Novel molecular insights into ATP synthesis in oxidative phosphorylation based on the principle of least action

In previous papers in Chemical Physics Letters, the author has analyzed the coupled nonequilibrium processes of ATP synthesis in oxidative phosphorylation (OXPHOS) with succinate as substrate. It was shown experimentally that the system evolves with time to a minimum unit action of 1.4 x 10(-3) J s natom O-1 mg protein(-1). Here the experimental value of the average unit action is suitably normalized. It is shown that the average unit action per elementary ion (proton or anion/countercation) translocation event through the F-O portion of the FOF1-ATP synthase yields a value of 6.70 x 10(-34) J s. This is equal to the value of the Planck's constant, h to within 1%. The results provide a novel molecular interpretation of energy transduction by ATP synthase in OXPHOS under optimal conditions, linking it to a fundamental physical constant.

Automated summary

This study analyzes the coupled nonequilibrium processes of ATP synthesis in oxidative phosphorylation and presents the experimental value of the average unit action. By normalizing the average unit action per ion translocation event, it is discovered that the value is remarkably close to the Planck's constant, providing a novel molecular interpretation of energy transduction.