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Exploring antibiotic resistant mechanism by microcalorimetry.

Authors :
Gao, Hui-Zhou
Yang, Qi
Yan, Xiao-Yan
Wang, Zhu-Jun
Feng, Ji-Li
Yang, Xia
Gao, Sheng-Li
Feng, Lei
Cheng, Xu
Jia, Chao
Yang, Ke-Wu
Source :
Journal of Thermal Analysis & Calorimetry; Jan2012, Vol. 107 Issue 1, p321-324, 4p
Publication Year :
2012

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 Δ G are 88.26, 89.44, 90.49, and 91.57 kJ mol at 293.15, 298.15, 303.15, and 308.15 K, respectively, activation enthalpy Δ H is 24.02 kJ mol, activation entropy Δ S is −219.2511 J mol K, apparent activation energy E is 26.5183 kJ mol, 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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
13886150
Volume :
107
Issue :
1
Database :
Complementary Index
Journal :
Journal of Thermal Analysis & Calorimetry
Publication Type :
Academic Journal
Accession number :
69625200
Full Text :
https://doi.org/10.1007/s10973-011-1362-7