title: Rotary catalysis of the stator ring of F(1)-ATPase.
abstract: F(1)-ATPase is a rotary motor protein in which 3 catalytic β-subunits in a stator α(3)β(3) ring undergo unidirectional and cooperative conformational changes to rotate the rotor γ-subunit upon adenosine triphosphate hydrolysis. The prevailing view of the mechanism behind this rotary catalysis elevated the γ-subunit as a "dictator" completely controlling the chemical and conformational states of the 3 catalytic β-subunits. However, our recent observations using high-speed atomic force microscopy clearly revealed that the 3 β-subunits undergo cyclic conformational changes even in the absence of the rotor γ-subunit, thus dethroning it from its dictatorial position. Here, we introduce our results in detail and discuss the possible operating principle behind the F(1)-ATPase, along with structurally related hexameric ATPases, also mentioning the possibility of generating hybrid nanomotors. This article is part of a Special Issue entitled: 17th European Bioenergetics Conference (EBEC 2012).
authors.affiliation: Department of Applied Chemistry, the University of Tokyo, Tokyo, Japan. iino@appchem.t.u-tokyo.ac.jp
authors.forename: Ryota
authors.initials: R
authors.lastname: Iino
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Noji
mesh_terms: D002384:Catalysis; D020134:Catalytic Domain; D056004:Molecular Dynamics Simulation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D006180:Proton-Translocating ATPases