Modeling the Active Site of the Purple Acid Phosphatase Enzyme with Hetero-Dinuclear Mixed Valence M(II)–Fe(III) [M = Zn, Ni, Co, and Cu] Complexes Supported over a [N(6)O] Unsymmetrical Ligand

[Image: see text] The active site of the purple acid phosphatase enzyme has been successfully modeled by a series of hetero-dinuclear M(II)–Fe(III) [M = Zn, Ni, Co, and Cu] type complexes of an unsymmetrical [N(6)O] ligand that contained a bridging phenoxide moiety and one imidazoyl and three pyridyl moieties as the terminal N-binding sites. In particular, the hetero-dinuclear complexes, {L[M(II)(μ-OAc)(2)Fe(III)]}(ClO(4))(2) [M = Zn (3a), Ni (3b), Co (4a), and Cu (4b)], were obtained directly from the phenoxy-bridged ligand (HL), namely 2-{[bis(2-methylpyridyl)amino]methyl}-6-{[((1-methylimidazol-2-yl)methyl)(2-pyridylmethyl)amino]methyl}-4-t-butylphenol (2), upon sequential addition of Fe(ClO(4))(3)·XH(2)O and M(ClO(4))(2)·6H(2)O (M = Zn and Ni) or M(OAc)(2)·XH(2)O (M = Co and Cu), in a low-to-moderate (ca. 32–53%) yield. The temperature-dependent magnetic susceptibility measurements indicated weak antiferromagnetic coupling interactions occurring between the two metal centers in their high-spin states. All of the 3(a–b) and 4(a–b) complexes successfully carried out the hydrolysis of the bis(2,4-dinitrophenyl)phosphate (2,4-BDNPP) substrate in a mixed CH(3)CN/H(2)O (v/v 1:1) medium in the pH range of 5.5–10.5 at room temperature, thereby mimicking the functional activity of the native enzyme. The spectrophotometric titration suggested a monoaquated and dihydroxo species of the type {L[(H(2)O)M(II)(μ-OH)Fe(III)(OH)]}(2+) to be the catalytically active species for the phosphodiester hydrolysis reaction within the pH range of ca. 5.80–7.15. Last, the kinetic studies on the hydrolysis of the model substrate, 2,4-BDNPP, divulge a Michaelis–Menten-type behavior for all complexes.