Evidence map›Paper›PMID 35906527›Full record

ArticlePhotochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology2022

Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome.

Heli Lehtivuori, Jessica Rumfeldt, Satu Mustalahti, Sami Kurkinen, Heikki Takala

Open access · hybridAbstract read
PubMed Publisher
In one paragraph

Article in Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. 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

5 authors at 4 institutions in 1 country.

Heli LehtivuoriNanoscience Center, Department of Physics, University of Jyvaskyla, 40014, Jyvaskyla, Finland.ORCID http://orcid.org/0000-0002-7450-2578
Jessica RumfeldtNanoscience Center, Department of Biological and Environmental Sciences, University of Jyvaskyla, 40014, Jyvaskyla, Finland.ORCID http://orcid.org/0000-0001-7861-377X
Satu MustalahtiNanoscience Center, Department of Chemistry, University of Jyvaskyla, 40014, Jyvaskyla, Finland.ORCID http://orcid.org/0000-0001-9685-0015
Sami KurkinenNanoscience Center, Department of Biological and Environmental Sciences, University of Jyvaskyla, 40014, Jyvaskyla, Finland.ORCID http://orcid.org/0000-0003-2515-7429
Heikki TakalaNanoscience Center, Department of Biological and Environmental Sciences, University of Jyvaskyla, 40014, Jyvaskyla, Finland. heikki.p.takala@jyu.fi.ORCID http://orcid.org/0000-0003-2518-8583
University of Jyväskylä · FITampere University of Applied Sciences · FIUniversity of Helsinki · FIUniversity of Turku · FI

Funding

Biotieteiden ja Ympäristön Tutkimuksen Toimikunta 285461Biotieteiden ja Ympäristön Tutkimuksen Toimikunta 330678Luonnontieteiden ja Tekniikan Tutkimuksen Toimikunta 277194Luonnontieteiden ja Tekniikan Tutkimuksen Toimikunta 290677
6 · The paper itself

Abstract

Phytochromes are red light-sensing photoreceptor proteins that bind a bilin chromophore. Here, we investigate the role of a conserved histidine (H260) and tyrosine (Y263) in the chromophore-binding domain (CBD) of Deinococcus radiodurans phytochrome (DrBphP). Using crystallography, we show that in the H260A variant, the missing imidazole side chain leads to increased water content in the binding pocket. On the other hand, Y263F mutation reduces the water occupancy around the chromophore. Together, these changes in water coordination alter the protonation and spectroscopic properties of the biliverdin. These results pinpoint the importance of this conserved histidine and tyrosine, and the related water network, for the function and applications of phytochromes.

Indexed as

DeinococcusPhytochromeBacterial ProteinsBinding SitesHistidineProtein ConformationTyrosineWaterBacterial ProteinsHistidinePhytochromeTyrosineWaterBiliverdin protonationPhytochrome structureSpectral responsesWater network

Identifiers

PMID35906527
OpenAlexW4288714882

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.