ArticleNature communications2024
A subgroup of light-driven sodium pumps with an additional Schiff base counterion.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 14 citations in OpenAlex.
- Molecular mechanism of calcium inhibition in viral channelrhodopsins.Nature communications · 2026Article
- Diverging pH dependence and photocycle dynamics across members of the CryoRhodopsin clade.Biophysical journal · 2026Article
- A red-light gate for a cation channel: The conducting state of channelrhodopsin-1 from Chlamydomonas augustae.Biophysical journal · 2026Article
- The Conformational Switches of a Bacterial Light-Driven Sodium Pump Characterized by Time-Resolved Resonance Raman Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Microsecond Time-Resolved Cryo-EM Based on Jet Vitrification.bioRxiv : the preprint server for biology · 2025Article
- A Detailed View on the (Re)isomerization Dynamics in Microbial Rhodopsins Using Complementary Near-UV and IR Readouts.Angewandte Chemie (International ed. in English) · 2025Article
- An affordable convertible: Engineering proton transfer pathways in microbial rhodopsins.Biophysical journal · 2024Article
- Schiff Bases Derived from Pyridoxal 5'-Phosphate and 2-X-Phenylamine (X = H, OH, SH): Substituent Effects on UV-Vis Spectra and Hydrolysis Kinetics.Molecules (Basel, Switzerland) · 2024Article
- Crystallographic insights into lipid-membrane protein interactions in microbial rhodopsins.Frontiers in molecular biosciences · 2024Article
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Authors and funding
21 authors at 10 institutions in 5 countries.
Funding
Abstract
Light-driven sodium pumps (NaRs) are unique ion-transporting microbial rhodopsins. The major group of NaRs is characterized by an NDQ motif and has two aspartic acid residues in the central region essential for sodium transport. Here we identify a subgroup of the NDQ rhodopsins bearing an additional glutamic acid residue in the close vicinity to the retinal Schiff base. We thoroughly characterize a member of this subgroup, namely the protein ErNaR from Erythrobacter sp. HL-111 and show that the additional glutamic acid results in almost complete loss of pH sensitivity for sodium-pumping activity, which is in contrast to previously studied NaRs. ErNaR is capable of transporting sodium efficiently even at acidic pH levels. X-ray crystallography and single particle cryo-electron microscopy reveal that the additional glutamic acid residue mediates the connection between the other two Schiff base counterions and strongly interacts with the aspartic acid of the characteristic NDQ motif. Hence, it reduces its pKa. Our findings shed light on a subgroup of NaRs and might serve as a basis for their rational optimization for optogenetics.
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