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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Detalles Bibliográficos
Autores principales: Adachi, Kengo, Oiwa, Kazuhiro, Yoshida, Masasuke, Nishizaka, Takayuki, Kinosita, Kazuhiko
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Pub. Group 2012
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3449090/
https://www.ncbi.nlm.nih.gov/pubmed/22929779
http://dx.doi.org/10.1038/ncomms2026

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3449090/
https://www.ncbi.nlm.nih.gov/pubmed/22929779
http://dx.doi.org/10.1038/ncomms2026

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