CHARACTERIZATION OF A HIGH ENERGY INTERMEDIATE OF OXIDATIVE PHOSPHORYLATION

Abstract
Evidence has been presented indicating that the intermediate at the first phosphorylation site of oxidative phosphorylation is a DPN high-energy protein, which combines first with Pi to release DPN and form a transient phosphorylated intermediate. The latter combines with ADP to form ATP and free protein. A reaction sequence of oxidative phosphorylation has been proposed which explains many of the findings in the bacterial and mitochondrial systems.