ArticleBiophysical journal2008
Excitation energy-transfer and the relative orientation of retinal and carotenoid in xanthorhodopsin.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 55 citations in OpenAlex.
- Vibronic Reorganization Suppresses Salinixanthin-to-Retinal Energy Transfer in the Freshwater Kin4B8 Xanthorhodopsin.The journal of physical chemistry letters · 2026Article
- Protonation-Enhanced Energy Transfer in Xanthorhodopsin Kin4B8.The journal of physical chemistry letters · 2025Article
- Structural and spectroscopic basis of excitation energy transfer in microbial rhodopsins binding xanthophylls.Chemical science · 2025Article
- Carotenoids bind rhodopsins and act as photocycle-accelerating pigments in marine Bacteroidota.Nature microbiology · 2025Article
- Fluorescence of the Retinal Chromophore in Microbial and Animal Rhodopsins.International journal of molecular sciences · 2023Review
- 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
- Article
- A bacterium from a mountain lake harvests light using both proton-pumping xanthorhodopsins and bacteriochlorophyll-based photosystems.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Isolation and characterization of a main porin from the outer membrane of Salinibacter ruber.Journal of bioenergetics and biomembranes · 2022Article
- Carotenoid binding in Gloeobacteria rhodopsin provides insights into divergent evolution of xanthorhodopsin types.Communications biology · 2022Article
- Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Diversity, Mechanism, and Optogenetic Application of Light-Driven Ion Pump Rhodopsins.Advances in experimental medicine and biology · 2021Review
- 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
- Engineering a FRET strategy to achieve a ratiometric two-photon fluorescence response with a large emission shift and its application to fluorescence imaging.Chemical science · 2015Article
- Direct determination of resonance energy transfer in photolyase: structural alignment for the functional state.The journal of physical chemistry. A · 2014Article
- Genomics and physiology of a marine flavobacterium encoding a proteorhodopsin and a xanthorhodopsin-like protein.PloS one · 2013Article
- Genome sequence of the Antarctic rhodopsins-containing flavobacterium Gillisia limnaea type strain (R-8282(T)).Standards in genomic sciences · 2012Article
- Aspartate-histidine interaction in the retinal schiff base counterion of the light-driven proton pump of Exiguobacterium sibiricum.Biochemistry · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The cell membrane of Salinibacter ruber contains xanthorhodopsin, a light-driven transmembrane proton pump with two chromophores: a retinal and the carotenoid, salinixanthin. Action spectra for transport had indicated that light absorbed by either is utilized for function. If the carotenoid is an antenna in this protein, its excited state energy has to be transferred to the retinal and should be detected in the retinal fluorescence. From fluorescence studies, we show that energy transfer occurs from the excited singlet S(2) state of salinixanthin to the S(1) state of the retinal. Comparison of the absorption spectrum with the excitation spectrum for retinal emission yields 45 +/- 5% efficiency for the energy transfer. Such high efficiency would require close proximity and favorable geometry for the two polyene chains, but from the heptahelical crystallographic structure of the homologous retinal protein, bacteriorhodopsin, it is not clear where the carotenoid can be located near the retinal. The fluorescence excitation anisotropy spectrum reveals that the angle between their transition dipole moments is 56 +/- 3 degrees . The protein accommodates the carotenoid as a second chromophore in a distinct binding site to harvest light with both extended wavelength and polarization ranges. The results establish xanthorhodopsin as the simplest biological excited-state donor-acceptor system for collecting light.
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