A model for conformational coupling of membrane potential and proton translocation to ATP synthesis and to active transport.
Acceptance of a membrane potential and/or a proton gradient as a possible means of transmitting energy from oxidations to ATP synthesis rests in part on a satisfactory hypothesis for how the potential or proton gradient could drive ATP synthesis. Recognition that energy input may drive ATP synthesis by change in binding of reactants at the catalytic site has led to the suggestions presented in this paper. These are that in oxidative phosphorylation and photophosphorylation, the requisite conformational changes may be coupled to exposure of charged groups to different sides of the membrane. The cycle of charged group exposure or movement may be driven by the membrane potential or, through protonation and deprotonation, may be coupled to proton translocation across the membrane. Effects of proton gradient and membrane potential may be additive. Similar conformational coupling suggestions may explain proton translocation coupled to ATP cleavage and active transport of metabolites coupled to membrane potential, proton gradients of ATP cleavage.
D000255:Adenosine Triphosphate / Q000096:biosynthesis*; D001693:Biological Transport, Active; D004734:Energy Metabolism; D007526:Isoelectric Point; D007700:Kinetics; D008564:Membrane Potentials; D008566:Membranes / Q000378:metabolism / Q000648:ultrastructure; D008954:Models, Biological; D010085:Oxidative Phosphorylation; D011522:Protons
D011522:Protons; D000255:Adenosine Triphosphate