ArticleProceedings of the National Academy of Sciences of the United States of America2015
Simple mechanism whereby the F1-ATPase motor rotates with near-perfect chemomechanical energy conversion.
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 18 papers.
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Who cites it
18 citing papers in PubMed.
- The lower γ region supports forward rotation in the latter half of the 80° substep of FProtein science : a publication of the Protein Society · 2026Article
- Development of electromagnetic tweezers for single-molecule energetics of kinesin.Biophysics and physicobiology · 2026Article
- Functional and structural characterization of FProtein science : a publication of the Protein Society · 2025Article
- The molecular mechanism of ATP synthase constrains the evolutionary landscape of chemiosmosis.Biophysical journal · 2025Review
- Mechanism of ATP hydrolysis dependent rotation of bacterial ATP synthase.Nature communications · 2023Article
- Rotary mechanism of V/A-ATPases-how is ATP hydrolysis converted into a mechanical step rotation in rotary ATPases?Frontiers in molecular biosciences · 2023Review
- FFrontiers in microbiology · 2022Review
- ATPase-based implementation of enforced ATP wasting in Saccharomyces cerevisiae for improved ethanol production.Biotechnology for biofuels · 2020Article
- Tight Chemomechanical Coupling of the FBiophysical journal · 2020Article
- Method to extract multiple states in FProceedings of the National Academy of Sciences of the United States of America · 2019Article
- 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
- 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 Role of Mitochondrial HFrontiers in oncology · 2018Review
- Regulation of the HCellular and molecular life sciences : CMLS · 2017Review
- Perfect chemomechanical coupling of FProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Catalytic robustness and torque generation of the FBiophysical reviews · 2017Review
- Thermodynamics and kinetics of the FoF1-ATPase: application of the probability isotherm.Royal Society open science · 2016Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
F1-ATPase is a motor enzyme in which a central shaft γ subunit rotates 120° per ATP in the cylinder made of α3β3 subunits. During rotation, the chemical energy of ATP hydrolysis (ΔGATP) is converted almost entirely into mechanical work by an elusive mechanism. We measured the force for rotation (torque) under various ΔGATP conditions as a function of rotation angles of the γ subunit with quasi-static, single-molecule manipulation and estimated mechanical work (torque × traveled angle) from the area of the function. The torque functions show three sawtooth-like repeats of a steep jump and linear descent in one catalytic turnover, indicating a simple physical model in which the motor is driven by three springs aligned along a 120° rotation angle. Although the second spring is unaffected by ΔGATP, activation of the first spring (timing of the torque jump) delays at low [ATP] (or high [ADP]) and activation of the third spring delays at high [Pi]. These shifts decrease the size and area of the sawtooth (magnitude of the work). Thus, F1-ATPase responds to the change of ΔGATP by shifting the torque jump timing and uses ΔGATP for the mechanical work with near-perfect efficiency.
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