Dinuclear nickel(II) complexes as models for the active of urease

Yamane, Heitaro; Hosokawa, Y.; Nakao, Y.; Matsumoto, Keiji; Takamizawa, Satoshi; Mori, Wasuke; Suzuki, Shuichi

doi:10.1016/s0162-0134(97)80063-3

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“…Several previous studies focused on the phosphatase-like activity of di-Ni(II) complexes (Table 3 and Scheme 1 ; Yamaguchi et al, 1997 , 2001 ; Yamane et al, 1997 , 2001 ; Parimala and Kandaswamy, 2003 ; Jikido et al, 2005 ; Greatti et al, 2008 ; Ren et al, 2011 ; Piovezan et al, 2012 ; Wu and Wang, 2014 ; Massoud et al, 2016 ; Xavier and Neves, 2016 ). In a number of cases the experimental conditions in terms of solvent (acetonitrile/aqueous buffer) and substrate (BDNPP) were similar to those employed in the present work, although the pH at which the k cat and K m values were determined did vary, making direct comparisons difficult (Greatti et al, 2004 , 2008 ; Piovezan et al, 2012 ; Massoud et al, 2016 ; Xavier and Neves, 2016 ).…”

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confidence: 99%

Synthesis, Magnetic Properties, and Catalytic Properties of a Nickel(II)-Dependent Biomimetic of Metallohydrolases

et al. 2018

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A dinickel(II) complex of the ligand 1,3-bis(bis(pyridin-2-ylmethyl)amino)propan-2-ol (HL1) has been prepared and characterized to generate a functional model for nickel(II) phosphoesterase enzymes. The complex, [Ni2(L1)(μ-OAc)(H2O)2](ClO4)2·H2O, was characterized by microanalysis, X-ray crystallography, UV-visible, and IR absorption spectroscopy and solid state magnetic susceptibility measurements. Susceptibility studies show that the complex is antiferromagnetically coupled with the best fit parameters J = −27.4 cm−1, g = 2.29, D = 28.4 cm−1, comparable to corresponding values measured for the analogous dicobalt(II) complex [Co2(L1)(μ-OAc)](ClO4)2·0.5 H2O (J = −14.9 cm−1 and g = 2.16). Catalytic measurements with the diNi(II) complex using the substrate bis(2,4-dinitrophenyl)phosphate (BDNPP) demonstrated activity toward hydrolysis of the phosphoester substrate with Km ~10 mM, and kcat ~0.025 s−1. The combination of structural and catalytic studies suggests that the likely mechanism involves a nucleophilic attack on the substrate by a terminal nucleophilic hydroxido moiety.

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