The dinuclear complex [Zn₂(DPCPMP)(pivalate)](ClO₄), where DPCPMP is the new unsymmetrical ligand [2-(N-(3-((bis((pyridin-2-yl) methyl)amino)methyl)-2-hydroxy-5-methylbenzyl)-N-((pyridin-2-yl)methyl)amino) acetic acid], has been synthesized and characterized. The complex is a functional model for zinc phosphoesterases with dinuclear active sites. The hydrolytic efficacy of the complex has been investigated using bis-(2,4-dinitrophenyl)phosphate (BDNPP), a DNA analog, as substrate. Speciation studies using potentiometric titrations have been performed for both the ligand and the corresponding dizinc complex to elucidate the formation of the active hydrolysis catalyst; they reveals that the dinuclear zinc(II) complexes, [Zn₂(DPCPMP)]^{2 +} and [Zn₂(DPCPMP)(OH)] ⁺ predominate the solution above pH 4. The relatively high pK _a of 8.38 for water deprotonation suggests that a terminal hydroxide complex is formed. Kinetic investigations of BDNPP hydrolysis over the pH range 5.5-11.0 and with varying metal to ligand ratio (metal salt:ligand = 0.5:1 to 3:1) have been performed. Variable temperature studies gave the activation parameters ΔH^‡ = 95.6 kJ mol^{- 1}, ΔS^‡ = - 44.8 J mol^{- 1} K^{- 1}, and ΔG^‡ = 108.0 kJ mol^{- 1}. The cumulative results indicate the hydroxido-bridged dinuclear Zn(II) complex [Zn₂(DPCPMP) (μ-OH)]⁺ as the effective catalyst. The mechanism of hydrolysis has been probed by computational modeling using density functional theory (DFT). Calculations show that the reaction goes through one concerted step (S _N2 type) in which the bridging hydroxide in the transition state becomes terminal and performs a nucleophilic attack on the BDNPP phosphorus; the leaving group dissociates simultaneously in an overall inner sphere type activation. The calculated free energy barrier is in good agreement with the experimentally determined activation parameters.