ArticleThe Journal of biological chemistry2013
A blue-shifted light-driven proton pump for neural silencing.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 74 citations in OpenAlex.
- Molecular Properties of a Novel Inward Proton Pump Rhodopsin, GhXeR.The journal of physical chemistry. B · 2026Article
- Article
- Blue-shifted ancyromonad channelrhodopsins for multiplex optogenetics.bioRxiv : the preprint server for biology · 2025Article
- Protonation of Asp116 and distortion of the all-trans retinal chromophore in Krokinobacter eikastus rhodopsin 2 causes a redshift in absorption maximum upon dehydration.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023Article
- A blue-shifted anion channelrhodopsin from the Colpodellida alga Vitrella brassicaformis.Scientific reports · 2023Article
- Biophysical characterization of microbial rhodopsins with DSE motif.Biophysics and physicobiology · 2023Article
- Excited-state dynamics of all-trans protonated retinal Schiff base in CRABPII-based rhodopsin mimics.Biophysical journal · 2022Article
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Pro219 is an electrostatic color determinant in the light-driven sodium pump KR2.Communications biology · 2021Article
- An optogenetic assay method for electrogenic transporters using Escherichia coli co-expressing light-driven proton pump.Protein science : a publication of the Protein Society · 2021Article
- BiPOLES is an optogenetic tool developed for bidirectional dual-color control of neurons.Nature communications · 2021Article
- Functional expression of the eukaryotic proton pump rhodopsin OmR2 in Escherichia coli and its photochemical characterization.Scientific reports · 2021Article
- Exploration of natural red-shifted rhodopsins using a machine learning-based Bayesian experimental design.Communications biology · 2021Article
- Color-tuning of natural variants of heliorhodopsin.Scientific reports · 2021Article
- Diversity, Mechanism, and Optogenetic Application of Light-Driven Ion Pump Rhodopsins.Advances in experimental medicine and biology · 2021Review
- Exploring the Retinal Binding Cavity of Archaerhodopsin-3 by Replacing the Retinal Chromophore With a Dimethyl Phenylated Derivative.Frontiers in molecular biosciences · 2021Article
- De novo rational design of a freestanding, supercharged polypeptide, proton-conducting membrane.Science advances · 2020Article
- Vectorial Proton Transport Mechanism of RxR, a Phylogenetically Distinct and Thermally Stable Microbial Rhodopsin.Scientific reports · 2020Article
- Quantitation of the neural silencing activity of anion channelrhodopsins in Caenorhabditis elegans and their applicability for long-term illumination.Scientific reports · 2019Article
- Red-shifting mutation of light-driven sodium-pump rhodopsin.Nature communications · 2019Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ion-transporting rhodopsins are widely utilized as optogenetic tools both for light-induced neural activation and silencing. The most studied representative is Bacteriorhodopsin (BR), which absorbs green/red light (∼570 nm) and functions as a proton pump. Upon photoexcitation, BR induces a hyperpolarization across the membrane, which, if incorporated into a nerve cell, results in its neural silencing. In this study, we show that several residues around the retinal chromophore, which are completely conserved among BR homologs from the archaea, are involved in the spectral tuning in a BR homolog (HwBR) and that the combination mutation causes a large spectral blue shift (λmax = 498 nm) while preserving the robust pumping activity. Quantum mechanics/molecular mechanics calculations revealed that, compared with the wild type, the β-ionone ring of the chromophore in the mutant is rotated ∼130° because of the lack of steric hindrance between the methyl groups of the retinal and the mutated residues, resulting in the breakage of the π conjugation system on the polyene chain of the retinal. By the same mutations, similar spectral blue shifts are also observed in another BR homolog, archearhodopsin-3 (also called Arch). The color variant of archearhodopsin-3 could be successfully expressed in the neural cells of Caenorhabditis elegans, and illumination with blue light (500 nm) led to the effective locomotory paralysis of the worms. Thus, we successfully produced a blue-shifted proton pump for neural silencing.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.