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作 者:Xia Yang Ya-Jun Zhou Pei He Yun-Hua Guo Cong-Jun Liu Ke-Wu Yang
出 处:《Chinese Chemical Letters》2014年第10期1323-1326,共4页中国化学快报(英文版)
基 金:supported by the National Natural Science Foundation of China (Nos.21272186 and 81361138018)
摘 要:In an effort to understand the recombination of a B2 metallo-β-lactamase(MβL),the binding of metals to apo-ImiS was studied by isothermal titration calorimetry and fluorescence spectra.The binding of Zn(Ⅱ),Co(Ⅱ) to apo-lmiS resulted in activation free energies △G_≠~θ values of 93.719 and 92.948 kJ mol^(-1),respectively,and increasing of fluorescence intensity at maxima emission of 340 nm.In an effort to understand the recombination of a B2 metallo-β-lactamase(MβL),the binding of metals to apo-ImiS was studied by isothermal titration calorimetry and fluorescence spectra.The binding of Zn(Ⅱ),Co(Ⅱ) to apo-lmiS resulted in activation free energies △G_≠~θ values of 93.719 and 92.948 kJ mol^(-1),respectively,and increasing of fluorescence intensity at maxima emission of 340 nm.
关 键 词:Antibiotic resistant bacteria Metallo-β-lactamases Metalloprotein recombinant Thermokinetic parameters
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