Energy transduction in the F1 motor of ATP synthase
Abstract
ATP synthase is the universal enzyme that manufactures ATP from ADP and phosphate by using the energy derived from a transmembrane protonmotive gradient. It can also reverse itself and hydrolyse ATP to pump protons against an electrochemical gradient. ATP synthase carries out both its synthetic and hydrolytic cycles by a rotary mechanism. This has been confirmed in the direction of hydrolysis after isolation of the soluble F1 portion of the protein and visualization of the actual rotation of the central 'shaft' of the enzyme with respect to the rest of the molecule, making ATP synthase the world's smallest rotary engine. Here we present a model for this engine that accounts for its mechanochemical behaviour in both the hydrolysing and synthesizing directions. We conclude that the F1 motor achieves its high mechanical torque and almost 100% efficiency because it converts the free energy of ATP binding into elastic strain, which is then released by a coordinated kinetic and tightly coupled conformational mechanism to create a rotary torque.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The F1 ATPase uses its beta-sheet as a spring to store energy from ATP, and then rapidly releases it to create high-speed rotary torque of about 100 Hz.
“For example, the F1 ATPase (the smallest rotary motor) uses its beta-sheet as a spring to store energy from ATP, and then rapidly releases it to create the high-speed rotary torque ( ~100 Hz)91.”
From Membrane compression by synaptic vesicle exocytosis triggers ultrafast endocytosis (2023) · cites this paper as [91]
Cited by
Sorted by citations
A structural change in the kinesin motor protein that drives motility
Rice, S., Lin, A. W., Safer, D., Hart, C. L., Naber, N., Carragher, B. O., Cain, S. M., Pechatnikova, E., Wilson-Kubalek, E. M., Whittaker, M., et al. (1999) · Nature · doi:10.1038/45483 · Cited by 798 · see citing works
Multiscale Modeling of Biological Functions: From Enzymes to Molecular Machines (Nobel Lecture)
Warshel, A. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201403689 · Cited by 245 · see citing works
“[63, 64]), the origin of the coupling between chemical and mechanical events in the F1F0ATPsynthase has not been elucidated or simulated in a consistent and unbiased way.”
BackgroundMembrane compression by synaptic vesicle exocytosis triggers ultrafast endocytosis
Ogunmowo, T. H., Jing, H., Raychaudhuri, S., Kusick, G. F., Imoto, Y., Li, S., Itoh, K., Ma, Y., Jafri, H., Dalva, M. B., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38595-2 · Cited by 51 · see citing works
“In a broader biological context, similar mechanical systems have been demonstrated at the molecular level:Forexample, the F1 ATPase(thesmallest rotary motor) uses its beta-sheet as a spring to store energy from ATP, and then rapidly releases it to create the high-speed rotary torque (~100Hz) 91 .”
- Authors
- Wang, H., & Oster, G.
- Affiliations
- University of California, Berkeley (US)
- Corresponding author
- Oster, George
- ORCID
- Wang, Hongyun
- Venue
- Nature
- Published
- 1998-11
- Volume
- 396
- Issue
- 6708
- Pages
- 279-282
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1893057187
- Cited by
- 440
- References
- 0
- Citations by year
- 2026: 4 · 2025: 10 · 2024: 4 · 2023: 4 · 2022: 12 · 2021: 9 · 2020: 8 · 2019: 8 · 2018: 12 · 2017: 14 · 2016: 13 · 2015: 14 · 2014: 16 · 2013: 23 · 2012: 23
- FWCI
- 6.86
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (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 › Protein Structure and Dynamics
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
- Keywords
- ATP synthase, energy transduction, rotary mechanism, proton motive force, ATP hydrolysis, ATP production, mechanochemistry, elastic strain, conformational coupling, torque, enzyme catalytic efficiency
- MeSH terms
- Adenosine Triphosphate, Biomechanical Phenomena, Elasticity, Energy Metabolism, Proton-Translocating ATPases, Hydrolysis, Models, Chemical, Models, Molecular, Protein Conformation, Thermodynamics, Catalytic Domain, Molecular Motor Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
