@article{oai:kanazawa-u.repo.nii.ac.jp:00010915,
 author = {内橋, 貴之 and 安藤, 敏夫 and Uchihashi, Takayuki and Iino, Ryota and Ando, Toshio and Noji, Hiroyuki},
 issue = {6043},
 journal = {Science},
 month = {Aug},
 note = {F1 is an adenosine triphosphate (ATP)–driven motor in which three torque-generating β subunits in the α3β3 stator ring sequentially undergo conformational changes upon ATP hydrolysis to rotate the central shaft γ unidirectionally. Although extensive experimental and theoretical work has been done, the structural basis of cooperative torque generation to realize the unidirectional rotation remains elusive. We used high-speed atomic force microscopy to show that the rotorless F1 still “rotates”; in the isolated α3β3 stator ring, the three β subunits cyclically propagate conformational states in the counterclockwise direction, similar to the rotary shaft rotation in F1. The structural basis of unidirectionality is programmed in the stator ring. These findings have implications for cooperative interplay between subunits in other hexameric ATPases., 金沢大学ナノ生命科学研究所 / 金沢大学理工研究域数物科学系},
 pages = {755--758},
 title = {High-speed atomic force microscopy reveals rotary catalysis of rotor-less F1-ATPase},
 volume = {333},
 year = {2011}
}