The effects of adenylylimidodiphosphate (AMP-PNP) and guanylylimidodiphosphate (GMP-PNP) on the kinetics of MgATP, MgITP and MgGTP hydrolysis by mitochondrial ATPase (EC 3.6.1.3) from human placenta were studied. AMP-PNP is a noncompetitive inhibitor of hydrolysis of all substrates used, both in the presence and in the absence of the activating HCO3- anion. At least two binding sites for AMP-PNP are present in the F1. Unlike AMP-PNP, GMP-PNP was shown to be a competitive inhibitor of hydrolysis of all substrates used. The results of the kinetic experiments presented support the alternating three-site mechanism of ATP hydrolysis by mitochondrial ATPase.
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