Journal of the American Chemical Society, volume 129, issue 43, pages 13035-13042
An opsin shift in rhodopsin: Retinal S0-S1 excitation in protein, in solution, and in the gas phase
Publication type: Journal Article
Publication date: 2007-10-01
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 15
ISSN: 00027863, 15205126
General Chemistry
Catalysis
Biochemistry
Colloid and Surface Chemistry
Abstract
We considered a series of model systems for treating the photoabsorption of the 11-cis retinal chromophore in the protonated Schiff-base form in vacuum, solutions, and the protein environment. A high computational level, including the quantum mechanical-molecular mechanical (QM/MM) approach for solution and protein was utilized in simulations. The S0-S1 excitation energies in quantum subsystems were evaluated by means of an augmented version of the multiconfigurational quasidegenerate perturbation theory (aug-MCQDPT2) with the ground-state geometry parameters optimized in the density functional theory PBE0/cc-pVDZ approximation. The computed positions of absorption bands lambdamax, 599(g), 448(s), and 515(p) nm for the gas phase, solution, and protein, respectively, are in excellent agreement with the corresponding experimental data, 610(g), 445(s), and 500(p) nm. Such consistency provides a support for the formulated qualitative conclusions on the role of the chromophore geometry, environmental electrostatic field, and the counterion in different media. An essentially nonplanar geometry conformation of the chromophore group in the region of the C14-C15 bond was obtained for the protein, in particular, owing to the presence of the neighboring charged amino acid residue Glu181. Nonplanarity of the C14-C15 bond region along with the influence of the negatively charged counterions Glu181 and Glu113 are found to be important to reproduce the spectroscopic features of retinal chromophore inside the Rh cavity. Furthermore, the protein field is responsible for the largest bond-order decrease at the C11-C12 double bond upon excitation, which may be the reason for the 11-cis photoisomerization specificity.
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5
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- We do not take into account publications that without a DOI.
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Bravaya K. et al. An opsin shift in rhodopsin: Retinal S0-S1 excitation in protein, in solution, and in the gas phase // Journal of the American Chemical Society. 2007. Vol. 129. No. 43. pp. 13035-13042.
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Bravaya K., Bochenkova A. V., Granovsky A., Nemukhin A. An opsin shift in rhodopsin: Retinal S0-S1 excitation in protein, in solution, and in the gas phase // Journal of the American Chemical Society. 2007. Vol. 129. No. 43. pp. 13035-13042.
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TY - JOUR
DO - 10.1021/ja0732126
UR - https://doi.org/10.1021%2Fja0732126
TI - An opsin shift in rhodopsin: Retinal S0-S1 excitation in protein, in solution, and in the gas phase
T2 - Journal of the American Chemical Society
AU - Granovsky, Alexander
AU - Bravaya, Ksenia B.
AU - Bochenkova, Anastasia V.
AU - Nemukhin, Alexander
PY - 2007
DA - 2007/10/01 00:00:00
PB - American Chemical Society (ACS)
SP - 13035-13042
IS - 43
VL - 129
SN - 0002-7863
SN - 1520-5126
ER -
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@article{2007_Bravaya
author = {Alexander Granovsky and Ksenia B. Bravaya and Anastasia V. Bochenkova and Alexander Nemukhin},
title = {An opsin shift in rhodopsin: Retinal S0-S1 excitation in protein, in solution, and in the gas phase},
journal = {Journal of the American Chemical Society},
year = {2007},
volume = {129},
publisher = {American Chemical Society (ACS)},
month = {oct},
url = {https://doi.org/10.1021%2Fja0732126},
number = {43},
pages = {13035--13042},
doi = {10.1021/ja0732126}
}
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MLA
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Bravaya, Ksenia B., et al. “An opsin shift in rhodopsin: Retinal S0-S1 excitation in protein, in solution, and in the gas phase.” Journal of the American Chemical Society, vol. 129, no. 43, Oct. 2007, pp. 13035-13042. https://doi.org/10.1021%2Fja0732126.