title: ATP synthase: what dictates the size of a ring?
abstract: Recent data suggest the source of F(0)F(1) ATP synthase determines a significant and surprising difference in the size of a putative rotating ring of integral membrane subunits of F(0); this can be correlated with biochemical data suggesting there is variation in the number of protons translocated per ATP synthesised.
authors.affiliation: Department of Biochemistry, University of Oxford, Oxford, UK. ferguson@bioch.ox.ac.uk
authors.forename: S J
authors.initials: SJ
authors.lastname: Ferguson
mesh_terms: D000255:Adenosine Triphosphate / Q000096:biosynthesis / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology*; D007425:Intracellular Membranes / Q000201:enzymology; D046911:Macromolecular Substances; D008928:Mitochondria / Q000201:enzymology*; D008954:Models, Biological; D020836:Protein Structure, Quaternary; D021122:Protein Subunits; D018892:Proton-Motive Force; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism*; D012399:Rotation
chemical_list: D046911:Macromolecular Substances; D021122:Protein Subunits; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases