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Exploring antibiotic resistant mechanism by microcalorimetry

Determination of thermokinetic parameters of metallo-β-lactamase L1 catalyzing penicillin G hydrolysis

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Abstract

In an effort to probe the reaction of antibiotic hydrolysis catalyzed by B3 metallo-β-lactamase (MβL), the thermodynamic parameters of penicillin G hydrolysis catalyzed by MβL L1 from Stenotrophomonas maltophilia were determined by microcalorimetric method. The values of activation free energy ΔG θ≠ are 88.26, 89.44, 90.49, and 91.57 kJ mol−1 at 293.15, 298.15, 303.15, and 308.15 K, respectively, activation enthalpy ΔH θ≠ is 24.02 kJ mol−1, activation entropy ΔS θ≠ is −219.2511 J mol−1 K−1, apparent activation energy E is 26.5183 kJ mol−1, and the reaction order is 1.0. The thermodynamic parameters reveal that the penicillin G hydrolysis catalyzed by MβL L1 is an exothermic and spontaneous reaction.

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Acknowledgements

This work was supported by grants (to K. W. Y) from National Natural Science Fund of China (20972127), Doctoral Fund of China (200806970005), Natural Science Fund of Shaanxi Province (2009JM2002) and Key Fund for International Cooperation of Shaanxi Province (2010KW-16).

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Authors and Affiliations

  1. Key Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of Education, College of Chemistry and Materials Science, Northwest University, Xi’an, 710069, People’s Republic of China

    Hui-Zhou Gao, Qi Yang, Xiao-Yan Yan, Zhu-Jun Wang, Ji-Li Feng, Xia Yang, Sheng-Li Gao, Lei Feng, Xu Cheng, Chao Jia & Ke-Wu Yang

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  1. Hui-Zhou Gao
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  2. Qi Yang
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  3. Xiao-Yan Yan
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Correspondence to Ke-Wu Yang.

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Gao, HZ., Yang, Q., Yan, XY. et al. Exploring antibiotic resistant mechanism by microcalorimetry. J Therm Anal Calorim 107, 321–324 (2012). https://doi.org/10.1007/s10973-011-1362-7

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  • DOI: https://doi.org/10.1007/s10973-011-1362-7

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