Open Access
Nature Communications, volume 10, issue 1, publication number 1210
Intrinsic photoisomerization dynamics of protonated Schiff-base retinal
Publication type: Journal Article
Publication date: 2019-03-14
Journal:
Nature Communications
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 16.6
ISSN: 20411723
PubMed ID:
30872581
General Chemistry
General Biochemistry, Genetics and Molecular Biology
General Physics and Astronomy
Abstract
The retinal protonated Schiff-base (RPSB) in its all-trans form is found in bacterial rhodopsins, whereas visual rhodopsin proteins host 11-cis RPSB. In both cases, photoexcitation initiates fast isomerization of the retinal chromophore, leading to proton transport, storage of chemical energy or signaling. It is an unsolved problem, to which degree this is due to protein interactions or intrinsic RPSB quantum properties. Here, we report on time-resolved action-spectroscopy studies, which show, that upon photoexcitation, cis isomers of RPSB have an almost barrierless fast 400 fs decay, whereas all-trans isomers exhibit a barrier-controlled slow 3 ps decay. Moreover, formation of the 11-cis isomer is greatly favored for all-trans RPSB when isolated. The very fast photoresponse of visual photoreceptors is thus directly related to intrinsic retinal properties, whereas bacterial rhodopsins tune the excited state potential-energy surface to lower the barrier for particular double-bond isomerization, thus changing both the timescale and specificity of the photoisomerization.The primary photoresponse of protonated Schiff-base retinal in visual and bacterial rhodopsins is fast sub-ps isomerisation. Here, the authors show that the fast photoisomerization of rhodopsin is related to an intrinsic retinal property, whereas bacterial rhodopsins tune the excited-state potential-energy surface and improve the isomerization timescale and specificity.
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Kiefer H. V. et al. Intrinsic photoisomerization dynamics of protonated Schiff-base retinal // Nature Communications. 2019. Vol. 10. No. 1. 1210
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Kiefer H. V., Gruber E., Langeland J., Kusochek P. A., Bochenkova A. V., Andersen L. P. Intrinsic photoisomerization dynamics of protonated Schiff-base retinal // Nature Communications. 2019. Vol. 10. No. 1. 1210
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TY - JOUR
DO - 10.1038/s41467-019-09225-7
UR - https://doi.org/10.1038%2Fs41467-019-09225-7
TI - Intrinsic photoisomerization dynamics of protonated Schiff-base retinal
T2 - Nature Communications
AU - Kiefer, H. V.
AU - Gruber, Elisabeth
AU - Langeland, Jeppe
AU - Kusochek, Pavel A
AU - Bochenkova, Anastasia V.
AU - Andersen, L P
PY - 2019
DA - 2019/03/14 00:00:00
PB - Springer Nature
IS - 1
VL - 10
PMID - 30872581
SN - 2041-1723
ER -
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@article{2019_Kiefer,
author = {H. V. Kiefer and Elisabeth Gruber and Jeppe Langeland and Pavel A Kusochek and Anastasia V. Bochenkova and L P Andersen},
title = {Intrinsic photoisomerization dynamics of protonated Schiff-base retinal},
journal = {Nature Communications},
year = {2019},
volume = {10},
publisher = {Springer Nature},
month = {mar},
url = {https://doi.org/10.1038%2Fs41467-019-09225-7},
number = {1},
doi = {10.1038/s41467-019-09225-7}
}