摘要:
Covalently-modified tyrosines are found as cofactors in enzymes such as galactose oxidase and the copper-dependent amine oxidases. In these cases, cofactor formation has been proposed to occur via oxidation of a copper-tyrosine precursor, making electron transfer chemistry in copper-phenolates a key to cofactor biogenesis. Our work was motivated by a desire to understand the ET reactivity of simple metal coordinated phenolate model complexes. Copper and zinc complexes of phenolate ligands were prepared, and their electron and energy-transfer reactivity toward Ru(R(2)bpy)(3)(2+)*(/3+) studied to test the electron-transfer reactivity of metal-coordinated phenolates. M(salxn) (M = Cu2+ Zn2+; salxn = salen, N,N'-disalicylidene-1,2-ethylenediamine; salpen, N,N'-disalicylidene-1,3-propylenediamine; salben, N,N'-disalicylidene-1,4-butylenediamine: salophen, N,N'-disalicylidene-o-phenylenediamine) were synthesized along with the more easily oxidized complexes Cu(bppa) (Hbppa, bis-pyridyl phenolamine) and Cu(icoph) (H(2)icoph, bis-iminocatechol o-phenylenediamine). Zn(salophen) and Cu(salophen) were oxidized by Ru(bpy)(3)(3+), indicating that electron transfer was thermodynamically favorable. Cu(salxn) complexes were observed to be efficient energy-transfer quenchers of Ru(bpy)(3)(2+)*; in contrast, Cu(bppa) and Cu(icoph) quenched Ru(bpy)3(2+)* by electron transfer, with observed reorganization energy lambda = 22 kcal/mol. The large self-exchange reorganization energy calculated for the Cu-coordinated phenolates suggest that the CAO and GalOx cofactors may be poor 1e(-) redox centers, with very slow rates for cofactor biogenesis. (C) 2008 Elsevier Ltd. All rights reserved.