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How does electron exchange correlation influence reactivity of metallo-β-lactamase L1 against cephalosporin antibioticsстатья
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 15 февраля 2024 г.
- Авторы: Levina Elena, Tsirelson Vladimir
- Журнал: Chemical Physics
- Том: 566
- Год издания: 2023
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Номер статьи: 111774
- DOI: 10.1016/j.chemphys.2022.111774
- Аннотация: Cephalosporin hydrolysis by the metallo-β-lactamase L1 is a reaction where electron delocalization in thesubstrate-protein complex affects the reaction rate: the more cephalosporin lone pairs are localized on the Natom, the higher hydrolysis rates are. We show that high Fermi hole variability is responsible for the stipulationof the electron lone pairs’ localization. One-electron potentials reveal that higher lone pairs’ localization isexpressed in the dominance of the static exchange correlation (reflected in the average Fermi hole depth) inthe N atom vicinity. However, this dominance was found to be defined by the height of the kinetic exchangepotential barriers (expressing the Fermi hole variability and the response of the exchange correlation hidden inthe kinetic potential to electron density variations), rather than by the features of the static exchange correlationitself. The need to account both static and kinetic exchange correlations for the reliable description of theelectron delocalization explains inapplicability of the simple geometric criteria for the chemical bonding study in considred systems.
- Добавил в систему: Цирельсон Владимир Григорьевич