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Molecular motors

What makes ATP synthase spin?

Nature volume 402, pages 247–249 (1999)Cite this article

Many years ago, when enzymes were first recognized as being proteins, few people could have imagined the wondrous, precise and diverse structures that make possible their catalytic and other functions. The ATP synthase enzyme, for example, performs catalysis as a molecular machine with an unexpected internal rotary mechanism. On page 263 of this issue, Rastogi and Girvin1 report the latest insights into this mechanism. Using sophisticated NMR and chemical probes, they have revealed structural changes in a critical subunit that could drive the rotation.

ATP synthase, also known as F1F0 ATPase, catalyses the formation of ATP (adenosine triphosphate) from ADP (adenosine diphosphate) and Pi (inorganic phosphate), in processes known as oxidative phosphorylation (driven by oxidations in animal cells and microorganisms) and photophosphorylation (driven by light in plant cells). Once formed, ATP is cleaved back to ADP and Pi, as it provides the energy to drive a myriad of metabolic processes including biosyntheses, muscle contraction, and nerve and brain function.

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Figure 1: Model of the Escherichia coli ATP synthase.
Figure 2: How rotation of the γ subunit drives catalysis.

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  1. the Molecular Biology Institute, University of California, 611 Circle Drive East, Los Angeles, 90095-1570, California, USA

    Paul D. Boyer

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  1. Paul D. Boyer
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Correspondence to Paul D. Boyer.

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Boyer, P. What makes ATP synthase spin?. Nature 402, 247–249 (1999). https://doi.org/10.1038/46193

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