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J. Biol. Chem., Vol. 265, Issue 31, 18725-18728, Nov, 1990
YM Milgrom, LL Ehler and PD Boyer
The F1-ATPase from chloroplasts (CF1) lacks catalytic capacity for ATP
hydrolysis if ATP is not bound at noncatalytic sites. CF1 heat activated in
the presence of ADP, with less than one ADP and no ATP at non-catalytic
sites, shows a pronounced lag in the onset of ATP hydrolysis after exposure
to 5-20 microM ATP. The onset of activity correlates well with the binding
of ATP at the last two of the three noncatalytic sites. The dependence of
activity on the presence of ATP at non-catalytic sites is shown at
relatively low or high free Mg2+ concentrations, with or without
bicarbonate as an activating anion, and when the binding of ATP at
noncatalytic sites is slowed 3-4-fold by sulfate. The latent CF1 activated
by dithiothreitol also requires ATP at noncatalytic sites for ATPase
activity. A similar requirement by other F1-ATPases and by ATP synthases
seems plausible.
ATP binding at noncatalytic sites of soluble chloroplast F1-ATPase is required for expression of the enzyme activity
Department of Chemistry and Biochemistry and Molecular Biology Institute, University of California, Los Angeles 90024.
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