Evidence map›Paper›PMID 24036118›Full record

ArticleThe Journal of biological chemistry2013

Unusual spectral properties of bacteriophytochrome Agp2 result from a deprotonation of the chromophore in the red-absorbing form Pr.

Benjamin Zienicke, Isabel Molina, René Glenz, Patrick Singer, Dorothee Ehmer, Francisco Velazquez Escobar, Peter Hildebrandt, Rolf Diller, Tilman Lamparter

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

25 citing papers in PubMed, 61 citations in OpenAlex.

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  8. Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022
    Article
  9. Crystal structure of a far-red-sensing cyanobacteriochrome reveals an atypical bilin conformation and spectral tuning mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

9 authors at 3 institutions in 1 country.

Benjamin ZienickeFrom the Botanical Institute, Karlsruhe Institute of Technology, Kaiserstrasse 2, D-76131 Karlsruhe, Germany.
Isabel Molina
René Glenz
Patrick Singer
Dorothee Ehmer
Francisco Velazquez Escobar
Peter Hildebrandt
Rolf Diller
Tilman Lamparter
Karlsruhe Institute of Technology · DEUniversity of Kaiserslautern · DETechnische Universität Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phytochromes are widely distributed photoreceptors with a bilin chromophore that undergo a typical reversible photoconversion between the two spectrally different forms, Pr and Pfr. The phytochrome Agp2 from Agrobacterium tumefaciens belongs to the group of bathy phytochromes that have a Pfr ground state as a result of the Pr to Pfr dark conversion. Agp2 has untypical spectral properties in the Pr form reminiscent of a deprotonated chromophore as confirmed by resonance Raman spectroscopy. UV/visible absorption spectroscopy showed that the pKa is >11 in the Pfr form and ∼7.6 in the Pr form. Unlike other phytochromes, photoconversion thus results in a pKa shift of more than 3 units. The Pr/Pfr ratio after saturating irradiation with monochromatic light is strongly pH-dependent. This is partially due to a back-reaction of the deprotonated Pr chromophore at pH 9 after photoexcitation as found by flash photolysis. The chromophore protonation and dark conversion were affected by domain swapping and site-directed mutagenesis. A replacement of the PAS or GAF domain by the respective domain of the prototypical phytochrome Agp1 resulted in a protonated Pr chromophore; the GAF domain replacement afforded an inversion of the dark conversion. A reversion was also obtained with the triple mutant N12S/Q190L/H248Q, whereas each single point mutant is characterized by decelerated Pr to Pfr dark conversion.

Indexed as

Agrobacterium tumefaciensAmino Acid SubstitutionBacterial ProteinsMutagenesis, Site-DirectedMutation, MissensePhytochromeProtein Structure, TertiaryRecombinant ProteinsSpectrophotometry, UltravioletSpectrum Analysis, RamanBacterial ProteinsPhytochromeRecombinant ProteinsBacterial Protein KinasesBacterial Signal TransductionBilinBiliproteinDomain Swap MutantsFlash PhotolysisPhotobiologyPhotoreceptorsRaman SpectroscopyUV Spectroscopy

Identifiers

PMID24036118
PMCPMC3814768
OpenAlexW2078213703

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.