ArticleBiophysical journal2012
Tuning the primary reaction of channelrhodopsin-2 by imidazole, pH, and site-specific mutations.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Diverging pH dependence and photocycle dynamics across members of the CryoRhodopsin clade.Biophysical journal · 2026Article
- CryoRhodopsins: A comprehensive characterization of a group of microbial rhodopsins from cold environments.Science advances · 2025Article
- Reversible Photochromic Reactions of Bacteriorhodopsin fromMolecules (Basel, Switzerland) · 2024Article
- Multiple retinal isomerizations during the early phase of the bestrhodopsin photoreaction.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Aion is a bistable anion-conducting channelrhodopsin that provides temporally extended and reversible neuronal silencing.Communications biology · 2022Article
- Color-tuning of natural variants of heliorhodopsin.Scientific reports · 2021Article
- Channelrhodopsin-mediated optogenetics highlights a central role of depolarization-dependent plant proton pumps.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Photoreaction Dynamics of Red-Shifting Retinal Analogues Reconstituted in Proteorhodopsin.The journal of physical chemistry. B · 2019Article
- Coherent control of an opsin in living brain tissue.Nature physics · 2017Article
- Reaction dynamics of the chimeric channelrhodopsin C1C2.Scientific reports · 2017Article
- Dampening Spontaneous Activity Improves the Light Sensitivity and Spatial Acuity of Optogenetic Retinal Prosthetic Responses.Scientific reports · 2016Article
- Optochemokine Tandem for Light-Control of Intracellular Ca2.PloS one · 2016Article
- Comparison of the structural changes occurring during the primary phototransition of two different channelrhodopsins from Chlamydomonas algae.Biochemistry · 2015Article
- Channelrhodopsin-2-XXL, a powerful optogenetic tool for low-light applications.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The EF loop in green proteorhodopsin affects conformation and photocycle dynamics.Biophysical journal · 2013Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Femtosecond time-resolved absorption measurements were performed to investigate the influence of the pH, imidazole concentration, and point mutations on the isomerization process of Channelrhodopsin-2. Apart from the typical spectral characteristics of retinal isomerization, an additional absorption feature rises for the wild-type (wt) on a timescale from tens of ps to 1 ns within the spectral range of the photoproduct and is attributed to an equilibration between different K-intermediates. Remarkably, this absorption feature vanishes upon addition of imidazole or lowering the pH. In the latter case, the isomerization is dramatically slowed down, due to protonation of negatively charged amino acids within the retinal binding pocket, e.g., E123 and D253. Moreover, we investigated the influence of several point mutations within the retinal binding pocket E123T, E123D, C128T, and D156C. For E123T, the isomerization is retarded compared to wt and E123D, indicating that a negatively charged residue at this position functions as an effective catalyst in the isomerization process. In the case of the C128T mutant, all primary processes are slightly accelerated compared to the wt, whereas the isomerization dynamics for the D156C mutant is similar to wt after addition of imidazole.
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