ArticleProceedings of the National Academy of Sciences of the United States of America2016
Photochemical reaction cycle transitions during anion channelrhodopsin gating.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 65 citations in OpenAlex.
- Tutorial: Transient Absorption Spectroscopy for Probing Ultrafast Dynamics.ACS physical chemistry Au · 2026Article
- Val109 and Ile170 contribute to channel function in Guillardia theta-derived anion channelrhodopsins.Scientific reports · 2026Article
- Apusomonad rhodopsins: A new family of ultraviolet to blue light-absorbing rhodopsin channels.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- A second photoactivatable state of the anion-conducting channelrhodopsin GtACR1 empowers persistent activity.Communications biology · 2025Article
- Blue-shifted ancyromonad channelrhodopsins for multiplex optogenetics.bioRxiv : the preprint server for biology · 2025Article
- CryoRhodopsins: A comprehensive characterization of a group of microbial rhodopsins from cold environments.Science advances · 2025Article
- Genetics-Based Targeting Strategies for Precise Neuromodulation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Parallel photocycle kinetic model of anion channelrhodopsin GtACR1 function.Biophysical journal · 2024Article
- The open channel state in anion channelrhodopsin GtACR1 is a red-absorbing intermediate.Biophysical journal · 2024Article
- Channel Gating in Kalium Channelrhodopsin Slow Mutants.Journal of molecular biology · 2024Article
- Isospectral intermediates in the photochemical reaction cycle of anion channelrhodopsin GtACR1.Biophysical journal · 2023Article
- Sequential absorption of two photons creates a bistable form of RubyACR responsible for its strong desensitization.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- A blue-shifted anion channelrhodopsin from the Colpodellida alga Vitrella brassicaformis.Scientific reports · 2023Article
- Aion is a bistable anion-conducting channelrhodopsin that provides temporally extended and reversible neuronal silencing.Communications biology · 2022Article
- Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Article
- The crystal structure of bromide-boundeLife · 2021Article
- Time-resolved spectroscopic and electrophysiological data reveal insights in the gating mechanism of anion channelrhodopsin.Communications biology · 2021Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
A recently discovered family of natural anion channelrhodopsins (ACRs) have the highest conductance among channelrhodopsins and exhibit exclusive anion selectivity, which make them efficient inhibitory tools for optogenetics. We report analysis of flash-induced absorption changes in purified wild-type and mutant ACRs, and of photocurrents they generate in HEK293 cells. Contrary to cation channelrhodopsins (CCRs), the ion conducting state of ACRs develops in an L-like intermediate that precedes the deprotonation of the retinylidene Schiff base (i.e., formation of an M intermediate). Channel closing involves two mechanisms leading to depletion of the conducting L-like state: (i) Fast closing is caused by a reversible L⇔M conversion. Glu-68 in Guillardia theta ACR1 plays an important role in this transition, likely serving as a counterion and proton acceptor at least at high and neutral pH. Incomplete suppression of M formation in the GtACR1_E68Q mutant indicates the existence of an alternative proton acceptor. (ii) Slow closing of the channel parallels irreversible depletion of the M-like and, hence, L-like state. Mutation of Cys-102 that strongly affected slow channel closing slowed the photocycle to the same extent. The L and M intermediates were in equilibrium in C102A as in the WT. In the position of Glu-123 in channelrhodopsin-2, ACRs contain a noncarboxylate residue, the mutation of which to Glu produced early Schiff base proton transfer and strongly inhibited channel activity. The data reveal fundamental differences between natural ACR and CCR conductance mechanisms and their underlying photochemistry, further confirming that these proteins form distinct families of rhodopsin channels.
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