Evidence map›Paper›PMID 36326150›Full record

ArticleThe journal of physical chemistry. B2022

Observation of Cation Chromophore Photoisomerization of a Fluorescent Protein Using Millisecond Synchrotron Serial Crystallography and Infrared Vibrational and Visible Spectroscopy.

James M Baxter, Christopher D M Hutchison, Karim Maghlaoui, Violeta Cordon-Preciado, R Marc L Morgan, Pierre Aller, Agata Butryn, Danny Axford, Sam Horrell, Robin L Owen and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.6field-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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
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 at 3 institutions in 1 country.

James M BaxterDepartment of Life Sciences, Imperial College London, LondonSW7 2AZ, United Kingdom.ORCID 0000-0002-4641-6760
Christopher D M HutchisonDepartment of Life Sciences, Imperial College London, LondonSW7 2AZ, United Kingdom.
Karim MaghlaouiDepartment of Life Sciences, Imperial College London, LondonSW7 2AZ, United Kingdom.
Violeta Cordon-PreciadoDepartment of Life Sciences, Imperial College London, LondonSW7 2AZ, United Kingdom.
R Marc L MorganDepartment of Life Sciences, Imperial College London, LondonSW7 2AZ, United Kingdom.
Pierre AllerResearch Complex at Harwell, Rutherford Appleton Laboratory, DidcotOX11 0FAUnited Kingdom.ORCID 0000-0002-1793-7030
Agata ButrynResearch Complex at Harwell, Rutherford Appleton Laboratory, DidcotOX11 0FAUnited Kingdom.ORCID 0000-0002-5227-4770
Danny AxfordDiamond Light Source, Harwell Science and Innovation Campus, DidcotOX11 0DE, United Kingdom.
Sam HorrellDiamond Light Source, Harwell Science and Innovation Campus, DidcotOX11 0DE, United Kingdom.
Robin L OwenDiamond Light Source, Harwell Science and Innovation Campus, DidcotOX11 0DE, United Kingdom.
Selina L S StormDiamond Light Source, Harwell Science and Innovation Campus, DidcotOX11 0DE, United Kingdom.
Nicholas E DevenishDiamond Light Source, Harwell Science and Innovation Campus, DidcotOX11 0DE, United Kingdom.
Jasper J van ThorDepartment of Life Sciences, Imperial College London, LondonSW7 2AZ, United Kingdom.ORCID 0000-0001-6356-3116
Imperial College London · GBDiamond Light Source · GBRutherford Appleton Laboratory · GB

Funding

Biotechnology and Biological Sciences Research Council BB/P00752X/1
6 · The paper itself

Abstract

The chromophores of reversibly switchable fluorescent proteins (rsFPs) undergo photoisomerization of both the trans and cis forms. Concurrent with cis/trans photoisomerisation, rsFPs typically become protonated on the phenolic oxygen resulting in a blue shift of the absorption. A synthetic rsFP referred to as rsEospa, derived from EosFP family, displays the same spectroscopic behavior as the GFP-like rsFP Dronpa at pH 8.4 and involves the photoconversion between nonfluorescent neutral and fluorescent anionic chromophore states. Millisecond time-resolved synchrotron serial crystallography of rsEospa at pH 8.4 shows that photoisomerization is accompanied by rearrangements of the same three residues as seen in Dronpa. However, at pH 5.5 we observe that the OFF state is identified as the cationic chromophore with additional protonation of the imidazolinone nitrogen which is concurrent with a newly formed hydrogen bond with the Glu212 carboxylate side chain. FTIR spectroscopy resolves the characteristic up-shifted carbonyl stretching frequency at 1713 cm

Indexed as

NitrogenSynchrotronsCationsCrystallography, X-RayLuminescent ProteinsSpectroscopy, Fourier Transform InfraredCationsLuminescent ProteinsNitrogen

Identifiers

PMID36326150
PMCPMC9677427
OpenAlexW4308060167

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.