Abstract
Mitochondrial F1FO ATP synthase, the key enzyme for mitochondrial ATP synthesis, is driven by the proton motive force, PMF. Several studies showed the existence of intramitochondrial heterogeneity of PMF, including a pH gradient between primary proton pumps and ATP synthase. In order to understand the impact of ATP synthase on the proton motive force in more detail, we generated pH maps of mitochondrial sub-compartments under respiratory and hyperglycemic conditions in a mammalian cell line. We found that reverse ATP synthase activity is a strong determinant of local pH values in either condition.
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