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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....
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Crystallographic Association
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4851625/ https://www.ncbi.nlm.nih.gov/pubmed/27191011 http://dx.doi.org/10.1063/1.4948338 |
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author | Stensitzki, T. Yang, Y. Muders, V. Schlesinger, R. Heberle, J. Heyne, K. |
author_facet | Stensitzki, T. Yang, Y. Muders, V. Schlesinger, R. Heberle, J. Heyne, K. |
author_sort | Stensitzki, T. |
collection | PubMed |
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. |
format | Online Article Text |
id | pubmed-4851625 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | American Crystallographic Association |
record_format | MEDLINE/PubMed |
spelling | pubmed-48516252016-05-17 Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization Stensitzki, T. Yang, Y. Muders, V. Schlesinger, R. Heberle, J. Heyne, K. Struct Dyn SPECIAL TOPIC: THE HAMBURG CONFERENCE ON FEMTOCHEMISTRY (FEMTO12) 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. American Crystallographic Association 2016-04-29 /pmc/articles/PMC4851625/ /pubmed/27191011 http://dx.doi.org/10.1063/1.4948338 Text en © 2016 Author(s). 2329-7778/2016/3(4)/043208/8 All article content, except where otherwise noted, is licensed under a Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | SPECIAL TOPIC: THE HAMBURG CONFERENCE ON FEMTOCHEMISTRY (FEMTO12) Stensitzki, T. Yang, Y. Muders, V. Schlesinger, R. Heberle, J. Heyne, K. Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization |
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 |
topic | SPECIAL TOPIC: THE HAMBURG CONFERENCE ON FEMTOCHEMISTRY (FEMTO12) |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4851625/ https://www.ncbi.nlm.nih.gov/pubmed/27191011 http://dx.doi.org/10.1063/1.4948338 |
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