Article abstract
Nature Structural & Molecular Biology 14, 841 - 846 (2007)
Published online: 26 August 2007 | Corrected online: 17 September 2007 | doi:10.1038/nsmb1296
There is a Corrigendum (October 2007) associated with this Article.
F1-ATPase rotates by an asymmetric, sequential mechanism using all three catalytic subunits
Takayuki Ariga1,2,4, Eiro Muneyuki1,3 & Masasuke Yoshida1
Abstract
F1-ATPase, the catalytic part of FoF1-ATP synthase, rotates the central 
subunit within the 
3
3 cylinder in 120° steps, each step consuming a single ATP molecule. However, how the catalytic activity of each subunit is coordinated with the other two subunits to drive rotation remains unknown. Here we show that hybrid F1 containing one or two mutant subunits with altered catalytic kinetics rotates in an asymmetric stepwise fashion. Analysis of the rotations reveals that for any given subunit, the subunit binds ATP at 0°, cleaves ATP at 
200° and carries out a third catalytic event at 320°. This demonstrates the concerted nature of the F1 complex activity, where all three subunits participate to drive each 120° rotation of the subunit with a 120° phase difference, a process we describe as a 'sequential three-site mechanism'.
- Chemical Resources Laboratory, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8503, Japan.
- Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka, 565-0871, Japan.
- Department of Physics, Faculty of Science and Engineering, Chuo University, Kasuga 1-13-27, Bunkyo-ku, Tokyo, 112-8551, Japan.
- Present address: Department of Physics, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan.
Correspondence to: Takayuki Ariga1,2,4 e-mail: ariga@chem.scphys.kyoto-u.ac.jp
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