A brief view of oxidative phosphorylation.

Abstract

This article briefly reviews the mechanism of ATP synthesis by mitochondria. The interaction of dicyclohexylcarbodiimide of oligomycin at the membrane sector (F0) of the ATP synthase complex alters the mode of ATP binding at the catalytic sites of F1. The rate of energy production by the respiratory chain modulates the kinetics of ATP synthesis between a low Km-low Vmax mode and a high Km-high Vmax mode. The turnover number of the ATP synthase in the direction of ATP synthesis was determined to be 440s-1. Finally, kinetic and equilibrium binding studies have shown that three molecules of ADP bind to the ATP synthase in a sequential manner before rapid ATP synthesis ensues.