title: Essentials for ATP synthesis by F1F0 ATP synthases.
abstract: The majority of cellular energy in the form of adenosine triphosphate (ATP) is synthesized by the ubiquitous F(1)F(0) ATP synthase. Power for ATP synthesis derives from an electrochemical proton (or Na(+)) gradient, which drives rotation of membranous F(0) motor components. Efficient rotation not only requires a significant driving force (DeltamuH(+)), consisting of membrane potential (Deltapsi) and proton concentration gradient (DeltapH), but also a high proton concentration at the source P side. In vivo this is maintained by dynamic proton movements across and along the surface of the membrane. The torque-generating unit consists of the interface of the rotating c ring and the stator a subunit. Ion translocation through this unit involves a sophisticated interplay between the c-ring binding sites, the stator arginine, and the coupling ions on both sides of the membrane. c-ring rotation is transmitted to the eccentric shaft gamma-subunit to elicit conformational changes in the catalytic sites of F(1), leading to ATP synthesis.
authors.affiliation: Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, Stockholm, Sweden. christoph@dbb.su.se
authors.forename: Christoph
authors.initials: C
authors.lastname: von Ballmoos
authors.forename: Alexander
authors.initials: A
authors.lastname: Wiedenmann
authors.forename: Peter
authors.initials: P
authors.lastname: Dimroth
mesh_terms: D000255:Adenosine Triphosphate / Q000096:biosynthesis*; D000818:Animals; D001419:Bacteria / Q000378:metabolism; D006801:Humans; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism*
chemical_list: D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases