ArticleProceedings of the National Academy of Sciences of the United States of America2016
Biophysical comparison of ATP synthesis mechanisms shows a kinetic advantage for the rotary process.
Article in Proceedings of the National Academy of Sciences of the United States of America, 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.
- An Expanded Markov State Model-Transition Path Theory Framework for Ion Conduction Reactive Pathways through Membrane Channels.The journal of physical chemistry letters · 2026Article
- Multistate Kinetic Model of the Sodium-Potassium ATPase.The journal of physical chemistry. B · 2025Article
- Multi-scale reactor designs extend the physical limits ofbioRxiv : the preprint server for biology · 2024Article
- WESTPA 2.0: High-Performance Upgrades for Weighted Ensemble Simulations and Analysis of Longer-Timescale Applications.Journal of chemical theory and computation · 2022Article
- From OCR and ECAR to energy: Perspectives on the design and interpretation of bioenergetics studies.The Journal of biological chemistry · 2021Review
- Poor Person's pH Simulation of Membrane Proteins.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Opposing Pressures of Speed and Efficiency Guide the Evolution of Molecular Machines.Molecular biology and evolution · 2019Article
- Mechanisms for achieving high speed and efficiency in biomolecular machines.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Allocating dissipation across a molecular machine cycle to maximize flux.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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Authors and funding
4 authors.
Funding
Abstract
The ATP synthase (F-ATPase) is a highly complex rotary machine that synthesizes ATP, powered by a proton electrochemical gradient. Why did evolution select such an elaborate mechanism over arguably simpler alternating-access processes that can be reversed to perform ATP synthesis? We studied a systematic enumeration of alternative mechanisms, using numerical and theoretical means. When the alternative models are optimized subject to fundamental thermodynamic constraints, they fail to match the kinetic ability of the rotary mechanism over a wide range of conditions, particularly under low-energy conditions. We used a physically interpretable, closed-form solution for the steady-state rate for an arbitrary chemical cycle, which clarifies kinetic effects of complex free-energy landscapes. Our analysis also yields insights into the debated "kinetic equivalence" of ATP synthesis driven by transmembrane pH and potential difference. Overall, our study suggests that the complexity of the F-ATPase may have resulted from positive selection for its kinetic advantage.
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