A novel asymmetric di-Ni(II) system as a highly efficient functional model for phosphodiesterase: synthesis, structures, physicochemical properties and catalytic kinetics

A novel asymmetric phenol-based 'end-off' dinucleating ligand 2-{(2-piperidylmethyl)amino]methyl}-4-bromo-6-(1-methylhomopiperazine-4-yl)methyl]phenol (HL) and three dinuclear nickel(II) complexes, Ni?L(μ-OH)] (ClO?)? (1), Ni?L(DNBA)?(CH?CN)?]BPh? (2) and Ni?L(BPP)?(CH?CN)?]BPh? (3) have been synthesized and characterized by a variety of techniques including: NMR, infrared and UV-vis spectroscopies, mass spectrometry, elemental analysis, molar conductivity, thermal analysis, magnetochemistry and single-crystal X-ray diffractometry. The UV-vis spectrum of complex 1 exhibits a strong peak at 510 nm, a characteristic absorption of a d-d transition of the square-planar four-coordinated Ni(II) center. Utilizing this feature, the stepwise formation of mono- and dinickel centers in solution can be monitored. Phosphodiesterase activity of a dinuclear Ni(II) system (complex 1), formed in situ by a 2?:?1 mixture of Ni(2+) ions and the ligand HL, was investigated using bis(4-nitrophenyl)phosphate (BNPP) as the substrate. The pH dependence of the BNPP cleavage in water-ethanol (1?:?1, v/v) reveals a bell-shaped pH-k(obs) profile with an optimum at about pH 8.3 which is parallel to the formation of the dinuclear species Ni?L(μ-OH)](2+), according to the increase of the peak at 510 nm in the UV-vis absorption spectrum . These studies reveal that the di-Ni(II) system shows the highest catalytic activity reported so far, with an acceleration rate 1.28 × 10? times faster than the uncatalyzed reaction. The bridging hydroxyl group in Ni?L(μ-OH)](2+) is responsible for the hydrolysis reaction. The possible mechanism for the BNPP cleavage promoted by di-Ni(II) system is proposed on the basis of kinetic and spectral analyses. This study provides a less common example of the asymmetric phosphodiesterase model, which is like the active sites of most native metallohydrolases.