ArticleScientific reports2016
F1 rotary motor of ATP synthase is driven by the torsionally-asymmetric drive shaft.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
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- Living Cell as a Self-Synchronized Chemical Reactor.The journal of physical chemistry letters · 2024Review
- Directed proton transfer from FBiophysical reviews · 2023Review
- Accounts of applied molecular rotors and rotary motors: recent advances.Nanoscale advances · 2023Review
- Generalized Solutions of Parrondo's Games.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020Article
- Natural products and other inhibitors of FEuropean journal of medicinal chemistry · 2020Review
- FliIScientific reports · 2020Article
- 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
- Dynamical regimes and stability of circular granular ratchets.Scientific reports · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
F1F0 ATP synthase (ATPase) either facilitates the synthesis of ATP in a process driven by the proton moving force (pmf), or uses the energy from ATP hydrolysis to pump protons against the concentration gradient across the membrane. ATPase is composed of two rotary motors, F0 and F1, which compete for control of their shared γ -shaft. We present a self-consistent physical model of F1 motor as a simplified two-state Brownian ratchet using the asymmetry of torsional elastic energy of the coiled-coil γ -shaft. This stochastic model unifies the physical concepts of linear and rotary motors, and explains the stepped unidirectional rotary motion. Substituting the model parameters, all independently known from recent experiments, our model quantitatively reproduces the ATPase operation, e.g. the 'no-load' angular velocity is ca. 400 rad/s anticlockwise at 4 mM ATP. Increasing the pmf torque exerted by F0 can slow, stop and overcome the torque generated by F1, switching from ATP hydrolysis to synthesis at a very low value of 'stall torque'. We discuss the motor efficiency, which is very low if calculated from the useful mechanical work it produces - but is quite high when the 'useful outcome' is measured in the number of H(+) pushed against the chemical gradient.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.