Hydrolysis of ITP generates a membrane potential in submitochondrial particles.
ITP hydrolysis catalysed by the ATPase of submitochondrial particles from both bovine heart and rat liver is shown to be linked to the generation of a membrane potential, and therefore also to proton translocation. The magnitude of the membrane potential is similar to that observed during ATP hydrolysis at equivalent concentrations of phosphate and nucleoside tri- and diphosphates. An explanation is suggested for why in other reports ITP was found to be a poor substrate for supporting energy-linked reactions that are driven by the membrane potential.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D007292:Inosine Nucleotides / Q000378:metabolism*; D007293:Inosine Triphosphate / Q000378:metabolism*; D008564:Membrane Potentials; D008928:Mitochondria / Q000378:metabolism*; D008929:Mitochondria, Heart / Q000378:metabolism*; D008930:Mitochondria, Liver / Q000378:metabolism*; D013367:Submitochondrial Particles / Q000378:metabolism* / Q000502:physiology; D013379:Substrate Specificity
D007292:Inosine Nucleotides; D007293:Inosine Triphosphate; D000251:Adenosine Triphosphatases