Studies on PNPP Hydrolysis Catalyzed by Schiff Base Cobalt（Ⅱ） Complexes Containing Benzoaza-15-crown-5

Three novel Schiff base cobalt（Ⅱ） complexes containing benzoaza-15-crown-5, CoL^1, CoL^2 and CoL^3 were synthesized and characterized, and these complexes were used in catalytic hydrolysis of carboxylic ester （PNPP, p-nitrophenyl picolinate） as mimic hydrolytic metalloenzyme. The analysis of specific absorption spectra of the hydrolytic reaction systems indicated that the catalytic hydrolysis involved the key intermediates formed by PNPP with cobalt（Ⅱ） complexes. The CoL^3 bearing the electron withdrawing group shows better catalytic activity due to its stabilization effect on active species MLS^-. The catalytic mechanism of PNPP hydrolysis was also proposed. The kinetic parameter of PNPP catalytic hydrolysis has been calculated and the activation energy for the catalytic hydrolysis is 43.69, 39.76 and 35.44 kJ·mol^-1, respectively.     

猪肝DFP酸催化水解反应产物的等速电泳分析

DFP酸可催化水解二异丙基氟磷酸酯（DFP）分子中的P－F键,使其断裂产生磷酸二异丙基酯和HF。根据电位滴定法和离子选择电极法对猪肝中发现的两种DFP水解酶活力测定的结果,利用毛细管等速电泳分析仪对这两种酶催化DFP水解的产物进行了定性分析。结果表明,猪肝中小分子质量的酸催化DFP水解反应时,并非水解P－F键．而是水解P－OR键,说明该酶是一种催化DFP分子中磷酯健水解的磷酯酶。     

Organophosphate hydrolase — an enzyme catalyzing degradation of phosphorus-containing toxins and pesticides

The available investigations on the structure and properties of the enzyme organophosphate hydrolase exhibiting catalytic activity with respect to orthophosphates are reviewed. Recent data on the mechanism of enzymatic hydrolysis of paraoxon are surveyed. The role of two metal ions involved in the enzyme active site is considered. The substrate specificity and the influence of various inhibitors on the kinetic characteristics of the enzyme are discussed.     

1, 1, 1-三氨基甲基丙烷锌(Ⅱ)配合物模拟水解酶催化酯类水解研究

研究了1,1,1-三氨基甲基丙烷(Tamp)锌(Ⅱ)配合物作水解酶模拟物催化对硝基苯酚醋酸酯(NA)水解的动力学。结果表明催化水解速率对底物(NA)及配合物(Zntamp)浓度均呈一级反应,水解速率遵循速率方程dC/dt=(k