Intact rat liver mitochondria possess a very low hydrolytic activity, if any, towards exogenous pyrophosphate. This activity can be unmasked by making mitochondria permeable to PPi by toluene treatment or by disrupting them with detergents or ultrasound, thus indicating that the active site of pyrophosphatase is localized in the matrix. The initial rates of PPi hydrolysis of toluene-permeabilized mitochondria and purified pyrophosphatase were found to depend, in a similar manner, on PPi and Mg2+ concentrations. The simplest model consistent with these data in both cases implies that the reaction proceeds via two pathways and requires MgPPi as substrate and at least one Mg2+ ion as activator. In the presence of 0.4 mM Mg2+ (physiological concentration) the inhibition constant for Ca2+ is 12 microM and the enzyme activity is no less than 50% of the maximal one. The data obtained suggest that the activity of pyrophosphatase in mitochondria is high enough to keep free PPi concentration at a level close to the equilibrium one.
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