ArticleProceedings of the National Academy of Sciences of the United States of America2015
Elasticity, friction, and pathway of γ-subunit rotation in FoF1-ATP synthase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Decoding the Hot-Mitochondrion Paradox.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- The distortion-push mechanism for the γ subunit rotation in FProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- The ATPase asymmetry: Novel computational insight into coupling diverse FBiophysical journal · 2025Article
- Conformational ensemble of yeast ATP synthase at low pH reveals unique intermediates and plasticity in FNature structural & molecular biology · 2024Article
- Mechanism of proton-powered c-ring rotation in a mitochondrial ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- FBiophysical journal · 2023Article
- Molecular mechanism and energetics of coupling between substrate binding and product release in the FProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Changes within the central stalk of E. coli FCommunications biology · 2023Article
- Rotational Mechanism of FFrontiers in microbiology · 2022Review
- Molecular dynamics simulation of proton-transfer coupled rotations in ATP synthase FScientific reports · 2020Article
- Biophysical research in Okazaki, Japan.Biophysical reviews · 2020Review
- Insights into the origin of the high energy-conversion efficiency of FProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Mechanism of the electroneutral sodium/proton antiporter PaNhaP from transition-path shooting.Nature communications · 2019Article
- Structure of a bacterial ATP synthase.eLife · 2019Article
- The regulatory subunit ε in Escherichia coli FBiochimica et biophysica acta. Bioenergetics · 2018Review
- Structure, mechanism, and regulation of the chloroplast ATP synthase.Science (New York, N.Y.) · 2018Article
- Deciphering Intrinsic Inter-subunit Couplings that Lead to Sequential Hydrolysis of FBiophysical journal · 2017Article
- Methodology for the Simulation of Molecular Motors at Different Scales.The journal of physical chemistry. B · 2017Article
- Catalytic robustness and torque generation of the FBiophysical reviews · 2017Review
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2 authors.
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Abstract
We combine molecular simulations and mechanical modeling to explore the mechanism of energy conversion in the coupled rotary motors of FoF1-ATP synthase. A torsional viscoelastic model with frictional dissipation quantitatively reproduces the dynamics and energetics seen in atomistic molecular dynamics simulations of torque-driven γ-subunit rotation in the F1-ATPase rotary motor. The torsional elastic coefficients determined from the simulations agree with results from independent single-molecule experiments probing different segments of the γ-subunit, which resolves a long-lasting controversy. At steady rotational speeds of ∼ 1 kHz corresponding to experimental turnover, the calculated frictional dissipation of less than k(B)T per rotation is consistent with the high thermodynamic efficiency of the fully reversible motor. Without load, the maximum rotational speed during transitions between dwells is reached at ∼ 1 MHz. Energetic constraints dictate a unique pathway for the coupled rotations of the Fo and F1 rotary motors in ATP synthase, and explain the need for the finer stepping of the F1 motor in the mammalian system, as seen in recent experiments. Compensating for incommensurate eightfold and threefold rotational symmetries in Fo and F1, respectively, a significant fraction of the external mechanical work is transiently stored as elastic energy in the γ-subunit. The general framework developed here should be applicable to other molecular machines.
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