μ-η²:η²-peroxodicopper(II) complex with a secondary diamine ligand: A functional model of tyrosinase

The activation of dioxygen (O₂) by Cu(I) complexes is an important process in biological systems and industrial applications. In tyrosinase, a binuclear copper enzyme, a μ-η²: η²-peroxodicopper(II) species is accepted generally to be the active oxidant. Reported here is the characterization and reactivity of a μ-η²:η²-peroxodicopper(II) complex synthesized by reacting the Cu(I) complex of the secondary diamine ligand N,N′-di-tert-butyl-ethylenediamine (DBED), [(DBED)Cu(MeCN)](X) (1·X, X = CF₃SO₃, CH₃SO₃ ^-, SbF₆^-, BF₄^-), with O₂ at 193 K to give [{Cu(DBED)}₂(O₂)](X) ₂ (2·X₂). The UV-vis and resonance Raman spectroscopic features of 2 vary with the counteranion employed yet are invariant with change of solvent. These results implicate an intimate interaction of the counteranions with the Cu₂O₂ core. Such interactions are supported further by extended X-ray absorption fine structure (EXAFS) analyses of solutions that reveal weak copper-counteranion interactions. The accessibility of the Cu₂O₂ core to exogenous ligands such as these counteranions is manifest further in the reactivity of 2 with externally added substrates. Most notable is the hydroxylation reactivity with phenolates to give catechol and quinone products. Thus the strategy of using simple bidentate ligands at low temperatures provides not only spectroscopic models of tyrosinase but also functional models.