ArticleProceedings of the National Academy of Sciences of the United States of America2011
Electrostatic origin of the mechanochemical rotary mechanism and the catalytic dwell 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 60 papers.
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Who cites it
60 citing papers in PubMed.
- The distortion-push mechanism for the γ subunit rotation in FProceedings of the National Academy of Sciences of the United States of America · 2025Article
- The molecular mechanism of ATP synthase constrains the evolutionary landscape of chemiosmosis.Biophysical journal · 2025Review
- Physics-based modeling in the new era of enzyme engineering.Nature computational science · 2025Review
- On the Control of Directionality of Myosin.Journal of the American Chemical Society · 2024Article
- Article
- 2-Site versus 3-site models of ATP hydrolysis by FTheory in biosciences = Theorie in den Biowissenschaften · 2024Article
- Elucidating Events within the Black Box of Enzyme Catalysis in Energy Metabolism: Insights into the Molecular Mechanism of ATP Hydrolysis by FBiomolecules · 2023Article
- FBiophysical journal · 2023Article
- Modeling control and transduction of electrochemical gradients in acid-stressed bacteria.iScience · 2023Article
- Ordered-domain unfolding of thermophilic isolated β subunit ATP synthase.Protein science : a publication of the Protein Society · 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
- Physical pictures of rotation mechanisms of FFrontiers in molecular biosciences · 2023Article
- Beyond binding change: the molecular mechanism of ATP hydrolysis by FFrontiers in chemistry · 2023Article
- Application of Computational Biology and Artificial Intelligence in Drug Design.International journal of molecular sciences · 2022Review
- Application of Coarse-Grained (CG) Models to Explore Conformational Pathway of Large-Scale Protein Machines.Entropy (Basel, Switzerland) · 2022Article
- Rotational Mechanism of FFrontiers in microbiology · 2022Review
- FFrontiers in microbiology · 2022Review
- FFrontiers in microbiology · 2022Review
- Exploring the Activation Process of the β2AR-GJournal of the American Chemical Society · 2021Article
- Simulating the directional translocation of a substrate by the AAA+ motor in the 26S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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2 authors.
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Abstract
Understanding the nature of energy transduction in life processes requires a quantitative description of the energetics of the conversion of ATP to ADP by ATPases. Previous attempts to do so have provided an interesting insight but could not account for the rotary mechanism by a nonphenomenological structure/energy description. In particular it has been very challenging to account for the observations of the 80° and 40° rotational substates, without any prior information about such states in the simulation procedure. Here we use a coarse-grained model of F1-ATPase and generate, without the adjustment of phenomenological parameters, a structure-based free energy landscape that reproduces the energetics of the mechanochemical process. It is found that the landscape along the relevant rotary path is determined by the electrostatic free energy and not by steric effects. Furthermore, the generated surface and the corresponding Langevin dynamics simulations identify a hidden conformational barrier that provides a new fundamental interpretation of the catalytic dwell and illuminate the nature of the energy conversion process.
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