A critique of the chemosmotic model of energy coupling.
The chemosmotic model provides a framework for visualizing energy-coupled reactions (vectorial reaction sequences, membrane-dependent gradient formation, and charge separation of reacting species) and a mechanism for energy coupling (indirect coupling between the driving and driven reaction sequences mediated by a membrane potential or a protonmotive force). The mechanistic parameters of this model have been examined from four standpoints: compatibility with the experimental realities, supporting evidence that is unambiguous, compatibility with the enzymic nature of energy coupling, and the capability for generating verifiable predictions. Recent developments that have clarified the mechanism of ion transport, the nature of the protonic changes that accompany energy coupling, and the enzymic nature of energy coupling systems have made such an examination both timely and necessary. After weighing the available evidence, it has been concluded that the chemosmotic principle of indirect coupling has no basis in fact and that it is physically unsound in respect to the mechanism of energy coupling and enzymic catalysis.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000502:physiology*; D004734:Energy Metabolism; D007425:Intracellular Membranes / Q000502:physiology*; D007473:Ion Channels / Q000502:physiology; D008564:Membrane Potentials; D008928:Mitochondria / Q000502:physiology*; D011522:Protons
D007473:Ion Channels; D011522:Protons; D003576:Electron Transport Complex IV; D000251:Adenosine Triphosphatases