Evidence map›Paper›PMID 27019313›Full record

ArticleJournal of the American Chemical Society2016

The N-B Interaction through a Water Bridge: Understanding the Chemoselectivity of a Fluorescent Protein Based Probe for Peroxynitrite.

Zhi-jie Chen, Ziqi Tian, Karen Kallio, April L Oleson, Ao Ji, Dan Borchardt, De-en Jiang, S James Remington, Hui-wang Ai

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Review
  2. Review
  3. Small molecule probes for peroxynitrite detection.Redox biochemistry and chemistry · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
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  12. Review
  13. Article
  14. Article
  15. Playing with the Molecules of Life.ACS chemical biology · 2018
    Review
  16. Article
  17. 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

9 authors.

Zhi-jie ChenDepartment of Chemistry, University of California at Riverside , 501 Big Springs Road, Riverside, California 92521, United States.
Ziqi TianDepartment of Chemistry, University of California at Riverside , 501 Big Springs Road, Riverside, California 92521, United States.
Karen KallioDepartment of Physics and Institute of Molecular Biology, University of Oregon , Eugene, Oregon 97403, United States.
April L OlesonDepartment of Physics and Institute of Molecular Biology, University of Oregon , Eugene, Oregon 97403, United States.
Ao JiDepartment of Chemistry, University of California at Riverside , 501 Big Springs Road, Riverside, California 92521, United States.
Dan BorchardtDepartment of Chemistry, University of California at Riverside , 501 Big Springs Road, Riverside, California 92521, United States.
De-en JiangDepartment of Chemistry, University of California at Riverside , 501 Big Springs Road, Riverside, California 92521, United States.
S James RemingtonDepartment of Physics and Institute of Molecular Biology, University of Oregon , Eugene, Oregon 97403, United States.
Hui-wang AiDepartment of Chemistry, University of California at Riverside , 501 Big Springs Road, Riverside, California 92521, United States.

Funding

Lentiviral Systems for Controlled Mammalian Expression of Unnatural Fluorescent Protein ProbesR03EB020211 · NIBIB · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI AI, HUIWANG · 2015 to 2016
$152k
NIBIB NIH HHS R03 EB020211NIBIB NIH HHS R03EB020211
6 · The paper itself

Abstract

Boronic acid and esters have been extensively utilized for molecular recognition and chemical sensing. We recently reported a genetically encoded peroxynitrite (ONOO(-))-specific fluorescent sensor, pnGFP, based on the incorporation of a boronic acid moiety into a circularly permuted green fluorescent protein (cpGFP) followed by directed protein evolution. Different from typical arylboronic acids and esters, the chromophore of pnGFP is unreactive to millimolar concentrations of hydrogen peroxide (H2O2). The focus of this study is to explore the mechanism for the observed unusual chemoselectivity of pnGFP toward peroxynitrite over hydrogen peroxide by using site-directed mutagenesis, X-ray crystallography, (11)B NMR, and computational analysis. Our data collectively support that a His residue on the protein scaffold polarizes a water molecule to induce the formation of an sp(3)-hybridized boron in the chromophore, thereby tuning the reactivity of pnGFP with various reactive oxygen and nitrogen species (ROS/RNS). Our study demonstrates the first example of tunable boron chemistry in a folded nonnative protein, which offers wide implications in designing selective chemical probes.

Indexed as

Amino Acid SequenceBoronBoron CompoundsCrystallography, X-RayFluorescent DyesGreen Fluorescent ProteinsHydrogen PeroxideMagnetic Resonance SpectroscopyModels, MolecularMutagenesis, Site-DirectedPeroxynitrous AcidPhenylalanineSequence AlignmentSpectrometry, FluorescenceWater4-boronophenylalanineBoronBoron CompoundsFluorescent DyesGreen Fluorescent ProteinsHydrogen PeroxidePeroxynitrous AcidPhenylalanineWater

Identifiers

PMID27019313
PMCPMC4958459

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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.