% IMPORTANT: The following is UTF-8 encoded. This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.
@ARTICLE{Vierock:283048,
author = {Vierock, Johannes and Kaufmann, Joel C D and Faiß, Lukas
and Tillert, Linda and Krause, Benjamin S and Fischer, Paul
and Nguyen, Thi Bich Thao and Schmitz, Dietmar and Rost,
Benjamin R and Bartl, Franz and Hegemann, Peter},
title = {{M}ulticolor photoreactions of the red light-activated
channelrhodopsin {C}hrimson.},
journal = {Proceedings of the National Academy of Sciences of the
United States of America},
volume = {122},
number = {52},
issn = {0027-8424},
address = {Washington, DC},
publisher = {National Acad. of Sciences},
reportid = {DZNE-2025-01455},
pages = {e2513375122},
year = {2025},
abstract = {Channelrhodopsins are light-gated ion channels that are
used in modern neurosciences for the precise control of
cellular ion fluxes by light. With a peak absorption at 585
nm, Chrimson is the most red-shifted cation-conducting ChR.
It is frequently employed in multicolor experiments
alongside blue light-sensitive optogenetic tools and is so
far the only light-gated ion channel successfully applied in
human vision restoration. However, its photoresponses to
different wavelengths have not been thoroughly
characterized. In this study, we identify multiple
interconvertible dark states of Chrimson with distinct
absorption and photokinetic properties. Combining
electrophysiology and spectroscopy with optogenetic
experiments in neurons, we unveil that this dark state
heterogeneity is based on distinct protonation dynamics of
the counterion complex and alternative retinal
isomerization. In neurons, prolonged red illumination
reduces Chrimson's red light sensitivity, which is reflected
by a blue shift of the action spectrum. Blue light pulses
reverse this shift and increase the excitability in
subsequent red-light flashes. This understanding of
wavelength-dependent photoreactions in Chrimson will improve
the design of multicolor optogenetic experiments and inform
strategies for optimizing Chrimson for therapeutic
applications.},
keywords = {Channelrhodopsins: metabolism / Channelrhodopsins:
chemistry / Channelrhodopsins: genetics / Light /
Optogenetics: methods / Neurons: metabolism / Neurons:
radiation effects / Humans / Animals / HEK293 Cells / Red
Light / Chrimson (Other) / FTIR spectroscopy (Other) /
channelrhodopsins (Other) / optogenetics (Other) / retinal
prosthesis (Other) / Channelrhodopsins (NLM Chemicals)},
cin = {AG Schmitz},
ddc = {500},
cid = {I:(DE-2719)1810004},
pnm = {351 - Brain Function (POF4-351)},
pid = {G:(DE-HGF)POF4-351},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:41428877},
doi = {10.1073/pnas.2513375122},
url = {https://pub.dzne.de/record/283048},
}