Ten years of a biomimetic approach to the copper(II) radical site of galactose oxidase

An overview of recent progress in the modeling of the copper(II)-phenoxyl entity of the metalloenzyme Galactose Oxidase (GO) is presented. GO is an enzyme that is extremely engineered by nature: its active site exhibits several unusual features, such as a coordinated tyrosyl radical, post-translationally modified amino acids, and pi-stacked residues. Understanding each of these particularities has posed a challenge for chemists, who have consequently developed several biomimetic complexes during the last decade. The properties of representative complexes are described herein, with special emphasis given to copper(II) complexes involving tripodal ligands. All these biomimetic compounds have been developed with the aim of better understanding biologically relevant problems. I show here that the structural attributes, reactivity, electronic properties, self -processing, and many other properties of GO can be addressed successfully using model complexes.