Keywords: Zn II Fe III complex / Fe II Fe III complex / Purple acid phosphatases / Phosphate ester hydrolysisThe heterodinuclear Zn II Fe III complex 1 and the isostructural Fe II Fe III complex 2 with the dinucleating ligand from 2,6-bis[{bis(2-pyridylmethyl)amino}methyl]-4-methoxyphenol (HBPMOP, 3) were prepared and characterized by X-ray crystallography. Solution studies (UV/Vis spectroscopy; electrochemistry) are described. A pH-induced change in the coordination spheres of the metal centers is seen. These complexes serve as models for the mixed-valence oxidation state in purple acid phosphatases. The cleavage acceleration of the activated phosphodiester 2-hydroxypropyl p-nitrophenyl

The first (μ-oxo)diiron(III) complex with one terminal hydroxide ligand at each iron has been structurally characterized, thus providing new information on Fe−OH bonds. Acid/base equilibria were observed in aqueous solution, and the conjugate acid of the title complex was found to be a catalyst for hydrolysis of phosphodiesters at 50 °C, reinforcing the general idea about a synergistic effect in a dinuclear unit of a substrate binding site and a site containing a nucleophile. This effect has been proposed in the mechanism of purple acid phosphatase and other bimetallic hydrolases.

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