title: Notes on the mechanism of ATP synthesis.
abstract: The most commonly quoted mechanism of the coupling between the electrochemical proton gradient and the formation of ATP from ADP and P(i) assumes that all states of the F(1) portion of the ATP synthase have beta subunits in "tight," "loose," and "open" conformations. Models based on this assumption are inconsistent with some of the available experimental evidence. A mechanism that includes an additional beta subunit conformation, "closed," observed in the rat liver structure overcomes these difficulties.
authors.affiliation: Department of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Baltimore, Maryland 21205, USA.
authors.forename: M A
authors.initials: MA
authors.lastname: Bianchet
authors.forename: P L
authors.initials: PL
authors.lastname: Pedersen
authors.forename: L M
authors.initials: LM
authors.lastname: Amzel
mesh_terms: D000255:Adenosine Triphosphate / Q000096:biosynthesis*; D000818:Animals; D020134:Catalytic Domain; D004563:Electrochemistry; D008930:Mitochondria, Liver / Q000201:enzymology; D025261:Mitochondrial Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D008958:Models, Molecular; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D021122:Protein Subunits; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism*; D051381:Rats
chemical_list: D021122:Protein Subunits; D000255:Adenosine Triphosphate; D025261:Mitochondrial Proton-Translocating ATPases; D006180:Proton-Translocating ATPases