Evidence map›Paper›PMID 41823132›Full record

ReviewBiochemical Society transactions2026

Heme oxygenase-like dimetal oxidases and oxygenases.

Sydney S Skirboll, Anastasia E Ledinina, Thomas M Makris

Abstract readReview
In one paragraph

Review in Biochemical Society transactions, 2026. 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. Thiooxazole Formation on a NontypeablebioRxiv : the preprint server for biology · 2026
    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

3 authors.

Sydney S SkirbollDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC 27695, U.S.A.ORCID 0009-0007-0805-3704
Anastasia E LedininaDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC 27695, U.S.A.ORCID 0000-0001-9703-1169
Thomas M MakrisDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC 27695, U.S.A.ORCID 0000-0001-7927-620X

Funding

National Science Foundation CHE 2507508
6 · The paper itself

Abstract

The first heme oxygenase-like dimetal oxidase/oxygenase (HDO) was functionally validated through coordinated spectroscopic and rapid kinetic studies of the fatty acid decarboxylase UndA. The enzyme superfamily has since been recognized to orchestrate a variety of substrate transformations for natural product biosynthesis. In this mini-review, we report on the structures and the catalytic mechanisms of the major HDO subtypes that catalyze carbon-carbon bond cleavage, N-oxygenation, multi-step rearrangements, and radical hole-hopping. A summary of the current status of the field and opportunities for decrypting the molecular basis for the mechanistic divergence of the family are highlighted.

Indexed as

Heme Oxygenase (Decyclizing)OxidoreductasesOxygenasesHumansModels, MolecularOxygenHeme Oxygenase (Decyclizing)OxidoreductasesOxygenOxygenasesBioinformaticsBiophysicsdiironMetalloenzymesoxygen activation

Identifiers

PMID41823132
PMCPMC13108848

What OpenQuestion holds

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LicenceCC BY
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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.