Controlled rotation of the F1-ATPase reveals differential and continuous binding changes for ATP synthesis

Kengo Adachi (), Kazuhiro Oiwa, Masasuke Yoshida, Takayuki Nishizaka and Kazuhiko Kinosita
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Kengo Adachi: Faculty of Science, Gakushuin University, Toshima-ku
Kazuhiro Oiwa: Advanced ICT Research Institute, National Institute of Information and Communications Technology, Nishi-ku
Masasuke Yoshida: Faculty of Life Sciences, Kyoto Sangyo University, Kita-ku
Takayuki Nishizaka: Faculty of Science, Gakushuin University, Toshima-ku
Kazuhiko Kinosita: Faculty of Science and Engineering, Waseda University, Shinjuku-ku

Nature Communications, 2012, vol. 3, issue 1, 1-12

Abstract: Abstract F1-ATPase is an ATP-driven rotary molecular motor that synthesizes ATP when rotated in reverse. To elucidate the mechanism of ATP synthesis, we imaged binding and release of fluorescently labelled ADP and ATP while rotating the motor in either direction by magnets. Here we report the binding and release rates for each of the three catalytic sites for 360° of the rotary angle. We show that the rates do not significantly depend on the rotary direction, indicating ATP synthesis by direct reversal of the hydrolysis-driven rotation. ADP and ATP are discriminated in angle-dependent binding, but not in release. Phosphate blocks ATP binding at angles where ADP binding is essential for ATP synthesis. In synthesis rotation, the affinity for ADP increases by >104, followed by a shift to high ATP affinity, and finally the affinity for ATP decreases by >104. All these angular changes are gradual, implicating tight coupling between the rotor angle and site affinities.

Date: 2012
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DOI: 10.1038/ncomms2026

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