Evidence map›Paper›PMID 19842712›Full record

ArticleBiochemistry2009

Reconstitution of Gloeobacter violaceus rhodopsin with a light-harvesting carotenoid antenna.

Eleonora S Imasheva, Sergei P Balashov, Ah Reum Choi, Kwang-Hwan Jung, Janos K Lanyi

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
1.1field-weighted citation impact, top 27% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

50 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Fluorescence of the Retinal Chromophore in Microbial and Animal Rhodopsins.International journal of molecular sciences · 2023
    Review
  9. Responding to light signals: a comprehensive update on photomorphogenesis in cyanobacteria.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023
    Review
  10. Article
  11. Article
  12. Functional characterization of xanthorhodopsin in Salinivibrio socompensis, a novel halophile isolated from modern stromatolites.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Eleonora S ImashevaDepartment of Physiology and Biophysics, University of California, Irvine, California 92697, USA.
Sergei P Balashov
Ah Reum Choi
Kwang-Hwan Jung
Janos K Lanyi
University of California, Irvine · USSogang University · KR

Funding

LIGHT-DRIVEN ION TRANSPORT IN BACTERIAL RHODOPSINSR37GM029498 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI LANYI, JANOS K · 2000 to 2009
$4.5M
MECHANISM OF CHLORIDE TRANSPORT BY HALORHODOPSINR01GM029498 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI LANYI, JANOS K · 1985 to 2013
$2.1M
NIGMS NIH HHS GM29498NIGMS NIH HHS R01 GM029498NIGMS NIH HHS R37 GM029498
6 · The paper itself

Abstract

We show that salinixanthin, the light-harvesting carotenoid antenna of xanthorhodopsin, can be reconstituted into the retinal protein from Gloeobacter violaceus expressed in Escherichia coli. Reconstitution of gloeobacter rhodopsin with the carotenoid is accompanied by characteristic absorption changes and the appearance of CD bands similar to those observed for xanthorhodopsin that indicate immobilization and twist of the carotenoid in the binding site. As in xanthorhodopsin, the carotenoid functions as a light-harvesting antenna. The excitation spectrum for retinal fluorescence emission shows that ca. 36% of the energy absorbed by the carotenoid is transferred to the retinal. From excitation anisotropy, we calculate the angle between the two chromophores as being ca. 50 degrees , similar to that in xanthorhodopsin. The results indicate that gloeobacter rhodopsin binds salinixanthin in a manner similar to that of xanthorhodopsin and suggest that it might bind a carotenoid also in vivo. In the crystallographic structure of xanthorhodopsin, the conjugated chain of the carotenoid lies on the surface of helices E and F, and the 4-keto ring is immersed in the protein at van der Waals distance from the ionone ring of the retinal. The 4-keto ring is in the space occupied by a tryptophan in bacteriorhodopsin, which is replaced by the smaller glycine in xanthorhodopsin and gloeobacter rhodopsin. Specific binding of the carotenoid and its light-harvesting function are eliminated by a single mutation of the gloeobacter protein that replaces this glycine with a tryptophan. This indicates that the 4-keto ring is critically involved in carotenoid binding and suggests that a number of other recently identified retinal proteins, from a diverse group of organisms, could also contain carotenoid antenna since they carry the homologous glycine near the retinal.

Indexed as

Amino Acid SubstitutionBacteroidetesBinding SitesCarotenoidsCircular DichroismCyanobacteriaFluorescence PolarizationGlycosidesHydroxylamineMolecular ConformationProtein BindingRecombinant ProteinsRetinaldehydeRhodopsins, MicrobialSchiff BasesSpectrometry, FluorescenceCarotenoidsGlycosidesHydroxylamineRecombinant ProteinsRetinaldehydeRhodopsins, MicrobialsalinixanthinSchiff Bases

Identifiers

PMID19842712
PMCPMC2795404
OpenAlexW2043799762

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.