ID | 57456 |
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Sumi, Tomonari
Research Institute for Interdisciplinary Science, Department of Chemistry, Faculty of Science, Okayama University
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Klumpp, Stefan
Department Theory and Bio-Systems, Max Planck Institute of Colloids and Interfaces
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Abstract | We present a chemomechanical network model of the rotary molecular motor F1-ATPase which quantitatively describes not only the rotary motor dynamics driven by ATP hydrolysis but also the ATP synthesis caused by forced reverse rotations. We observe a high reversibility of F1-ATPase, that is, the main cycle of ATP synthesis corresponds to the reversal of the main cycle in the hydrolysis-driven motor rotation. However, our quantitative analysis indicates that torque-induced mechanical slip without chemomechanical coupling occurs under high external torque and reduces the maximal efficiency of the free energy transduction to 40–80% below the optimal efficiency. Heat irreversibly dissipates not only through the viscous friction of the probe but also directly from the motor due to torque-induced mechanical slip. Such irreversible heat dissipation is a crucial limitation for achieving a 100% free-energy transduction efficiency with biological nanomachines because biomolecules are easily deformed by external torque.
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Keywords | F-1-ATPase
rotary molecular motor
chemomechanical network model
free-energy transduction efficiency
ATP synthesis
torque-induced mechanical slip
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Published Date | 2019-04-24
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Publication Title |
Nano Letters
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Volume | volume19
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Issue | issue5
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Publisher | American Chemical Society
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Start Page | 3370
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End Page | 3378
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ISSN | 15306984
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NCID | AA11511812
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Content Type |
Journal Article
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language |
English
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OAI-PMH Set |
岡山大学
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Copyright Holders | Copyright © 2019 American Chemical Society
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File Version | author
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Related Url | isVersionOf https://doi.org/10.1021/acs.nanolett.9b01181
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Funder Name |
Japan Society for the Promotion of Science
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助成番号 | 18KK0151 : Understanding solvent-mediated forces with diverse responses to ions, co-solvents, and temperature
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