Studies of energy transport in heart cells: The functional coupling between mitochondrial creatine phosphokinase and ATP-ADP translocase: Kinetic evidence

Abstract

The dependence of the rate of creatine phosphate synthesis in the mitochondrial creatine phosphokinase reaction upon the rate of oxidative phosphorylation and ATP translocation from the matrix to outside of the mitochondria has been studied. It has been experimentally shown that mitochondrial creatine phosphokinase reacts slowly with ATP in the medium but is very active in utilization of ATP synthesized by the oxidative phosphorylation process. From these data, it is postulated, therefore, that the ATP-ADP translocase transports ATP molecules directly to the active site of creatine phosphokinase localized on the outer site of the inner membrane. This results in an increase in the effective concentration of ATP in the vinicity of the active sites of creatine kinase and in acceleration of the forward reaction (creatine phosphate synthesis). The kinetic theory based on this assumption allows a quantitative explanation of the observed dependences. These data indicate the tight functional coupling between ATP-ADP translocase and creatine phosphokinase in heart mitochondria. It is concluded that in heart cells energy can be transported by creatine phosphate molecules only.