title: The molecular mechanism of ATP synthesis by F1F0-ATP synthase.
abstract: ATP synthesis by oxidative phosphorylation and photophosphorylation, catalyzed by F1F0-ATP synthase, is the fundamental means of cell energy production. Earlier mutagenesis studies had gone some way to describing the mechanism. More recently, several X-ray structures at atomic resolution have pictured the catalytic sites, and real-time video recordings of subunit rotation have left no doubt of the nature of energy coupling between the transmembrane proton gradient and the catalytic sites in this extraordinary molecular motor. Nonetheless, the molecular events that are required to accomplish the chemical synthesis of ATP remain undefined. In this review we summarize current state of knowledge and present a hypothesis for the molecular mechanism of ATP synthesis.
authors: Department of Biochemistry and Biophysics, University of Rochester Medical Center, Box 712, 601 Elmwood Avenue, Rochester, NY 14642, USA. alan_senior@urmc.rochester.edu
authors: Alan E
authors: AE
authors: Senior
authors: Sashi
authors: S
authors: Nadanaciva
authors: Joachim
authors: J
authors: Weber
mesh_terms: D000255:Adenosine Triphosphate / Q000096:biosynthesis* / Q000737:chemistry; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray; D004252:DNA Mutational Analysis; D004926:Escherichia coli; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D020409:Molecular Motor Proteins; D010085:Oxidative Phosphorylation; D010785:Photophosphorylation; D010944:Plants; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism*; D012399:Rotation
chemical_list: D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases