ArticleProceedings of the National Academy of Sciences of the United States of America2015
Dissecting the role of the γ-subunit in the rotary-chemical coupling and torque generation of F1-ATPase.
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 33 papers.
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Who cites it
33 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
- Electric Forces and ATP Synthesis.Reviews of physiology, biochemistry and pharmacology · 2025Review
- On the Control of Directionality of Myosin.Journal of the American Chemical Society · 2024Article
- Article
- Exploring the activation mechanism of metabotropic glutamate receptor 2.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Long-Time Dynamics of Selected Molecular-Motor Components Using a Physics-Based Coarse-Grained Approach.Biomolecules · 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
- Application of Coarse-Grained (CG) Models to Explore Conformational Pathway of Large-Scale Protein Machines.Entropy (Basel, Switzerland) · 2022Article
- FFrontiers in microbiology · 2022Review
- FFrontiers in microbiology · 2022Review
- Article
- The catalytic dwell in ATPases is not crucial for movement against applied torque.Nature chemistry · 2020Article
- The 3 × 120° rotary mechanism ofProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Rotary catalysis of bovine mitochondrial FProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Revisiting the protomotive vectorial motion of FProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Elastic coupling power stroke mechanism of the FProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in FBiophysical journal · 2018Article
- The FPhotosynthesis research · 2017Review
- Theory of long binding events in single-molecule-controlled rotation experiments on FProceedings of the National Academy of Sciences of the United States of America · 2017Article
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2 authors.
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Abstract
Unraveling the molecular nature of the conversion of chemical energy (ATP hydrolysis in the α/β-subunits) to mechanical energy and torque (rotation of the γ-subunit) in F1-ATPase is very challenging. A major part of the challenge involves understanding the rotary-chemical coupling by a nonphenomenological structure-energy description, while accounting for the observed torque generated on the γ-subunit and its change due to mutation of this unit. Here we extend our previous study that used a coarse-grained model of the F1-ATPase to generate a structure-based free energy landscape of the rotary-chemical process. Our quantitative analysis of the landscape reproduced the observed torque for the wild-type enzyme. In doing so, we found that there are several possibilities of torque generation from landscapes with various shapes and demonstrated that a downhill slope along the chemical coordinate could still result in negligible torque, due to ineffective coupling of the chemistry to the γ-subunit rotation. We then explored the relationship between the functionality and the underlying sequence through systematic examination of the effect of various parts of the γ-subunit on free energy surfaces of F1-ATPase. Furthermore, by constructing several types of γ-deletion systems and calculating the corresponding torque generation, we gained previously unknown insights into the molecular nature of the F1-ATPase rotary motor. Significantly, our results are in excellent agreement with recent experimental findings and indicate that the rotary-chemical coupling is primarily established through electrostatic effects, although specific contacts through γ-ionizable residue side chains are not essential for establishing the basic features of the coupling.
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