Bimetaalic cores are versatile at metallobiosites and model studies using simple dinuclear complexes are becoming important. Recent recognition of heterodinuclear cores at the active sites of purple acid phosphatase (ZnFe), human calcineurin (ZnFe) and human protein phosphatase 1 (MnFe) has prompted us to provide structural models of phosphate adduct in those heterobimetallic phosphatases. We report here a diphenoxo-bridged heterodinuclear Zn(II)Pb(II) complex that hydrolyzes tris(p-nitro - phenyl)phosphate (TNP) to give a bis(p-nitrophenyl)phosphate (BNP) adduct of the complex.The phenol-based dinucleating macrocycle (L) 2 - , having two dissimilar metal-binding sites of N 2 O 2 and N 3 O 2 donor sets, forms a heterodinuclear Zn(II)Pb(II) complex, [ZnPb(L)(OH)]-ClO 4 H 2 O (abbreviated as ZnPb(OH)). The reaction of ZnPb(OH) with TNP in a methanolic solution resulted in the formation of [ZnPb(L)(BNP)]ClO 4 (ZnPb(BNP)). This suggests the hydrolysis of TNP to BNP in the process. It has been shown based on X-ray crystallography that in the adduct the Zn(II) and Pb(II) ions are bridged by the BNP.