Control of heart mitochondrial oxygen consumption by creatine kinase: the importance of enzyme localization.

Abstract

The route of movement of ADP produced in the mitochondrial creatine kinase reaction was investigated by recording the rate of ADP-dependent oxygen consumption in the presence of phosphoenolpyruvate and pyruvate kinase. This pyruvate kinase system completely abolished activation of respiration by ADP added or by ADP produced in the hexokinase reaction in the medium, but was not able to inhibit the creatine kinase activated respiration when creatine kinase was bound to the inner mitochondrial membrane. These different responses of oxidative phosphorylation were observed at equal ATPADP ratios in the medium. The data obtained evidence direct channeling of ADP from heart mitochondrial creatine kinase to the adenine nucleotide translocase without its prompt release into the medium.