Evidence map›Paper›PMID 19289053›Full record

ArticleBiophysical journal2009

Femtosecond carotenoid to retinal energy transfer in xanthorhodopsin.

Tomás Polívka, Sergei P Balashov, Pavel Chábera, Eleonora S Imasheva, Arkady Yartsev, Villy Sundström, Janos K Lanyi

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Protonation-Enhanced Energy Transfer in Xanthorhodopsin Kin4B8.The journal of physical chemistry letters · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. RubyACRs, nonalgal anion channelrhodopsins with highly red-shifted absorption.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

7 authors at 3 institutions in 2 countries.

Tomás PolívkaInstitute of Physical Biology, University of South Bohemia, Nové Hrady, Czech Republic. polivka@ufb.jcu.cz
Sergei P Balashov
Pavel Chábera
Eleonora S Imasheva
Arkady Yartsev
Villy Sundström
Janos K Lanyi
University of California, Irvine · USCzech Academy of Sciences · CZUniversity of South Bohemia in České Budějovice · CZ

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

Xanthorhodopsin of the extremely halophilic bacterium Salinibacter ruber represents a novel antenna system. It consists of a carbonyl carotenoid, salinixanthin, bound to a retinal protein that serves as a light-driven transmembrane proton pump similar to bacteriorhodopsin of archaea. Here we apply the femtosecond transient absorption technique to reveal the excited-state dynamics of salinixanthin both in solution and in xanthorhodopsin. The results not only disclose extremely fast energy transfer rates and pathways, they also reveal effects of the binding site on the excited-state properties of the carotenoid. We compared the excited-state dynamics of salinixanthin in xanthorhodopsin and in NaBH(4)-treated xanthorhodopsin. The NaBH(4) treatment prevents energy transfer without perturbing the carotenoid binding site, and allows observation of changes in salinixanthin excited-state dynamics related to specific binding. The S(1) lifetimes of salinixanthin in untreated and NaBH(4)-treated xanthorhodopsin were identical (3 ps), confirming the absence of the S(1)-mediated energy transfer. The kinetics of salinixanthin S(2) decay probed in the near-infrared region demonstrated a change of the S(2) lifetime from 66 fs in untreated xanthorhodopsin to 110 fs in the NaBH(4)-treated protein. This corresponds to a salinixanthin-retinal energy transfer time of 165 fs and an efficiency of 40%. In addition, binding of salinixanthin to xanthorhodopsin increases the population of the S(*) state that decays in 6 ps predominantly to the ground state, but a small fraction (<10%) of the S(*) state generates a triplet state.

Indexed as

Energy TransferAbsorptionBacterial ProteinsBinding SitesBorohydridesCarotenoidsGlycosidesKineticsMethanolRhodopsins, MicrobialSpectrum AnalysisBacterial ProteinsBorohydridesCarotenoidsGlycosidesMethanolRhodopsins, Microbialsalinixanthinsodium borohydridexanthorhodopsin, Salinibacter

Identifiers

PMID19289053
PMCPMC2717270
OpenAlexW2013481328

What OpenQuestion holds

Textmetadata
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.