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Modeling the Transient Kinetics of the L1 Metallo-β-Lactamase by Maria G. Khrenova; Alexander V. Nemukhin is a Chemistry article available to read on EtoBox.

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The transient absorption spectroscopy of hydrolysis of the chromogenic substrate nitrocefin by the L1 metallo-β-lactamase (MβL), a bacterial enzyme responsible for destruction of β-lactam antibiotics molecules, showed formation and decay of a plausible red-shifted reaction intermediate. We propose a mechanism of this important reaction consistent with the transient kinetic data. Quantum mechanics/molecular mechanics (QM/MM) simulations of the reaction pathway revealed occurrence of two reaction intermediates (I1, I2) between the enzyme-substrate (ES) and enzymeproduct (EP) complexes. The vertical S 0 -S 1 transition energies calculated at the minimum energy structures (ES, I1, I2, EP) using the time dependent DFT (TD-DFT) method allowed us to assign the experimental absorption bands to all reacting species. We numerically solved the equations of chemical kinetics with the rate constants of all elementary steps evaluated with the transition state theory and simulated the kinetic curves as well as the evolution of the absorption bands of ES, I2 and EP. Direct comparison to the experimental data allowed us to identify the I2 intermediate as the transient red-shifted species detected e

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Author

Maria G. Khrenova; Alexander V. Nemukhin

Publisher

American Chemical Society (ACS)

Published

2018

Language

EN

Field

Chemistry (Physical Sciences)