Mechanistic Insight into the Catechol Oxidase Activity by a Biomimetic Dinuclear Copper Complex

The biomimetic catalytic oxidation of 3,5-ditert-
butylcatechol by the dicopper(II) complex of the
ligand a,a¢-bis{bis[1-(1¢-methyl-2¢-benzimidazolyl)
methyl]amino}-m-xylene in the presence of dioxygen has
been investigated as a function of temperature and pH in
a mixed aqueous/organic solvent. The catalytic cycle
occurs in two steps, the first step being faster than the
second step. In the first step, one molecule of catechol is
oxidized by the dicopper(II) complex, and the copper(II)
centers are reduced. From the pH dependence, it is deduced
that the active species of the process is the
monohydroxo form of the dinuclear complex. In the
second step, the second molecule of catechol is oxidized
by the dicopper(I)-dioxygen complex formed upon
oxygenation of the reduced complex. In both cases,
catechol oxidation is an inner-sphere electron transfer
process involving binding of the catechol to the active
species. The binary catechol-dicopper(II) complex
formed in the first step could be characterized at very
low temperature (90 C), where substrate oxidation is
blocked. On the contrary, the ternary complex of dicopper(
I)-O2-catechol relevant to the second step does
not accumulate in solution and could not be characterized,
even at low temperature. The investigation of the
biphasic kinetics of the catalytic reaction over a range of
temperatures allowed the thermodynamic (DH and DS)
and activation parameters (DH „ and DS „ ) connected
with the key steps of the catecholase process to be
obtained.