ArticleBiophysical journal2014
Nonequilibrium dissipation-free transport in F₁-ATPase and the thermodynamic role of asymmetric allosterism.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Experimentally achieving minimal dissipation via thermodynamically optimal transport.Nature communications · 2025Article
- Tight Chemomechanical Coupling of the FBiophysical journal · 2020Article
- Efficiencies of molecular motors: a comprehensible overview.Biophysical reviews · 2020Review
- Fluctuation-response inequality out of equilibrium.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Simple mechanics of protein machines.Journal of the Royal Society, Interface · 2019Article
- Elastic coupling power stroke mechanism of the FProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Deciphering Intrinsic Inter-subunit Couplings that Lead to Sequential Hydrolysis of FBiophysical journal · 2017Article
- F1 rotary motor of ATP synthase is driven by the torsionally-asymmetric drive shaft.Scientific reports · 2016Article
- Thermodynamics and kinetics of the FoF1-ATPase: application of the probability isotherm.Royal Society open science · 2016Article
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Authors and funding
3 authors.
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Abstract
F1-ATPase (or F1), the highly efficient and reversible biochemical engine, has motivated physicists as well as biologists to imagine the design principles governing machines in the fluctuating world. Recent experiments have clarified yet another interesting property of F1; the dissipative heat inside the motor is very small, irrespective of the velocity of rotation and energy transport. Conceptual interest is devoted to the fact that the amount of internal dissipation is not simply determined by the sequence of equilibrium pictures, but also relies on the rotational-angular dependence of nucleotide affinity, which is a truly nonequilibrium aspect. We propose that the totally asymmetric allosteric model (TASAM), where adenosine triphosphate (ATP) binding to F1 is assumed to have low dependence on the angle of the rotating shaft, produces results that are most consistent with the experiments. Theoretical analysis proves the crucial role of two time scales in the model, which explains the universal mechanism to produce the internal dissipation-free feature. The model reproduces the characteristic torque dependence of the rotational velocity of F1 and predicts that the internal dissipation upon the ATP synthesis direction rotation becomes large at the low nucleotide condition.
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