title: Molecular mechanics of protonmotive F0F1 ATPases. Rolling well and turnstile hypothesis.
abstract: The reversible protonmotive F0F1 ATPases perform the uniquely important function of balancing the forces, and interconverting the potential energies, of phosphoryl transfer and proton translocation. The molecular mechanics of the processes of ligand conduction catalysed by the F0F1 ATPases is therefore especially interesting. This paper summarises the main structural and functional knowledge of the F0F1 ATPases in the light of current mechanistic hypotheses, and suggests a new type of rotating subunit hypothesis, which is related to that recently developed for bacterial flagellar motors.
authors.forename: P
authors.initials: P
authors.lastname: Mitchell
mesh_terms: D000244:Adenosine Diphosphate / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D008024:Ligands / Q000378:metabolism; D046911:Macromolecular Substances; D008956:Models, Chemical; D011487:Protein Conformation; D006180:Proton-Translocating ATPases; D011522:Protons
chemical_list: D008024:Ligands; D046911:Macromolecular Substances; D011522:Protons; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases