Evidence map›Paper›PMID 40353189›Full record

ArticleChemical science2025

Modulation of heme peroxo nucleophilicities with axial ligands reveal key insights into the mechanistic landscape of nitric oxide synthase.

Shanuk Rajapakse, Yuri Lee, Samith B Jayawardana, Joshua Helms, Pritam Mondal, Akhil Singh, Brad S Pierce, Hannah S Shafaat, Gayan B Wijeratne

Abstract read
In one paragraph

Article in Chemical science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

9 authors.

Shanuk RajapakseDepartment of Chemistry and Biochemistry, University of Alabama Tuscaloosa AL 35401 USA gwijeratne@ua.edu.ORCID https://orcid.org/0000-0002-6001-8881
Yuri LeeDepartment of Chemistry and Biochemistry, University of California Los Angeles CA 90095 USA shafaat@ucla.edu.ORCID https://orcid.org/0000-0002-3413-7764
Samith B JayawardanaDepartment of Chemistry and Biochemistry, University of Alabama Tuscaloosa AL 35401 USA gwijeratne@ua.edu.ORCID https://orcid.org/0000-0002-6251-7692
Joshua HelmsDepartment of Chemistry and Biochemistry, University of Alabama Tuscaloosa AL 35401 USA gwijeratne@ua.edu.
Pritam MondalDepartment of Chemistry and Biochemistry, University of Alabama Tuscaloosa AL 35401 USA gwijeratne@ua.edu.ORCID https://orcid.org/0000-0002-7071-1970
Akhil SinghDepartment of Chemistry and Biochemistry, University of Alabama Tuscaloosa AL 35401 USA gwijeratne@ua.edu.ORCID https://orcid.org/0000-0002-4326-9152
Brad S PierceDepartment of Chemistry and Biochemistry, University of Alabama Tuscaloosa AL 35401 USA gwijeratne@ua.edu.ORCID https://orcid.org/0000-0002-7432-6332
Hannah S ShafaatDepartment of Chemistry and Biochemistry, University of California Los Angeles CA 90095 USA shafaat@ucla.edu.ORCID https://orcid.org/0000-0003-0793-4650
Gayan B WijeratneDepartment of Chemistry and Biochemistry, University of Alabama Tuscaloosa AL 35401 USA gwijeratne@ua.edu.ORCID https://orcid.org/0000-0001-7609-6406

Funding

Metallobiochemistry of Mn/Fe protein cofactorsR35GM128852 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Hannah S Shafaat · 2018 to 2026
$2.3M
Pre-steady state kinetics and O2/NO-reactivity among thiol dioxygenase enzymesR15GM117511 · NIGMS · UNIVERSITY OF TEXAS ARLINGTON · PI PIERCE, BRADLEY S · 2015 to 2023
$1.2M
NIGMS NIH HHS R15 GM117511NIGMS NIH HHS R35 GM128852
6 · The paper itself

Abstract

Mid-valent heme-oxygen intermediates are central to a medley of pivotal physiological transformations in humans, and such systems are increasingly becoming more relevant therapeutic targets for challenging disease conditions. Nonetheless, precise mechanistic details pertaining to mid-valent heme intermediates as well as key structure-activity relationships remain enigmatic. To this end, this study strives to describe the influence of heme proximal ligation on the nucleophilic reactivity patterns of heme peroxo intermediates. A functional model system in which organic oxime substrates are used as

Identifiers

PMID40353189
PMCPMC12062894

What Socratic holds

Textmetadata
LicenceCC BY-NC
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 Socratic graph.