 2014: 29 · 2013: 46 · 2012: 41
- FWCI
- 15.62
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DORA PSI (Paul Scherrer Institute) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- F-ATPase, mitochondrial ATP synthase, bioenergetics, ATP production, proton motive force, C ring, subunit c, proton translocation, proton stoichiometry, mitochondrial respiration
- MeSH terms
- Adenosine Diphosphate, Adenosine Triphosphate, Amino Acid Sequence, Animals, Catalysis, Cattle, Energy Metabolism, Proton-Translocating ATPases, Mitochondria, Molecular Sequence Data, Catalytic Domain
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