Evidence map›Paper›PMID 35577919›Full record

ArticleNature chemistry2022

Ultrafast proton-coupled isomerization in the phototransformation of phytochrome.

Yang Yang, Till Stensitzki, Luisa Sauthof, Andrea Schmidt, Patrick Piwowarski, Francisco Velazquez Escobar, Norbert Michael, Anh Duc Nguyen, Michal Szczepek, Florian Nikolas Brünig and 8 more

Abstract read
In one paragraph

Article in Nature chemistry, 2022. 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
–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

19 citing papers in PubMed.

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  15. Photocobilins integrate BNature communications · 2024
    Article
  16. Review
  17. Ultrafast protein response in the Pfr state of Cph1 phytochrome.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
    Article
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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

18 authors.

Yang YangDepartment of Physics, Freie Universität Berlin, Berlin, Germany.
Till StensitzkiDepartment of Physics, Freie Universität Berlin, Berlin, Germany.
Luisa SauthofCharité - Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Institute of Medical Physics and Biophysics, Group Protein X-ray Crystallography and Signal Transduction, Berlin, Germany.
Andrea SchmidtCharité - Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Institute of Medical Physics and Biophysics, Group Protein X-ray Crystallography and Signal Transduction, Berlin, Germany.ORCID http://orcid.org/0000-0003-1985-1908
Patrick PiwowarskiInstitut für Biologie, Biophysikalische Chemie, Humboldt-Universität zu Berlin, Berlin, Germany.
Francisco Velazquez EscobarInstitut für Chemie, Technische Universität Berlin, Berlin, Germany.
Norbert MichaelInstitut für Chemie, Technische Universität Berlin, Berlin, Germany.
Anh Duc NguyenInstitut für Chemie, Technische Universität Berlin, Berlin, Germany.
Michal SzczepekCharité - Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Institute of Medical Physics and Biophysics, Group Protein X-ray Crystallography and Signal Transduction, Berlin, Germany.
Florian Nikolas BrünigDepartment of Physics, Freie Universität Berlin, Berlin, Germany.ORCID http://orcid.org/0000-0001-8583-6488
Roland Rüdiger NetzDepartment of Physics, Freie Universität Berlin, Berlin, Germany.ORCID http://orcid.org/0000-0003-0147-0162
Maria Andrea MroginskiInstitut für Chemie, Technische Universität Berlin, Berlin, Germany.ORCID http://orcid.org/0000-0002-7497-5631
Suliman AdamFritz Haber Center for Molecular Dynamics Research, Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel.ORCID http://orcid.org/0000-0002-0891-5008
Franz BartlInstitut für Biologie, Biophysikalische Chemie, Humboldt-Universität zu Berlin, Berlin, Germany.
Igor SchapiroFritz Haber Center for Molecular Dynamics Research, Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel.ORCID http://orcid.org/0000-0001-8536-6869
Peter HildebrandtInstitut für Chemie, Technische Universität Berlin, Berlin, Germany.ORCID http://orcid.org/0000-0003-1030-5900
Patrick ScheererCharité - Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Institute of Medical Physics and Biophysics, Group Protein X-ray Crystallography and Signal Transduction, Berlin, Germany.ORCID http://orcid.org/0000-0001-5028-2075
Karsten HeyneDepartment of Physics, Freie Universität Berlin, Berlin, Germany. Karsten.heyne@fu-berlin.de.ORCID http://orcid.org/0000-0002-3243-9160

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biological function of phytochromes is triggered by an ultrafast photoisomerization of the tetrapyrrole chromophore biliverdin between two rings denoted C and D. The mechanism by which this process induces extended structural changes of the protein is unclear. Here we report ultrafast proton-coupled photoisomerization upon excitation of the parent state (Pfr) of bacteriophytochrome Agp2. Transient deprotonation of the chromophore's pyrrole ring D or ring C into a hydrogen-bonded water cluster, revealed by a broad continuum infrared band, is triggered by electronic excitation, coherent oscillations and the sudden electric-field change in the excited state. Subsequently, a dominant fraction of the excited population relaxes back to the Pfr state, while ~35% follows the forward reaction to the photoproduct. A combination of quantum mechanics/molecular mechanics calculations and ultrafast visible and infrared spectroscopies demonstrates how proton-coupled dynamics in the excited state of Pfr leads to a restructured hydrogen-bond environment of early Lumi-F, which is interpreted as a trigger for downstream protein structural changes.

Indexed as

PhytochromeBacterial ProteinsBiliverdineHydrogen BondingIsomerismProtonsBacterial ProteinsBiliverdinePhytochromeProtons

Identifiers

PMID35577919
PMCPMC9252900

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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.