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JBC, Vol. 252, Issue 9, 2891-2899, May, 1977
H. S. Penefsky
Beef heart mitochondrial ATPase (F1) exhibited a single binding site for
Pi. The interaction with Pi was reversible, partially dependent on the
presence of divalent metal ions, and characterized by a dissociation
constant at pH 7.5 of 80 micronM. A variety of substances known to
influence oxidative phosphorylation or the activity of the soluble ATPase
(F1) also influenced Pi binding by the enzyme. Thus aurovertin, an
inhibitor of oxidative phosphorylation, which was bound tightly by F1 and
inhibited ATPase activity, enhanced Pi binding via a 4-fold increase in the
affinity of the enzyme for Pi (KD = 20 micronM) but did not alter binding
stoichiometry. Anions such as SO4(2-), SO3(2-), chromate, and
2,4-dinitrophenolate, which stimulated ATPase activity of F1, also enhanced
Pi binding. Inhibitors of ATPase activity such as
nickel/bathophenanthroline and the protein ATPase inhibitor of Pullman and
Monroy (Pullman, M. E., and Monroy, G. C. (1963) J. Biol. Chem. 238,
3762-3769) inhibited Pi binding. The adenine nucleotides ADP, ATP, and the
ATP analog adenylyl imidodiphosphate as well as the Pi analog arsenate,
also inhibited Pi binding. The observations suggest that the Pi binding
site was located in or near an adenine nucleotide binding site on the
molecule.
Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase
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