title: Synthase (H(+) ATPase): coupling between catalysis, mechanical work, and proton translocation.
abstract: Coupling with electrochemical proton gradient, ATP synthase (F(0)F(1)) synthesizes ATP from ADP and phosphate. Mutational studies on high-resolution structure have been useful in understanding this complicated membrane enzyme. We discuss mainly the mechanism of catalysis in the beta subunit of F(1) sector and roles of the gamma subunit in energy coupling. The gamma-subunit rotation during catalysis is also discussed.
authors.affiliation: Division of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University, CREST, Japan Science and Technology Corporation, Ibaraki, 567-0047, Osaka, Japan. m-futai@sanken.osaka-u.ac.jp
authors.forename: M
authors.initials: M
authors.lastname: Futai
authors.forename: H
authors.initials: H
authors.lastname: Omote
authors.forename: Y
authors.initials: Y
authors.lastname: Sambongi
authors.forename: Y
authors.initials: Y
authors.lastname: Wada
mesh_terms: D001419:Bacteria / Q000201:enzymology; D001665:Binding Sites; D002736:Chloroplasts / Q000201:enzymology; D007700:Kinetics; D008958:Models, Molecular; D020409:Molecular Motor Proteins; D009154:Mutation; D009711:Nucleotides / Q000378:metabolism; D011485:Protein Binding; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism; D011522:Protons
chemical_list: D020409:Molecular Motor Proteins; D009711:Nucleotides; D011522:Protons; D006180:Proton-Translocating ATPases