Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization

Vibrational dynamics of the retinal all-trans to 13-cis photoisomerization in channelrhodopsin-1 from Chlamydomonas augustae (CaChR1) was investigated by femtosecond visible pump mid-IR probe spectroscopy. After photoexcitation, the transient infrared absorption of C-C stretching modes was detected....

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Main Authors: T. Stensitzki, Y. Yang, V. Muders, R. Schlesinger, J. Heberle, K. Heyne
Format: Article
Language:English
Published: AIP Publishing LLC and ACA 2016-07-01
Series:Structural Dynamics
Online Access:http://dx.doi.org/10.1063/1.4948338
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author T. Stensitzki
Y. Yang
V. Muders
R. Schlesinger
J. Heberle
K. Heyne
author_facet T. Stensitzki
Y. Yang
V. Muders
R. Schlesinger
J. Heberle
K. Heyne
author_sort T. Stensitzki
collection DOAJ
description Vibrational dynamics of the retinal all-trans to 13-cis photoisomerization in channelrhodopsin-1 from Chlamydomonas augustae (CaChR1) was investigated by femtosecond visible pump mid-IR probe spectroscopy. After photoexcitation, the transient infrared absorption of C-C stretching modes was detected. The formation of the 13-cis photoproduct marker band at 1193 cm−1 was observed within the time resolution of 0.3 ps. We estimated the photoisomerization yield to (60 ± 6) %. We found additional time constants of (0.55 ± 0.05) ps and (6 ± 1) ps, assigned to cooling, and cooling processes with a back-reaction pathway. An additional bleaching band demonstrates the ground-state heterogeneity of retinal.
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spelling doaj.art-81f0c3d225fc47a4bc3a1afec9c8ccb02022-12-21T19:12:24ZengAIP Publishing LLC and ACAStructural Dynamics2329-77782016-07-0134043208043208-810.1063/1.4948338021693SDYFemtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerizationT. Stensitzki0Y. Yang1V. Muders2R. Schlesinger3J. Heberle4K. Heyne5 Department of Physics, Institute of Experimental Physics, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany Department of Physics, Institute of Experimental Physics, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany Genetic Biophysics, Department of Physics, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany Genetic Biophysics, Department of Physics, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany Experimental Molecular Biophysics, Department of Physics, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany Department of Physics, Institute of Experimental Physics, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, GermanyVibrational dynamics of the retinal all-trans to 13-cis photoisomerization in channelrhodopsin-1 from Chlamydomonas augustae (CaChR1) was investigated by femtosecond visible pump mid-IR probe spectroscopy. After photoexcitation, the transient infrared absorption of C-C stretching modes was detected. The formation of the 13-cis photoproduct marker band at 1193 cm−1 was observed within the time resolution of 0.3 ps. We estimated the photoisomerization yield to (60 ± 6) %. We found additional time constants of (0.55 ± 0.05) ps and (6 ± 1) ps, assigned to cooling, and cooling processes with a back-reaction pathway. An additional bleaching band demonstrates the ground-state heterogeneity of retinal.http://dx.doi.org/10.1063/1.4948338
spellingShingle T. Stensitzki
Y. Yang
V. Muders
R. Schlesinger
J. Heberle
K. Heyne
Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization
Structural Dynamics
title Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization
title_full Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization
title_fullStr Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization
title_full_unstemmed Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization
title_short Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization
title_sort femtosecond infrared spectroscopy of channelrhodopsin 1 chromophore isomerization
url http://dx.doi.org/10.1063/1.4948338
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