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Resonance Raman and FTIR spectroscopic characterization of the closed and open states of channelrhodopsin-1.

Muders, V; Kerruth, S; Lórenz-Fonfría, VA; Bamann, C; Heberle, J; Schlesinger, R (2014) Resonance Raman and FTIR spectroscopic characterization of the closed and open states of channelrhodopsin-1. FEBS Lett, 588 (14). pp. 2301-2306. ISSN 1873-3468 https://doi.org/10.1016/j.febslet.2014.05.019
SGUL Authors: Kerruth, Silke

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Abstract

Channelrhodopsin-1 from Chlamydomonas augustae (CaChR1) is a light-activated cation channel, which is a promising optogenetic tool. We show by resonance Raman spectroscopy and retinal extraction followed by high pressure liquid chromatography (HPLC) that the isomeric ratio of all-trans to 13-cis of solubilized channelrhodopsin-1 is with 70:30 identical to channelrhodopsin-2 from Chlamydomonas reinhardtii (CrChR2). Critical frequency shifts in the retinal vibrations are identified in the Raman spectrum upon transition to the open (conductive P2(380)) state. Fourier transform infrared spectroscopy (FTIR) spectra indicate different structures of the open states in the two channelrhodopsins as reflected by the amide I bands and the protonation pattern of acidic amino acids.

Item Type: Article
Additional Information: © 2014 The Authors. Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/3.0/).
Keywords: CaChR1, Channelrhodopsin, Optogenetics, Photoreceptor, Resonance Raman spectroscopy, Retinal, Chlamydomonas, Ion Channel Gating, Light, Plant Proteins, Protein Conformation, Retinaldehyde, Rhodopsin, Spectroscopy, Fourier Transform Infrared, Spectrum Analysis, Raman, Chlamydomonas, Retinaldehyde, Rhodopsin, Plant Proteins, Spectroscopy, Fourier Transform Infrared, Spectrum Analysis, Raman, Ion Channel Gating, Protein Conformation, Light, Biochemistry & Molecular Biology, 0601 Biochemistry And Cell Biology, 0304 Medicinal And Biomolecular Chemistry
SGUL Research Institute / Research Centre: Academic Structure > Molecular and Clinical Sciences Research Institute (MCS)
Journal or Publication Title: FEBS Lett
ISSN: 1873-3468
Language: eng
Dates:
DateEvent
27 June 2014Published
21 May 2014Published Online
9 May 2014Accepted
Publisher License: Creative Commons: Attribution-Noncommercial-No Derivative Works 3.0
PubMed ID: 24859039
Go to PubMed abstract
URI: https://openaccess.sgul.ac.uk/id/eprint/109127
Publisher's version: https://doi.org/10.1016/j.febslet.2014.05.019

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