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Controlled rotation of the F(1)-ATPase reveals differential and continuous binding changes for ATP synthesis

F(1)-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 r...

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Библиографические подробности
Главные авторы: Adachi, Kengo, Oiwa, Kazuhiro, Yoshida, Masasuke, Nishizaka, Takayuki, Kinosita, Kazuhiko
Формат: Artigo
Язык:Inglês
Опубликовано: Nature Pub. Group 2012
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Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC3449090/
https://ncbi.nlm.nih.gov/pubmed/22929779
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/ncomms2026
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