The
activity of many enzymes is regulated by associative processes.
To model this mechanism, we report here that the conformation of an
unstructured bimetallic Zn(II) complex can be controlled by its inclusion
in the cavity of a γ-cyclodextrin. This results in the formation
of a catalytic bimetallic site for the hydrolytic cleavage of the
RNA model substrate HPNP, whose reactivity is 30-fold larger with
respect to the unstructured complex. Competitive inhibition with 1-adamantanecarboxylate
displaces the metal complex from the cyclodextrin decreasing the reactivity.
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