Snapshots of a Metamorphosing Cu(II) Ground State in a Galactose Oxidase-Inspired Complex

The novel ligand 2,6-bis[S-(3,5-di-tert-butyl-2-hydroxyphenyl)sulfanylmethyl]pyridine (H(2)L1) and its copper(II) complex Cu(L1), 1, were synthesized with the aim of constructing a model of the active site of the enzyme galactose oxidase (GOase). Cyclic voltammetry studies show that 1 undergoes ligand-based quasi-reversible oxidations (phenolate/phenoxyl) and reversible metal-based reduction [copper(II)/copper(I)] similar to those of GOase, but at potentials much higher and lower, respectively, than those found for the enzyme. At room temperature, spectrophotometric titrations show that 1 binds strongly to 1 equiv of pyridine. In frozen solutions (77 K), 1 quantitatively binds both pyridine and ethers (e.g., 1,4-dioxane) as assessed by X- and Q-band EPR spectroscopy. Profound shifts in the pattern of g values result, from rhombic (g(1) > g(2) > g(3)) in toluene to either inverted axial patterns (g(1) = g(2) >> g(3)) in the presence of ethers or a near-axial pattern (g(1) >> g(2) > g(3)) in the presence of pyridine. Crystallographic analyses of the parent complex 1.MeCN, the dioxane-bridged dimer [(Cu(L1))(2)((mu-1,4)-1,4-dioxane)].(Me(2)CO)(2) (2), and the pyridine complex [Cu(L1)(pyridine)] (3) show that the pyridine and ether ligands bond to copper at a sixth octahedral position left vacant by the pentadentate NO(2)S(2) coordination mode of L1(2-) and induce perturbations of its geometry. Hybrid DFT calculations based on the crystallographic coordinates combined with perturbation theory expressions for the g values of a d(9) system correlate the results from EPR spectroscopy to the proportions of d(x)(2)(-)(y)(2) and d(z)(2) character in the relevant copper-centered unoccupied molecular orbital. The combination of spectroscopic, structural, and computational results for this set of copper(II) complexes provides a demonstrative example of the physical phenomena underlying rhombic EPR spectra of d(9) systems.