title: The regulation of catalysis in ATP synthase.
abstract: ATP synthase is regulated so as to prevent futile hydrolysis of ATP when the transmembrane proton electrochemical gradient, delta mu H+, falls. Mitochondria and chloroplasts have different mechanisms for inhibition of ATP synthase: by binding an inhibitor protein, and by stabilization of the ADP-inhibited state by making an intramolecular disulphide bond, respectively. The recently determined structure of bovine F1-ATPase is locked in a conformation that probably represents the ADP-inhibited state of the enzyme.
authors.affiliation: Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.
authors.forename: J E
authors.initials: JE
authors.lastname: Walker
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002384:Catalysis; D002736:Chloroplasts / Q000201:enzymology; D015536:Down-Regulation; D008928:Mitochondria / Q000201:enzymology*; D008969:Molecular Sequence Data; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism
chemical_list: D006180:Proton-Translocating ATPases