Evidence map›Paper›PMID 25253687›Full record

ArticleThe Journal of biological chemistry2014

Origins of fluorescence in evolved bacteriophytochromes.

Shyamosree Bhattacharya, Michele E Auldridge, Heli Lehtivuori, Janne A Ihalainen, Katrina T Forest

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
13.1field-weighted citation impact, top 1% 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

33 citing papers in PubMed, 67 citations in OpenAlex.

  1. The near-infrared bacteriophytochrome-derived fluorescent protein PENELOPE enables RESOLFT superresolution microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  3. 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
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  12. Rational conversion of chromophore selectivity of cyanobacteriochromes to accept mammalian intrinsic biliverdin.Proceedings of the National Academy of Sciences of the United States of America · 2019
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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

5 authors at 2 institutions in 2 countries.

Shyamosree BhattacharyaDepartments of Bacteriology, University of Wisconsin, Madison, Wisconsin 53706 and.
Michele E AuldridgeDepartments of Bacteriology, University of Wisconsin, Madison, Wisconsin 53706 and.
Heli LehtivuoriNanoscience Center, Department of Biological and Environmental Sciences, University of Jyväskylä, Jyväskylä, FI-40014 Finland.
Janne A IhalainenNanoscience Center, Department of Biological and Environmental Sciences, University of Jyväskylä, Jyväskylä, FI-40014 Finland. Electronic address: janne.ihalainen@jyu.fi.
Katrina T ForestDepartments of Bacteriology, University of Wisconsin, Madison, Wisconsin 53706 and. Electronic address: forest@bact.wisc.edu.
University of Wisconsin–Madison · USUniversity of Jyväskylä · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Use of fluorescent proteins to study in vivo processes in mammals requires near-infrared (NIR) biomarkers that exploit the ability of light in this range to penetrate tissue. Bacteriophytochromes (BphPs) are photoreceptors that couple absorbance of NIR light to photoisomerization, protein conformational changes, and signal transduction. BphPs have been engineered to form NIR fluorophores, including IFP1.4, Wi-Phy, and the iRFP series, initially by replacement of Asp-207 by His. This position was suggestive because its main chain carbonyl is within hydrogen-bonding distance to pyrrole ring nitrogens of the biliverdin chromophore, thus potentially functioning as a crucial transient proton sink during photoconversion. To explain the origin of fluorescence in these phytofluors, we solved the crystal structures of IFP1.4 and a comparison non-fluorescent monomeric phytochrome DrCBDmon. Met-186 and Val-288 in IFP1.4 are responsible for the formation of a tightly packed hydrophobic hub around the biliverdin D ring. Met-186 is also largely responsible for the blue-shifted IFP1.4 excitation maximum relative to the parent BphP. The structure of IFP1.4 revealed decreased structural heterogeneity and a contraction of two surface regions as direct consequences of side chain substitutions. Unexpectedly, IFP1.4 with Asp-207 reinstalled (IFPrev) has a higher fluorescence quantum yield (∼9%) than most NIR phytofluors published to date. In agreement, fluorescence lifetime measurements confirm the exceptionally long excited state lifetimes, up to 815 ps, in IFP1.4 and IFPrev. Our research helps delineate the origin of fluorescence in engineered BphPs and will facilitate the wide-spread adoption of phytofluors as biomarkers.

Indexed as

AnimalsBacteriaBiliverdineBiomarkersCloning, MolecularCrystallography, X-RayHydrogen BondingHydrophobic and Hydrophilic InteractionsLigandsModels, MolecularNitrogenPhytochromeProtein BindingProtein EngineeringProtein Structure, TertiarySpectrometry, FluorescenceBiliverdineBiomarkersLigandsNitrogenPhytochromeWaterFluorescencePhotoreceptorPhytochromeProtein EngineeringSpectroscopyStructural Biology

Identifiers

PMID25253687
PMCPMC4231690
OpenAlexW2035616558

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.