ArticleBiochemistry2006
Induced chirality of the light-harvesting carotenoid salinixanthin and its interaction with the retinal of xanthorhodopsin.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 50 citations in OpenAlex.
- Vibronic Reorganization Suppresses Salinixanthin-to-Retinal Energy Transfer in the Freshwater Kin4B8 Xanthorhodopsin.The journal of physical chemistry letters · 2026Article
- Carotenoids bind rhodopsins and act as photocycle-accelerating pigments in marine Bacteroidota.Nature microbiology · 2025Article
- Molecular Mechanisms behind Circular Dichroism Spectral Variations between Channelrhodopsin and Heliorhodopsin Dimers.The journal of physical chemistry letters · 2024Article
- Expression of Xanthorhodopsin in Escherichia coli.The protein journal · 2023Article
- Retinal-Carotenoid Interactions in a Sodium-Ion-Pumping Rhodopsin: Implications on Oligomerization and Thermal Stability.The journal of physical chemistry. B · 2023Article
- Isolation and characterization of a main porin from the outer membrane of Salinibacter ruber.Journal of bioenergetics and biomembranes · 2022Article
- Electronic Couplings and Electrostatic Interactions Behind the Light Absorption of Retinal Proteins.Frontiers in molecular biosciences · 2021Review
- Diversity, Mechanism, and Optogenetic Application of Light-Driven Ion Pump Rhodopsins.Advances in experimental medicine and biology · 2021Review
- The chirality origin of retinal-carotenoid complex in gloeobacter rhodopsin: a temperature-dependent excitonic coupling.Scientific reports · 2020Article
- Marine Bacteria versus Microalgae: Who Is the Best for Biotechnological Production of Bioactive Compounds with Antioxidant Properties and Other Biological Applications?Marine drugs · 2019Review
- Exploring the Valuable Carotenoids for the Large-Scale Production by Marine Microorganisms.Marine drugs · 2018Review
- Engineering a carotenoid-binding site in Dokdonia sp. PRO95 NaPhotosynthesis research · 2018Article
- Wavelength-dependent photocycle activity of xanthorhodopsin in the visible region.Biochemistry and biophysics reports · 2016Article
- Occurrence of viable, red-pigmented haloarchaea in the plumage of captive flamingoes.Scientific reports · 2015Article
- Removal and reconstitution of the carotenoid antenna of xanthorhodopsin.The Journal of membrane biology · 2011Article
- Reconstitution of gloeobacter rhodopsin with echinenone: role of the 4-keto group.Biochemistry · 2010Article
- Reconstitution of Gloeobacter violaceus rhodopsin with a light-harvesting carotenoid antenna.Biochemistry · 2009Article
- Femtosecond carotenoid to retinal energy transfer in xanthorhodopsin.Biophysical journal · 2009Article
- Crystallographic structure of xanthorhodopsin, the light-driven proton pump with a dual chromophore.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Excitation energy-transfer and the relative orientation of retinal and carotenoid in xanthorhodopsin.Biophysical journal · 2008Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In xanthorhodopsin, a retinal protein-carotenoid complex of Salinibacter ruber, the carotenoid salinixanthin functions as a light-harvesting antenna in supplying additional excitation energy for retinal isomerization and proton transport. Another retinal protein, archaerhodopsin, has been shown to contain a carotenoid, bacterioruberin, but without an antenna function. We report here that the binding site confers a chiral geometry on salinixanthin in xanthorhodopsin and confirm that the same is true for bacterioruberin in archaerhodopsin. Cell membranes containing these rhodopsins exhibit CD spectra with sharp positive bands in the visible region where the carotenoids absorb, and in the case of xanthorhodopsin a negative band at 536 nm, as well as bands in the UV region. The carotenoid in ethanol has very weak optical activity in the visible region of the spectrum. Denaturation of the opsin upon deprotonation of the Schiff base at pH 12.5 eliminates the induced CD bands in both proteins. In one of these proteins, but not in the other, the carotenoid binding site depends entirely on the retinal. Hydrolysis of the retinal Schiff base of xanthorhodopsin with hydroxylamine eliminates the induced CD bands of salinixanthin. In contrast, hydrolysis of the Schiff base in archaerhodopsin does not abolish the CD bands of bacterioruberin. Thus, consistent with its antenna function, the carotenoid binding site interacts closely with the retinal only in xanthorhodopsin, and this interaction is the major source of the CD bands. In this protein, protonation of the counterion with a decrease in pH from 8 to 5 causes significant changes in the CD spectrum. The observed spectral features suggest that binding of salinixanthin in xanthorhodopsin involves the cyclohexenone ring of the carotenoid and its conformational heterogeneity is restricted.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.