ArticleProceedings of the National Academy of Sciences of the United States of America2011
Torsional elasticity and energetics 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 26 papers.
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Who cites it
26 citing papers in PubMed.
- A minimal chemo-mechanical Markov model for rotary catalysis of FNature communications · 2026Article
- The distortion-push mechanism for the γ subunit rotation in FProceedings of the National Academy of Sciences of the United States of America · 2025Article
- 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
- 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
- FFrontiers in microbiology · 2022Review
- 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
- Interaction between γC87 and γR242 residues participates in energy coupling between catalysis and proton translocation in Escherichia coli ATP synthase.Biochimica et biophysica acta. Bioenergetics · 2019Article
- The regulatory subunit ε in Escherichia coli FBiochimica et biophysica acta. Bioenergetics · 2018Review
- Elastic coupling power stroke mechanism of the FProceedings of the National Academy of Sciences of the United States of America · 2018Article
- The FPhotosynthesis research · 2017Review
- Methodology for the Simulation of Molecular Motors at Different Scales.The journal of physical chemistry. B · 2017Article
- Chemomechanical Coupling in Hexameric Protein-Protein Interfaces Harnesses Energy within V-Type ATPases.Journal of the American Chemical Society · 2017Article
- Biophysical comparison of ATP synthesis mechanisms shows a kinetic advantage for the rotary process.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- F1 rotary motor of ATP synthase is driven by the torsionally-asymmetric drive shaft.Scientific reports · 2016Article
- The Phylogenetic Signature Underlying ATP Synthase c-Ring Compliance.Biophysical journal · 2015Article
- Elasticity, friction, and pathway of γ-subunit rotation in FoF1-ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Simple mechanism whereby the F1-ATPase motor rotates with near-perfect chemomechanical energy conversion.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Recent advances in QM/MM free energy calculations using reference potentials.Biochimica et biophysica acta · 2015Review
- Dissecting the role of the γ-subunit in the rotary-chemical coupling and torque generation of F1-ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Elastic properties and heterogeneous stiffness of the phi29 motor connector channel.Biophysical journal · 2014Article
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2 authors.
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No grant is acknowledged in the PubMed record.
Abstract
F(o)F(1)-ATPase is a rotary motor protein synthesizing ATP from ADP driven by a cross-membrane proton gradient. The proton flow through the membrane-embedded F(o) generates the rotary torque that drives the rotation of the asymmetric shaft of F(1). Mechanical energy of the rotating shaft is used by the F(1) catalytic subunit to synthesize ATP. It was suggested that elastic power transmission with transient storage of energy in some compliant part of the shaft is required for the observed high turnover rate. We used atomistic simulations to study the spatial distribution and structural determinants of the F(1) torsional elasticity at the molecular level and to comprehensively characterize the elastic properties of F(1)-ATPase. Our fluctuation analysis revealed an unexpected heterogeneity of the F(1) shaft elasticity. Further, we found that the measured overall torsional moduli of the shaft arise from two distinct contributions, the intrinsic elasticity and the effective potential imposed on the shaft by the catalytic subunit. Separation of these two contributions provided a quantitative description of the coupling between the rotor and the catalytic subunit. This description enabled us to propose a minimal quantitative model of the F(1) energetics along the rotary degrees of freedom near the resting state observed in the crystal structures. As opposed to the usually employed models where the motor mechanical progression is described by a single angular variable, our multidimensional treatment incorporates the spatially inhomogeneous nature of the shaft and its interactions with the stator and offers new insight into the mechanoenzymatics of F(1)-ATPase.
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