The ATP synthase: the understood, the uncertain and the unknown
Abstract
The ATP synthases are multiprotein complexes found in the energy-transducing membranes of bacteria, chloroplasts and mitochondria. They employ a transmembrane protonmotive force, Δp, as a source of energy to drive a mechanical rotary mechanism that leads to the chemical synthesis of ATP from ADP and Pi. Their overall architecture, organization and mechanistic principles are mostly well established, but other features are less well understood. For example, ATP synthases from bacteria, mitochondria and chloroplasts differ in the mechanisms of regulation of their activity, and the molecular bases of these different mechanisms and their physiological roles are only just beginning to emerge. Another crucial feature lacking a molecular description is how rotation driven by Δp is generated, and how rotation transmits energy into the catalytic sites of the enzyme to produce the stepping action during rotation. One surprising and incompletely explained deduction based on the symmetries of c-rings in the rotor of the enzyme is that the amount of energy required by the ATP synthase to make an ATP molecule does not have a universal value. ATP synthases from multicellular organisms require the least energy, whereas the energy required to make an ATP molecule in unicellular organisms and chloroplasts is higher, and a range of values has been calculated. Finally, evidence is growing for other roles of ATP synthases in the inner membranes of mitochondria. Here the enzymes form supermolecular complexes, possibly with specific lipids, and these complexes probably contribute to, or even determine, the formation of the cristae.
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There are only two basic ways that cells conserve energy as high energy phosphate bonds: substrate level phosphorylation and chemiosmotic energy harnessing using a rotor-stator ATP synthase.
“There are only two basic ways that cells conserve energy as high energy phosphate bonds: substrate level phosphorylation (Decker et al., 1970) and chemiosmotic energy harnessing using a rotor-stator ATP synthase (Walker et al., 1982; Walker, 2013).”
From Serpentinization as the source of energy, electrons, organics, catalysts, nutrients and pH gradients for the origin of LUCA and life (2023) · cites this paper as Walker, 2013
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Self-citationAssociation of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria
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Self-citationSu e of the Yeast F1Fo-ATP Synthase Forms Homodimers
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Self-citationATP Synthase that Lacks F0a-Subunit
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ATP Synthesis by Rotary Catalysis (Nobel lecture)
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Self-citationVDAC Regulation: A Mitochondrial Target to Stop Cell Proliferation
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- Authors
- Walker, J. E.
- Affiliations
- MRC Mitochondrial Biology Unit (GB)
- Corresponding author
- Walker, John E.
- ORCID
- Walker, John E.
- Venue
- Biochemical Society Transactions
- Publisher
- Portland Press Ltd.
- Published
- 2013-01-29
- Volume
- 41
- Issue
- 1
- Pages
- 1-16
- ISSN
- 0300-5127 (ISSN-L)
- 1470-8752
- OpenAlex
- W2104675030
- Cited by
- 614
- References
- 123
- Citations by year
- 2026: 39 · 2025: 44 · 2024: 48 · 2023: 39 · 2022: 47 · 2021: 56 · 2020: 61 · 2019: 46 · 2018: 52 · 2017: 42 · 2016: 42 · 2015: 54 · 2014: 30 · 2013: 13 · 2012: 1
- FWCI
- 4.36
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Society Transactions (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- ATP synthase, proton motive force, rotary mechanism, ATP production, enzyme regulation, mitochondrial ATP synthase, chloroplast ATP synthase, bacterial ATP synthase, supramolecular complexes
- MeSH terms
- Hydrolysis, Models, Molecular, Protein Conformation, ATP Synthetase Complexes, Uncertainty
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