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

Content Provider	PubMed Central
Author	Adachi, Kengo Oiwa, Kazuhiro Yoshida, Masasuke Takayuki, Nishizaka Kinosita, Kazuhiko
Copyright Year	2012
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.
Related Links	http://dx.doi.org/10.1038/ncomms2026
Starting Page	1022
File Format	PDF
ISSN	20411723
e-ISSN	20411723
Journal	Nature Communications
Volume Number	3
Language	English
Publisher	Nature Pub. Group
Publisher Date	2012-08-01
Access Restriction	Open
Rights Holder	Nature Pub. Group
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Physics and Astronomy(all) Chemistry(all) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Chemistry Physics and Astronomy Biochemistry, Genetics and Molecular Biology

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