Chemiosmotic vs conformational models of oxidative phosphorylation: Theory and mechanistic insights

The chemiosmotic model of oxidative phosphorylation (oxphos) proposed by Peter Mitchell in 1961 was revisited and its basic mechanistic assumptions that oxphos is driven by protonmotive force either across or within the mitochondrial inner membrane were re-evaluated in light of recent findings. Available evidence strongly suggests that non-chemiosmotic mechanisms such as the conformon or detailed conformational change-mediated mechanisms, such as Nath's torsional mechanism of energy transduction and ATP synthesis, are needed to explain the phenomenon of oxphos in enzymologically and quantum-mechanically realistic terms. An in-depth analysis of oxphos, taking into account recent findings reveal the logical errors or fallacies in dismissing conformational change-based models in favor of the chemiosmotic theory, and suggests the principal mechanistic events underlying chemomechanical coupling in bioenergetic processes in general.