ArticleScientific reports2018
Oligomeric states of microbial rhodopsins determined by high-speed atomic force microscopy and circular dichroic spectroscopy.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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53 citing papers in PubMed, 92 citations in OpenAlex.
- Molecular mechanism of calcium inhibition in viral channelrhodopsins.Nature communications · 2026Article
- Dual-Laser Laser-Induced Liquid Bead Ion Desorption Mass Spectrometry: A New Approach for Adjustable Softness and Higher Sensitivity.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Resurrecting Full-Length Ancestral Schizorhodopsins and Heliorhodopsins with Structure-Guided, Indel-Aware Sequence Reconstruction.ACS omega · 2026Article
- Mechanistic insights into NaThe Journal of biological chemistry · 2026Article
- CryoRhodopsins: A comprehensive characterization of a group of microbial rhodopsins from cold environments.Science advances · 2025Article
- Actinorhodopsin: an efficient and robust light-driven proton pump for bionanotechnological applications.Scientific reports · 2025Article
- Structural insights into the mechanism and dynamics of proteorhodopsin biogenesis and retinal scavenging.Nature communications · 2024Article
- Solid-state NMR of the retinal protonated Schiff base in microbial rhodopsins.Magnetic resonance letters · 2024Review
- Molecular Mechanisms behind Circular Dichroism Spectral Variations between Channelrhodopsin and Heliorhodopsin Dimers.The journal of physical chemistry letters · 2024Article
- A subgroup of light-driven sodium pumps with an additional Schiff base counterion.Nature communications · 2024Article
- NaMolecules (Basel, Switzerland) · 2023Review
- Structures of channelrhodopsin paralogs in peptidiscs explain their contrasting KNature communications · 2023Article
- Imaging single CaMKII holoenzymes at work by high-speed atomic force microscopy.Science advances · 2023Article
- Spatiotemporal resolution in high-speed atomic force microscopy for studying biological macromolecules in action.Microscopy (Oxford, England) · 2023Review
- Introduction of Session 2, "Advanced methods for retinal proteins".Biophysics and physicobiology · 2023Article
- Potassium-selective channelrhodopsins.Biophysics and physicobiology · 2023Article
- Protein dynamics of a light-driven NaBiophysics and physicobiology · 2023Article
- Retinal-Carotenoid Interactions in a Sodium-Ion-Pumping Rhodopsin: Implications on Oligomerization and Thermal Stability.The journal of physical chemistry. B · 2023Article
- Article
- Lipid membrane mimetics and oligomerization tune functional properties of proteorhodopsin.Biophysical journal · 2023Article
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Authors and funding
9 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Oligomeric assembly is a common feature of membrane proteins and often relevant to their physiological functions. Determining the stoichiometry and the oligomeric state of membrane proteins in a lipid bilayer is generally challenging because of their large size, complexity, and structural alterations under experimental conditions. Here, we use high-speed atomic force microscopy (HS-AFM) to directly observe the oligomeric states in the lipid membrane of various microbial rhodopsins found within eubacteria to archaea. HS-AFM images show that eubacterial rhodopsins predominantly exist as pentamer forms, while archaeal rhodopsins are trimers in the lipid membrane. In addition, circular dichroism (CD) spectroscopy reveals that pentameric rhodopsins display inverted CD couplets compared to those of trimeric rhodopsins, indicating different types of exciton coupling of the retinal chromophore in each oligomer. The results clearly demonstrate that the stoichiometry of the fundamental oligomer of microbial rhodopsins strongly correlate with the phylogenetic tree, providing a new insight into the relationship between the oligomeric structure and function-structural evolution of microbial rhodopsins.
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