ArticleScientific reports2021
Functional expression of the eukaryotic proton pump rhodopsin OmR2 in Escherichia coli and its photochemical characterization.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- 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
- A blue-shifted anion channelrhodopsin from the Colpodellida alga Vitrella brassicaformis.Scientific reports · 2023Article
- Detection of Membrane Potential-Dependent Rhodopsin Fluorescence Using Low-Intensity Light Emitting Diode for Long-Term Imaging.ACS omega · 2023Article
- Light-driven Proton Pumps as a Potential Regulator for Carbon Fixation in Marine Diatoms.Microbes and environments · 2023Article
- Rhodopsins build up the birefringent bodies of the dinoflagellate Oxyrrhis marina.Protoplasma · 2022Article
- The Photoreaction of the Proton-Pumping Rhodopsin 1 From the Maize Pathogenic BasidiomyceteFrontiers in molecular biosciences · 2022Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microbial rhodopsins are photoswitchable seven-transmembrane proteins that are widely distributed in three domains of life, archaea, bacteria and eukarya. Rhodopsins allow the transport of protons outwardly across the membrane and are indispensable for light-energy conversion in microorganisms. Archaeal and bacterial proton pump rhodopsins have been characterized using an Escherichia coli expression system because that enables the rapid production of large amounts of recombinant proteins, whereas no success has been reported for eukaryotic rhodopsins. Here, we report a phylogenetically distinct eukaryotic rhodopsin from the dinoflagellate Oxyrrhis marina (O. marina rhodopsin-2, OmR2) that can be expressed in E. coli cells. E. coli cells harboring the OmR2 gene showed an outward proton-pumping activity, indicating its functional expression. Spectroscopic characterization of the purified OmR2 protein revealed several features as follows: (1) an absorption maximum at 533 nm with all-trans retinal chromophore, (2) the possession of the deprotonated counterion (pK
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