Aromatic interactions and rotational strengths within protein environment: An electronic structural study on β-lactamases from class A

Christo Christov, Tatyana Karabencheva-Christova, Alessio Lodola

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

β-Lactamases are important enzymes, responsible for bacterial resistance against β-lactam antibiotics. The enzymes from class A are the most common and the most intensively studied. Here we present our electronic structural study on the relationships between electrostatic interactions and chiroptical properties of three enzymes from class A in the following directions: (i) an integrated influence of environment and ionization state on the rotational strengths mechanisms of tyrosine chromophore in TEM-1 β-lactamase; (ii) an effect of electrostatic environment on the mechanisms of aromatic rotational strengths in β-lactamases from Streptomyces albus and Staphylococcus aureus.
Original languageEnglish
Pages (from-to)89-95
JournalChemical Physics Letters
Volume456
Issue number1-3
DOIs
Publication statusPublished - 2008

Fingerprint Dive into the research topics of 'Aromatic interactions and rotational strengths within protein environment: An electronic structural study on β-lactamases from class A'. Together they form a unique fingerprint.

Cite this