Vibronic dynamics of the ultrafast all-trans to 13-cis photoisomerization of retinal in channelrhodopsin-1

Channelrhodopsins are light-gated ion channels with extensive applications in optogenetics. Channelrhodopsin-1 from Chlamydomonas augustae (CaChR1) exhibits a red-shifted absorption spectrum as compared to Channelrhodopsin-2, which is highly beneficial for optogenetic application. The primary event...

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Main Authors: Schnedermann, C, Muders, V, Ehrenberg, D, Schlesinger, R, Kukura, P, Heberle, J
Format: Journal article
Language:English
Published: American Chemical Society 2016
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author Schnedermann, C
Muders, V
Ehrenberg, D
Schlesinger, R
Kukura, P
Heberle, J
author_facet Schnedermann, C
Muders, V
Ehrenberg, D
Schlesinger, R
Kukura, P
Heberle, J
author_sort Schnedermann, C
collection OXFORD
description Channelrhodopsins are light-gated ion channels with extensive applications in optogenetics. Channelrhodopsin-1 from Chlamydomonas augustae (CaChR1) exhibits a red-shifted absorption spectrum as compared to Channelrhodopsin-2, which is highly beneficial for optogenetic application. The primary event in the photocycle of CaChR1 involves an isomerization of the protein-bound retinal chromophore. Here, we apply highly time-resolved vibronic spectroscopy to reveal the electronic and structural dynamics associated with the first step of the photocycle of CaChR1. We observe vibrationally coherent formation of the P1 intermediate exhibiting a twisted 13-cis retinal with a 110 ± 7 fs time constant. Comparison with low-temperature resonance Raman spectroscopy of the corresponding trapped photoproduct demonstrates that this rapidly formed P1 intermediate is stable for several hundreds of nanoseconds.
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spelling oxford-uuid:c48089f7-7db1-442c-a47c-4e20b1d55ce32022-03-27T06:23:51ZVibronic dynamics of the ultrafast all-trans to 13-cis photoisomerization of retinal in channelrhodopsin-1Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:c48089f7-7db1-442c-a47c-4e20b1d55ce3EnglishSymplectic Elements at OxfordAmerican Chemical Society2016Schnedermann, CMuders, VEhrenberg, DSchlesinger, RKukura, PHeberle, JChannelrhodopsins are light-gated ion channels with extensive applications in optogenetics. Channelrhodopsin-1 from Chlamydomonas augustae (CaChR1) exhibits a red-shifted absorption spectrum as compared to Channelrhodopsin-2, which is highly beneficial for optogenetic application. The primary event in the photocycle of CaChR1 involves an isomerization of the protein-bound retinal chromophore. Here, we apply highly time-resolved vibronic spectroscopy to reveal the electronic and structural dynamics associated with the first step of the photocycle of CaChR1. We observe vibrationally coherent formation of the P1 intermediate exhibiting a twisted 13-cis retinal with a 110 ± 7 fs time constant. Comparison with low-temperature resonance Raman spectroscopy of the corresponding trapped photoproduct demonstrates that this rapidly formed P1 intermediate is stable for several hundreds of nanoseconds.
spellingShingle Schnedermann, C
Muders, V
Ehrenberg, D
Schlesinger, R
Kukura, P
Heberle, J
Vibronic dynamics of the ultrafast all-trans to 13-cis photoisomerization of retinal in channelrhodopsin-1
title Vibronic dynamics of the ultrafast all-trans to 13-cis photoisomerization of retinal in channelrhodopsin-1
title_full Vibronic dynamics of the ultrafast all-trans to 13-cis photoisomerization of retinal in channelrhodopsin-1
title_fullStr Vibronic dynamics of the ultrafast all-trans to 13-cis photoisomerization of retinal in channelrhodopsin-1
title_full_unstemmed Vibronic dynamics of the ultrafast all-trans to 13-cis photoisomerization of retinal in channelrhodopsin-1
title_short Vibronic dynamics of the ultrafast all-trans to 13-cis photoisomerization of retinal in channelrhodopsin-1
title_sort vibronic dynamics of the ultrafast all trans to 13 cis photoisomerization of retinal in channelrhodopsin 1
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