ArticleBiochemistry2014
Retinal chromophore structure and Schiff base interactions in red-shifted channelrhodopsin-1 from Chlamydomonas augustae.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 33 citations in OpenAlex.
- A red-light gate for a cation channel: The conducting state of channelrhodopsin-1 from Chlamydomonas augustae.Biophysical journal · 2026Article
- Multicolor photoreactions of the red light-activated channelrhodopsin Chrimson.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- My remembrances of H.G. Khorana: exploring the mechanism of bacteriorhodopsin with site-directed mutagenesis and FTIR difference spectroscopy.Biophysical reviews · 2023Review
- Optical Switching Between Long-lived States of Opsin Transmembrane Voltage Sensors.Photochemistry and photobiology · 2021Article
- Toward Multiplexed Optogenetic Circuits.Frontiers in bioengineering and biotechnology · 2021Review
- Novel Modular Rhodopsins from Green Algae Hold Great Potential for Cellular Optogenetic Modulation Across the Biological Model Systems.Life (Basel, Switzerland) · 2020Article
- Ultrafast Backbone Protonation in Channelrhodopsin-1 Captured by Polarization Resolved Fs Vis-pump-IR-Probe Spectroscopy and Computational Methods.Molecules (Basel, Switzerland) · 2020Article
- Analog Retinal Redshifts Visible Absorption of QuasAr Transmembrane Voltage Sensors into Near-infrared.Photochemistry and photobiology · 2020Article
- Photoreaction Dynamics of Red-Shifting Retinal Analogues Reconstituted in Proteorhodopsin.The journal of physical chemistry. B · 2019Article
- All-optical crosstalk-free manipulation and readout of Chronos-expressing neurons.Journal of physics D: Applied physics · 2019Article
- Strong pH-Dependent Near-Infrared Fluorescence in a Microbial Rhodopsin Reconstituted with a Red-Shifting Retinal Analogue.The journal of physical chemistry letters · 2018Article
- Optogenetic regulation of transcription.BMC neuroscience · 2018Review
- Donor-Acceptor Conjugated Linear Polyenes: A Study of Excited State Intramolecular Charge Transfer, Photoisomerization and Fluorescence Probe Properties.Journal of fluorescence · 2018Article
- Raman spectroscopy of a near infrared absorbing proteorhodopsin: Similarities to the bacteriorhodopsin O photointermediate.PloS one · 2018Article
- Conversion of microbial rhodopsins: insights into functionally essential elements and rational protein engineering.Biophysical reviews · 2017Review
- Proton transfer reactions in the red light-activatable channelrhodopsin variant ReaChR and their relevance for its function.The Journal of biological chemistry · 2017Article
- Structural Changes in an Anion Channelrhodopsin: Formation of the K and L Intermediates at 80 K.Biochemistry · 2017Article
- Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization.Structural dynamics (Melville, N.Y.) · 2016Article
- Resonance Raman Study of an Anion Channelrhodopsin: Effects of Mutations near the Retinylidene Schiff Base.Biochemistry · 2016Article
- Kinetic and vibrational isotope effects of proton transfer reactions in channelrhodopsin-2.Biophysical journal · 2015Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Channelrhodopsins (ChRs), which form a distinct branch of the microbial rhodopsin family, control phototaxis in green algae. Because ChRs can be expressed and function in neuronal membranes as light-gated cation channels, they have rapidly become an important optogenetic tool in neurobiology. While channelrhodopsin-2 from the unicellular alga Chlamydomonas reinhardtii (CrChR2) is the most commonly used and extensively studied optogenetic ChR, little is known about the properties of the diverse group of other ChRs. In this study, near-infrared confocal resonance Raman spectroscopy along with hydrogen-deuterium exchange and site-directed mutagenesis were used to study the structure of red-shifted ChR1 from Chlamydomonas augustae (CaChR1). These measurements reveal that (i) CaChR1 has an all-trans-retinal structure similar to those of the light-driven proton pump bacteriorhodopsin (BR) and sensory rhodopsin II but different from that of the mixed retinal composition of CrChR2, (ii) lowering the pH from 7 to 2 or substituting neutral residues for Glu169 or Asp299 does not significantly shift the ethylenic stretch frequency more than 1-2 cm(-1) in contrast to BR in which a downshift of 7-9 cm(-1) occurs reflecting neutralization of the Asp85 counterion, and (iii) the CaChR1 protonated Schiff base (SB) has stronger hydrogen bonding than BR. A model is proposed to explain these results whereby at pH 7 the predominant counterion to the SB is Asp299 (the homologue to Asp212 in BR) while Glu169 (the homologue to Asp85 in BR) exists in a neutral state. We observe an unusual constancy of the resonance Raman spectra over the broad range from pH 9 to 2 and discuss its implications. These results are in accord with recent visible absorption and current measurements of CaChR1 [Sineshchekov, O. A., et al. (2013) Intramolecular proton transfer in channelrhodopsins. Biophys. J. 104, 807-817; Li, H., et al. (2014) Role of a helix B lysine residue in the photoactive site in channelrhodopsins. Biophys. J. 106, 1607-1617].
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