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Energy transduction in the F1 motor of ATP synthase

Nature volume 396, pages 279–282 (1998)Cite this article

Abstract

ATP synthase is the universal enzyme that manufactures ATP from ADP and phosphate by using the energy derived from a transmembrane protonmotive gradient. It can also reverse itself and hydrolyse ATP to pump protons against an electrochemical gradient. ATP synthase carries out both its synthetic and hydrolytic cycles by a rotary mechanism1,2,3,4. This has been confirmed in the direction of hydrolysis5,6 after isolation of the soluble F1 portion of the protein and visualization of the actual rotation of the central ‘shaft’ of the enzyme with respect to the rest of the molecule, making ATP synthase the world's smallest rotary engine. Here we present a model for this engine that accounts for its mechanochemical behaviour in both the hydrolysing and synthesizing directions. We conclude that the F1 motor achieves its high mechanical torque and almost 100% efficiency because it converts the free energy of ATP binding into elastic strain, which is then released by a coordinated kinetic and tightly coupled conformational mechanism to create a rotary torque.

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Figure 1: Structure of ATP synthase.
Figure 2: Conformation changes in the β-subunit.
Figure 3: Energy profiles.
Figure 4: Model predictions.

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Acknowledgements

We thank J. Walker for discussions on the motions of the β-subunit and for videos of the three configurations which simulated our interpolated videos; R. Nakamoto for advice on the switch 1 and 2 interactions; M. Yoshida, K. Kinosita and their co-workers for inspiring the construction of the F1 model by their ingenious experiments; and M. Grabe and K. Kinosita for insightful comments and suggestions on the manuscript.

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  1. Department of Molecular and Cellular Biology, and College of Natural Resources, University of California, Berkeley, 94720-3112, California, USA

    Hongyun Wang & George Oster

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  1. Hongyun Wang
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  2. George Oster
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Correspondence to George Oster.

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Wang, H., Oster, G. Energy transduction in the F1 motor of ATP synthase. Nature 396, 279–282 (1998). https://doi.org/10.1038/24409

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