Journal of Physical Chemistry Letters, volume 12, issue 34, pages 8263-8271
Protonation States of Molecular Groups in the Chromophore-Binding Site Modulate Properties of the Reversibly Switchable Fluorescent Protein rsEGFP2
Publication type: Journal Article
Publication date: 2021-08-23
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 5.7
ISSN: 19487185
Physical and Theoretical Chemistry
General Materials Science
Abstract
The role of protonation states of the chromophore and its neighboring amino acid side chains of the reversibly switching fluorescent protein rsEGFP2 upon photoswitching is characterized by molecular modeling methods. Numerous conformations of the chromophore-binding site in computationally derived model systems are obtained using the quantum chemistry and QM/MM approaches. Excitation energies are computed using the extended multiconfigurational quasidegenerate perturbation theory (XMCQDPT2). The obtained structures and absorption spectra allow us to provide an interpretation of the observed structural and spectral properties of rsEGFP2 in the active ON and inactive OFF states. The results demonstrate that in addition to the dominating anionic and neutral forms of the chromophore, the cationic and zwitterionic forms may participate in the photoswitching of rsEGFP2. Conformations and protonation forms of the Glu223 and His149 side chains in the chromophore-binding site play an essential role in stabilizing specific protonation forms of the chromophore.
Citations by journals
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1
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Current Opinion in Structural Biology
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Current Opinion in Structural Biology
1 publication, 20%
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Journal of Physical Chemistry Letters
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Journal of Physical Chemistry Letters
1 publication, 20%
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Molecules
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Molecules
1 publication, 20%
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Journal of the American Chemical Society
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Journal of the American Chemical Society
1 publication, 20%
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Photosynthesis Research
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Photosynthesis Research
1 publication, 20%
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1
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Citations by publishers
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2
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American Chemical Society (ACS)
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American Chemical Society (ACS)
2 publications, 40%
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Elsevier
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Elsevier
1 publication, 20%
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Multidisciplinary Digital Publishing Institute (MDPI)
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Multidisciplinary Digital Publishing Institute (MDPI)
1 publication, 20%
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Springer Nature
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Springer Nature
1 publication, 20%
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1
2
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Grigorenko B. et al. Protonation States of Molecular Groups in the Chromophore-Binding Site Modulate Properties of the Reversibly Switchable Fluorescent Protein rsEGFP2 // Journal of Physical Chemistry Letters. 2021. Vol. 12. No. 34. pp. 8263-8271.
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Grigorenko B., Domratcheva T., Polyakov I. V., Nemukhin A. Protonation States of Molecular Groups in the Chromophore-Binding Site Modulate Properties of the Reversibly Switchable Fluorescent Protein rsEGFP2 // Journal of Physical Chemistry Letters. 2021. Vol. 12. No. 34. pp. 8263-8271.
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TY - JOUR
DO - 10.1021/acs.jpclett.1c02415
UR - https://doi.org/10.1021%2Facs.jpclett.1c02415
TI - Protonation States of Molecular Groups in the Chromophore-Binding Site Modulate Properties of the Reversibly Switchable Fluorescent Protein rsEGFP2
T2 - Journal of Physical Chemistry Letters
AU - Polyakov, Igor V.
AU - Nemukhin, Alexander
AU - Grigorenko, Bella
AU - Domratcheva, Tatiana
PY - 2021
DA - 2021/08/23 00:00:00
PB - American Chemical Society (ACS)
SP - 8263-8271
IS - 34
VL - 12
SN - 1948-7185
ER -
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@article{2021_Grigorenko,
author = {Igor V. Polyakov and Alexander Nemukhin and Bella Grigorenko and Tatiana Domratcheva},
title = {Protonation States of Molecular Groups in the Chromophore-Binding Site Modulate Properties of the Reversibly Switchable Fluorescent Protein rsEGFP2},
journal = {Journal of Physical Chemistry Letters},
year = {2021},
volume = {12},
publisher = {American Chemical Society (ACS)},
month = {aug},
url = {https://doi.org/10.1021%2Facs.jpclett.1c02415},
number = {34},
pages = {8263--8271},
doi = {10.1021/acs.jpclett.1c02415}
}
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Grigorenko, Bella, et al. “Protonation States of Molecular Groups in the Chromophore-Binding Site Modulate Properties of the Reversibly Switchable Fluorescent Protein rsEGFP2.” Journal of Physical Chemistry Letters, vol. 12, no. 34, Aug. 2021, pp. 8263-8271. https://doi.org/10.1021%2Facs.jpclett.1c02415.