ArticleScientific reports2017
Spectral Tuning Mechanism of Primate Blue-sensitive Visual Pigment Elucidated by FTIR Spectroscopy.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 25 citations in OpenAlex.
- Bromelain-induced physicochemical and structural changes in beef myofibrillar proteins and their molecular interaction mechanisms.Food chemistry: X · 2026Article
- Deprotonation of retinal Schiff base and structural dynamics in the early photoreaction of primate blue cone visual pigment.Biophysical journal · 2025Article
- Discovering Key Activation Hotspots in the MJournal of the American Chemical Society · 2025Article
- Schiff base deprotonation and structural changes in a mouse UV-sensitive cone visual pigment revealed by FTIR spectroscopy at 77 K.Biophysics and physicobiology · 2025Article
- Glu102Biochemistry · 2024Article
- Introduction of Session 8, "Structural mechanism of animal rhodopsins and GPCR".Biophysics and physicobiology · 2023Article
- Early Proton Transfer Reaction in a Primate Blue-Sensitive Visual Pigment.Biochemistry · 2022Article
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Light-induced difference FTIR spectroscopy of primate blue-sensitive visual pigment at 163 K.Biophysics and physicobiology · 2021Article
- Specificity of the chromophore-binding site in human cone opsins.The Journal of biological chemistry · 2019Article
- Convergent evolution of tertiary structure in rhodopsin visual proteins from vertebrates and box jellyfish.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein-bound water molecules are essential for the structure and function of many membrane proteins, including G-protein-coupled receptors (GPCRs). Our prior work focused on studying the primate green- (MG) and red- (MR) sensitive visual pigments using low-temperature Fourier transform infrared (FTIR) spectroscopy, which revealed protein-bound waters in both visual pigments. Although the internal waters are located in the vicinity of both the retinal Schiff base and retinal β-ionone ring, only the latter showed differences between MG and MR, which suggests their role in color tuning. Here, we report FTIR spectra of primate blue-sensitive pigment (MB) in the entire mid-IR region, which reveal the presence of internal waters that possess unique water vibrational signals that are reminiscent of a water cluster. These vibrational signals of the waters are influenced by mutations at position Glu113 and Trp265 in Rh, which suggest that these waters are situated between these two residues. Because Tyr265 is the key residue for achieving the spectral blue-shift in λ
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