TY - JOUR
T1 - Aromatic interactions and rotational strengths within protein environment: An electronic structural study on β-lactamases from class A
AU - Christov, Christo
AU - Karabencheva-Christova, Tatyana
AU - Lodola, Alessio
PY - 2008
Y1 - 2008
N2 - 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.
AB - 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.
U2 - 10.1016/j.cplett.2008.03.012
DO - 10.1016/j.cplett.2008.03.012
M3 - Article
SN - 0009-2614
VL - 456
SP - 89
EP - 95
JO - Chemical Physics Letters
JF - Chemical Physics Letters
IS - 1-3
ER -