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Issue 11, 2011
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Mechanochemistry of F1motor protein

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Abstract

Although a variety of physical perturbations are utilised to control chemical reactions or bias chemical equilibria, mechanical force is not generally an option for controlling chemical reactions due to technical complexity. However, upon attaching handles to a responsive moiety and pulling, twisting or pushing it, unique means of controlling chemistry are permitted because mechanical force is intrinsically anisotropic for chemical structures. One remarkable example in natural systems is F1-ATPase, the water-soluble part of FoF1-ATP synthase. F1-ATPase is a rotary motor protein in which the rotor subunit rotates against the surrounding catalytic stator ring, hydrolysing ATP. A unique feature of F1-ATPase is that it synthesises ATP against the large chemical potential of ATP hydrolysis when its rotation is mechanically reversed. This mini-review will introduce the latest findings about the mechanochemical properties of F1-ATPase, and summarise the common concepts of mechanochemistry it shares with synthetic molecular systems.

Graphical abstract: Mechanochemistry of F1motor protein

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Article information


Submitted
07 May 2011
Accepted
20 Jun 2011
First published
18 Jul 2011

Chem. Sci., 2011,2, 2086-2093
Article type
Minireview

Mechanochemistry of F1motor protein

H. Noji, D. Okuno and T. Ikeda, Chem. Sci., 2011, 2, 2086
DOI: 10.1039/C1SC00276G

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