Evidence map›Paper›PMID 25901821›Full record

ArticleNature chemistry2015

A protonation-coupled feedback mechanism controls the signalling process in bathy phytochromes.

Francisco Velazquez Escobar, Patrick Piwowarski, Johannes Salewski, Norbert Michael, Maria Fernandez Lopez, Anna Rupp, Bilal Muhammad Qureshi, Patrick Scheerer, Franz Bartl, Nicole Frankenberg-Dinkel and 3 more

Abstract read
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In one paragraph

Article in Nature chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
–field-weighted citation impact
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

30 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Propagation of Photoinduced Electric Field Changes Through Phytochrome and their Impact on Conformational Transitions.Chemphyschem : a European journal of chemical physics and physical chemistry · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Vibrational couplings between protein and cofactor in bacterial phytochrome Agp1 revealed by 2D-IR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Article
  16. Article
  17. Ultrafast proton release reaction and primary photochemistry of phycocyanobilin in solution observed with fs-time-resolved mid-IR and UV/Vis spectroscopy.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021
    Article
  18. Review
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  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

13 authors.

Francisco Velazquez EscobarInstitut für Chemie, Technische Universität Berlin, Sekr. PC 14, Straße des 17. Juni 135, Berlin D-10623, Germany.
Patrick PiwowarskiInstitut für Medizinische Physik und Biophysik, AG Spektroskopie, Charité - Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.
Johannes SalewskiInstitut für Chemie, Technische Universität Berlin, Sekr. PC 14, Straße des 17. Juni 135, Berlin D-10623, Germany.
Norbert MichaelInstitut für Chemie, Technische Universität Berlin, Sekr. PC 14, Straße des 17. Juni 135, Berlin D-10623, Germany.
Maria Fernandez LopezInstitut für Chemie, Technische Universität Berlin, Sekr. PC 14, Straße des 17. Juni 135, Berlin D-10623, Germany.
Anna RuppInstitut für Medizinische Physik und Biophysik, AG Spektroskopie, Charité - Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.
Bilal Muhammad QureshiInstitut für Medizinische Physik und Biophysik, AG Protein X-ray Crystallography and Signal Transduction, Charité - Universitätsmedizin Berlin, Charitéplatz 1, D-10117, Berlin, Germany.
Patrick ScheererInstitut für Medizinische Physik und Biophysik, AG Protein X-ray Crystallography and Signal Transduction, Charité - Universitätsmedizin Berlin, Charitéplatz 1, D-10117, Berlin, Germany.
Franz BartlInstitut für Medizinische Physik und Biophysik, AG Spektroskopie, Charité - Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.
Nicole Frankenberg-DinkelFachbereich Biologie, Abteilung Mikrobiologie, Technische Universität Kaiserslautern, Paul-Ehrlich-Straße 23, Kaiserslautern D-67663, Germany.
Friedrich SiebertInstitut für Molekulare Medizin und Zellforschung, Sektion Biophysik, Albert-Ludwigs-Universität, Freiburg, Hermann-Herderstraße 9, Freiburg D-79104, Germany.
Maria Andrea MroginskiInstitut für Chemie, Technische Universität Berlin, Sekr. PC 14, Straße des 17. Juni 135, Berlin D-10623, Germany.
Peter HildebrandtInstitut für Chemie, Technische Universität Berlin, Sekr. PC 14, Straße des 17. Juni 135, Berlin D-10623, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phytochromes are bimodal photoswitches composed of a photosensor and an output module. Photoactivation of the sensor is initiated by a double bond isomerization of the tetrapyrrole chromophore and eventually leads to protein conformational changes. Recently determined structural models of phytochromes identify differences between the inactive and the signalling state but do not reveal the mechanism of photosensor activation or deactivation. Here, we report a vibrational spectroscopic study on bathy phytochromes that demonstrates that the formation of the photoactivated state and thus (de)activation of the output module is based on proton translocations in the chromophore pocket coupling chromophore and protein structural changes. These proton transfer steps, involving the tetrapyrrole and a nearby histidine, also enable thermal back-isomerization of the chromophore via keto-enol tautomerization to afford the initial dark state. Thus, the same proton re-arrangements inducing the (de)activation of the output module simultaneously initiate the reversal of this process, corresponding to a negative feedback mechanism.

Indexed as

FeedbackProtonsSignal TransductionModels, MolecularPhytochromePhytochromeProtons

Identifiers

PMID25901821

What OpenQuestion holds

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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.