title: The structure of bovine mitochondrial F1-ATPase: an example of rotary catalysis.
abstract: There is now compelling evidence in support of a rotary catalytic mechanism in F1-ATPase, and, by extension, in the intact ATP synthase. Although models have been proposed to explain how protein translocation in F0 results in rotation of the gamma-subunit relative to the alpha 3/beta 3 assembly in F1 [22], these are still speculative. It seems likely that a satisfactory explanation of this mechanism will ultimately depend on structural information on the intact ATP synthase.
authors: MRC Laboratory of Molecular Biology, Cambridge, U.K.
authors: A G
authors: AG
authors: Leslie
authors: J P
authors: JP
authors: Abrahams
authors: K
authors: K
authors: Braig
authors: R
authors: R
authors: Lutter
authors: R I
authors: RI
authors: Menz
authors: G L
authors: GL
authors: Orriss
authors: M J
authors: MJ
authors: van Raaij
authors: J E
authors: JE
authors: Walker
mesh_terms: D000818:Animals; D002384:Catalysis; D020134:Catalytic Domain; D002417:Cattle; D004791:Enzyme Inhibitors / Q000737:chemistry; D066298:In Vitro Techniques; D008928:Mitochondria / Q000201:enzymology*; D008958:Models, Molecular; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D012399:Rotation
chemical_list: D004791:Enzyme Inhibitors; D006180:Proton-Translocating ATPases