TY  - JOUR
A1  - Muders, Vera
A1  - Kerruth, Silke
A1  - Lórenz-Fonfría, Víctor A.
A1  - Bamann, Christian
A1  - Heberle, Joachim
A1  - Schlesinger, Ramona
T1  - Resonance Raman and FTIR spectroscopic characterization of the closed and open states of channelrhodopsin-1
T2  - FEBS Letters
N2  - 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.
KW  - CaChR1
KW  - Channelrhodopsin
KW  - Optogenetics
KW  - Photoreceptor
KW  - Resonance Raman spectroscopy
KW  - Retinal
Y1  - 2014
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/34978
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-349784
SN  - 1873-3468
SN  - 0014-5793
N1  - (c) 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/).
VL  - 588
IS  - 14
SP  - 2301
EP  - 2306
PB  - Elsevier
CY  - Amsterdam [u.a.]
ER  -