ArticlePloS one2013
Electric field driven torque in ATP synthase.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Decoding the Hot-Mitochondrion Paradox.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Fitness difference between two synonymous mutations of Phytophthora infestans ATP6 gene.BMC ecology and evolution · 2024Article
- Directed proton transfer from FBiophysical reviews · 2023Review
- Bacterial F-type ATP synthases follow a well-choreographed assembly pathway.Nature communications · 2022Article
- Structural basis of proton translocation and force generation in mitochondrial ATP synthase.eLife · 2017Article
- Thermodynamics and kinetics of the FoF1-ATPase: application of the probability isotherm.Royal Society open science · 2016Article
- A mechano-chemiosmotic model for the coupling of electron and proton transfer to ATP synthesis in energy-transforming membranes: a personal perspective.Photosynthesis research · 2015Article
- A thermo-physical analysis of the proton pump vacuolar-ATPase: the constructal approach.Scientific reports · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
FO-ATP synthase (FO) is a rotary motor that converts potential energy from ions, usually protons, moving from high- to low-potential sides of a membrane into torque and rotary motion. Here we propose a mechanism whereby electric fields emanating from the proton entry and exit channels act on asymmetric charge distributions in the c-ring, due to protonated and deprotonated sites, and drive it to rotate. The model predicts a scaling between time-averaged torque and proton motive force, which can be hindered by mutations that adversely affect the channels. The torque created by the c-ring of FO drives the γ-subunit to rotate within the ATP-producing complex (F1) overcoming, with the aid of thermal fluctuations, an opposing torque that rises and falls with angular position. Using the analogy with thermal Brownian motion of a particle in a tilted washboard potential, we compute ATP production rates vs. proton motive force. The latter shows a minimum, needed to drive ATP production, which scales inversely with the number of proton binding sites on the c-ring.
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Registered trials
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