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