Asymmetric dinuclear metal complexes as models for active sites in hydrolases and redox enzymes

Recent advances in the synthesis of biomimetic asymmetric dinuclear transition metal complexes are reviewed. Emphasis is put on description of asymmetric model complexes for the active sites of the enzymes purple acid phosphatase, zinc phosphotriesterase, urease, Cu, Zn superoxide dismutase, tyrosinase, and catechol oxidase.