ArticleProceedings of the National Academy of Sciences of the United States of America2011
Thermodynamic efficiency and mechanochemical coupling of F1-ATPase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 176 citations in OpenAlex.
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- The molecular mechanism of ATP synthase constrains the evolutionary landscape of chemiosmosis.Biophysical journal · 2025Review
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- Simultaneous application of enzyme and thermodynamic constraints to metabolic models using an updated Python implementation of GECKO.Microbiology spectrum · 2023Article
- Mechanochemical active ratchet.Scientific reports · 2023Article
- Electromagnetic Forces and Torques: From Dielectrophoresis to Optical Tweezers.Chemical reviews · 2023Review
- Physical pictures of rotation mechanisms of FFrontiers in molecular biosciences · 2023Article
- Controlling dynamics in extended molecular frameworks.Nature reviews. Chemistry · 2022Review
- Modulation of the HFrontiers in molecular biosciences · 2022Review
- How Does FFrontiers in microbiology · 2022Review
- Physical bioenergetics: Energy fluxes, budgets, and constraints in cells.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Cooperative stator assembly of bacterial flagellar motor mediated by rotation.Nature communications · 2021Article
- Reversible catalysis.Nature reviews. Chemistry · 2021Review
- Tight Chemomechanical Coupling of the FBiophysical journal · 2020Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
F(1)-ATPase is a nanosized biological energy transducer working as part of F(o)F(1)-ATP synthase. Its rotary machinery transduces energy between chemical free energy and mechanical work and plays a central role in the cellular energy transduction by synthesizing most ATP in virtually all organisms. However, information about its energetics is limited compared to that of the reaction scheme. Actually, fundamental questions such as how efficiently F(1)-ATPase transduces free energy remain unanswered. Here, we demonstrated reversible rotations of isolated F(1)-ATPase in discrete 120° steps by precisely controlling both the external torque and the chemical potential of ATP hydrolysis as a model system of F(o)F(1)-ATP synthase. We found that the maximum work performed by F(1)-ATPase per 120° step is nearly equal to the thermodynamical maximum work that can be extracted from a single ATP hydrolysis under a broad range of conditions. Our results suggested a 100% free-energy transduction efficiency and a tight mechanochemical coupling of F(1)-ATPase.
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