Evidence map›Paper›PMID 29488750›Full record

ArticleThe journal of physical chemistry. A2018

High-Frequency/High-Field Electron Paramagnetic Resonance and Theoretical Studies of Tryptophan-Based Radicals.

Ian Davis, Teruaki Koto, James R Terrell, Alexander Kozhanov, J Krzystek, Aimin Liu

Abstract read
In one paragraph

Article in The journal of physical chemistry. A, 2018. 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
0.5field-weighted citation impact, top 39% 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, 10 citations in OpenAlex.

  1. Fluorinated Tryptophan Derivatives for Photo-CIDNP NMR.The journal of physical chemistry. B · 2026
    Article
  2. Catalase-peroxidase (KatG): a potential frontier in tuberculosis drug development.Critical reviews in biochemistry and molecular biology · 2024
    Review
  3. 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

6 authors at 3 institutions in 1 country.

Ian DavisDepartment of Chemistry , University of Texas , San Antonio , Texas 78249 , United States.
Teruaki KotoDepartment of Chemistry , University of Texas , San Antonio , Texas 78249 , United States.
James R TerrellDepartment of Chemistry , Georgia State University , Atlanta , Georgia 30303 , United States.
Alexander KozhanovDepartment of Physics and Astronomy , Georgia State University , Atlanta , Georgia 30303 , United States.
J KrzystekNational High Magnetic Field Laboratory , Florida State University , Tallahassee , Florida 32310 , United States.
Aimin LiuDepartment of Chemistry , University of Texas , San Antonio , Texas 78249 , United States.ORCID http://orcid.org/0000-0002-4182-8176
Georgia State University · USThe University of Texas at San Antonio · USFlorida State University · US

Funding

Heme-dependent chemistry in tyrosine oxidation: Diversity Supplement on 5R01GM108988-08 for supporting Samuel MontoyaR01GM108988 · NIGMS · UNIVERSITY OF TEXAS SAN ANTONIO · PI LIU, AIMIN · 2014 to 2025
$4.2M
NIGMS NIH HHS R01 GM108988
6 · The paper itself

Abstract

Tryptophan-based free radicals have been implicated in a myriad of catalytic and electron transfer reactions in biology. However, very few of them have been trapped so that biophysical characterizations can be performed in a high-precision context. In this work, tryptophan derivative-based radicals were studied by high-frequency/high-field electron paramagnetic resonance (HFEPR) and quantum chemical calculations. Radicals were generated at liquid nitrogen temperature with a photocatalyst, sacrificial oxidant, and violet laser. The precise g-anisotropies of l- and d-tryptophan, 5-hydroxytryptophan, 5-methoxytryptophan, 5-fluorotryptophan, and 7-hydroxytryptophan were measured directly by HFEPR. Quantum chemical calculations were conducted to predict both neutral and cationic radical spectra for comparison with the experimental data. The results indicate that under the experimental conditions, all radicals formed were cationic. Spin densities of the radicals were also calculated. The various line patterns and g-anisotropies observed by HFEPR can be understood in terms of spin-density populations and the positioning of oxygen atom substitution on the tryptophan ring. The results are considered in the light of the tryptophan and 7-hydroxytryptophan diradical found in the biosynthesis of the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase.

Identifiers

PMID29488750
PMCPMC5876142
OpenAlexW2788193065

What OpenQuestion holds

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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.