Evidence map›Paper›PMID 23027869›Full record

ArticleThe Journal of biological chemistry2012

A photochromic histidine kinase rhodopsin (HKR1) that is bimodally switched by ultraviolet and blue light.

Meike Luck, Tilo Mathes, Sara Bruun, Roman Fudim, Rolf Hagedorn, Tra My Tran Nguyen, Suneel Kateriya, John T M Kennis, Peter Hildebrandt, Peter Hegemann

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

60 citing papers in PubMed, 121 citations in OpenAlex.

  1. Multistep 11-Journal of the American Chemical Society · 2025
    Article
  2. Article
  3. Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025
    Review
  4. Review
  5. Multiple retinal isomerizations during the early phase of the bestrhodopsin photoreaction.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Review
  8. Review
  9. Optogenetics at the presynapse.Nature neuroscience · 2022
    Review
  10. Article
  11. Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  12. Rhodopsin-Based Optogenetics: Basics and Applications.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  13. Article
  14. Review
  15. Molecular Biology of Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Molecular Properties and Optogenetic Applications of Enzymerhodopsins.Advances in experimental medicine and biology · 2021
    Review
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

10 authors at 4 institutions in 3 countries.

Meike LuckInstitute of Biology, Experimental Biophysics, Humboldt-Universität zu Berlin, 10115 Berlin, Germany.
Tilo Mathes
Sara Bruun
Roman Fudim
Rolf Hagedorn
Tra My Tran Nguyen
Suneel Kateriya
John T M Kennis
Peter Hildebrandt
Peter Hegemann
Humboldt-Universität zu Berlin · DETechnische Universität Berlin · DEUniversity of Delhi · INVrije Universiteit Amsterdam · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rhodopsins are light-activated chromoproteins that mediate signaling processes via transducer proteins or promote active or passive ion transport as ion pumps or directly light-activated channels. Here, we provide spectroscopic characterization of a rhodopsin from the Chlamydomonas eyespot. It belongs to a recently discovered but so far uncharacterized family of histidine kinase rhodopsins (HKRs). These are modular proteins consisting of rhodopsin, a histidine kinase, a response regulator, and in some cases an effector domain such as an adenylyl or guanylyl cyclase, all encoded in a single protein as a two-component system. The recombinant rhodopsin fragment, Rh, of HKR1 is a UVA receptor (λ(max) = 380 nm) that is photoconverted by UV light into a stable blue light-absorbing meta state Rh-Bl (λ(max) = 490 nm). Rh-Bl is converted back to Rh-UV by blue light. Raman spectroscopy revealed that the Rh-UV chromophore is in an unusual 13-cis,15-anti configuration, which explains why the chromophore is deprotonated. The excited state lifetime of Rh-UV is exceptionally stable, probably caused by a relatively unpolar retinal binding pocket, converting into the photoproduct within about 100 ps, whereas the blue form reacts 100 times faster. We propose that the photochromic HKR1 plays a role in the adaptation of behavioral responses in the presence of UVA light.

Indexed as

Ultraviolet RaysAdaptation, PhysiologicalAdenylyl CyclasesBinding SitesChlamydomonas reinhardtiiGuanylate CyclaseHistidine KinasePlant ProteinsProtein KinasesProtein Structure, TertiaryRhodopsinAdenylyl CyclasesGuanylate CyclaseHistidine KinasePlant ProteinsProtein KinasesRhodopsin

Identifiers

PMID23027869
PMCPMC3501036
OpenAlexW2129603261

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.