Evidence map›Paper›PMID 39092113›Full record

ArticleChemical science2024

Non-Aufbau electronic structure in radical enzymes and control of the highly reactive intermediates.

M Hossein Khalilian, Gino A DiLabio

Abstract read
In one paragraph

Article in Chemical science, 2024. 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. 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

2 authors.

M Hossein KhalilianDepartment of Chemistry, The University of British Columbia 3247 University Way Kelowna British Columbia V1V 1V7 Canada Gino.DiLabio@ubc.ca +1-250-807-6617.
Gino A DiLabioDepartment of Chemistry, The University of British Columbia 3247 University Way Kelowna British Columbia V1V 1V7 Canada Gino.DiLabio@ubc.ca +1-250-807-6617.ORCID https://orcid.org/0000-0002-3778-3892

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Radicals are highly reactive, short-lived chemical species that normally react indiscriminately with biological materials, and yet, nature has evolved thousands of enzymes that employ radicals to catalyze thermodynamically challenging chemistry. How these enzymes harness highly reactive radical intermediates to steer the catalysis to the correct outcome is a topic of intense investigation. Here, the results of detailed QM/MM calculations on archetype radical B

Identifiers

PMID39092113
PMCPMC11290419

What OpenQuestion holds

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LicenceCC BY-NC
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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.