Formation of mu-peroxo Dicopper(II) -(-)-Sparteine Complex with an Axial Ligand

摘要

We performed a UV-vis spectroscopic study on formation of a new benzoate (Bz-)-bridged butterfly type (-r)2:n2-peroxo dicopper (II) complex of (-)-sparteine (Sp) in dichloromethane solution. The spectroscopic result of this system suggested that an analogous Bz--binding side-on peroxide species to [CuII2(aSp)_2([mu-r:r-O2)(Bz~)]+ (αSp = α-isosparteine) was formed at -80 °C in the similar mode reported, previously.IntroductionType III copper proteins of hemocyanin (Hc) and Tyrosinase (Tyr) contain redox-active dicopper cores, working for dioxygen-transportation and substrate-oxygenation, respectively1. Tyr catalyzes ortho-hydroxylation of phenol ring, for metabolizing L-tyrosine in biological systems. At the active sites of deoxy-Hc and Tyr, a reduced dicopper (I) center is oxygenated to form a (-r)2:2-peroxo dicopper (II) core as the intermediate species .