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 [N₆O] Unsymmetrical Ligand.

ABSTRACT: 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 [N₆O] 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)₂Fe^III]}(ClO₄)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(ClO₄)₃

SUBMITTER: Pathak C 

PROVIDER: S-EPMC6641979 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature