Další formáty:
BibTeX
LaTeX
RIS
@article{1347769,
author = {Novotný, Jan and Bazzi, Sophia and Marek, Radek and Kozelka, Jiří},
article_number = {28},
doi = {http://dx.doi.org/10.1039/C6CP01524G},
keywords = {lone-pair-pi interaction; anion-pi; DFT; energy decomposition analysis},
language = {eng},
issn = {1463-9076},
journal = {Physical Chemistry Chemical Physics},
title = {Lone-pair–pi interactions: analysis of the physical origin and biolological implications},
url = {http://dx.doi.org/10.1039/C6CP01524G},
volume = {18},
year = {2016}
}
TY - JOUR
ID - 1347769
AU - Novotný, Jan - Bazzi, Sophia - Marek, Radek - Kozelka, Jiří
PY - 2016
TI - Lone-pair–pi interactions: analysis of the physical origin and biolological implications
JF - Physical Chemistry Chemical Physics
VL - 18
IS - 28
SP - 19472-19481
EP - 19472-19481
PB - Royal Society of Chemistry
SN - 14639076
KW - lone-pair-pi interaction
KW - anion-pi
KW - DFT
KW - energy decomposition analysis
UR - http://dx.doi.org/10.1039/C6CP01524G
L2 - http://dx.doi.org/10.1039/C6CP01524G
N2 - Lone-pair-pi (lp-pi) interactions have been suggested to stabilize DNA and protein structures, and to participate in the formation of DNA-protein complexes. To elucidate their physical origin, we have carried out a theoretical multi-approach analysis of two biologically relevant model systems, the water-indole and water-uracil complexes, which we compared with the structurally similar chloride-tetracyanobenzene (TCB) complex previously shown to contain a strong charge-transfer (CT) binding component. We demonstrate that the CT component in lp-pi interactions between water and indole/uracil is significantly smaller than that stabilizing the Cl-TCB reference system. The strong lp(Cl-)-pi(TCB)* orbital interaction is characterized by a small energy gap and an efficient lp-pi* overlap. In contrast, in lp-pi interactions between water and indole or uracil, the corresponding energy gap is larger and the overlap less efficient. As a result, water-uracil and water-indole interactions are weak forces composed by smaller contributions from electrostatics, polarization, dispersion, and charge transfer. In addition, indole exhibits a negative electrostatic potential at its pi-face, making lp-pi interactions less favorable than O-H···pi hydrogen bonding. Consequently, some of the water-tryptophan contacts observed in X-ray structures of proteins and previously interpreted as lp-pi interactions [Luisi et al., Proteins 2004, 57, 1-8], might in fact arise from O-H···pi hydrogen bonding.
ER -
NOVOTNÝ, Jan, Sophia BAZZI, Radek MAREK a Jiří KOZELKA. Lone-pair–pi interactions: analysis of the physical origin and biolological implications. \textit{Physical Chemistry Chemical Physics}. Royal Society of Chemistry, 2016, roč.~18, č.~28, s.~19472-19481. ISSN~1463-9076. Dostupné z: https://dx.doi.org/10.1039/C6CP01524G.
|
