Evidence map›Paper›PMID 41221500›Full record

ArticleBiophysics reports2025

Porphyrins as cofactors in enzyme-catalyzed organic reactions.

Rui Wang, Jinghui Zhang

Abstract read
In one paragraph

Article in Biophysics reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Rui WangHefei National Laboratory for Physical Sciences at the Microscale and Department of Chemistry, University of Science and Technology of China, Hefei 230026, China.
Jinghui ZhangHefei National Laboratory for Physical Sciences at the Microscale and Department of Chemistry, University of Science and Technology of China, Hefei 230026, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Porphyrins, a class of cyclic compounds featuring a metal ion at the core of their macrocyclic structure, have long been recognized as indispensable cofactors in natural enzymatic processes. These porphyrin-based enzymes enable a wide variety of complex biochemical transformations under mild conditions with high yield, regioselectivity and stereoselectivity. As mimics of P450 enzymes, the integration of porphyrins into artificial enzymatic systems to catalyze unnatural organic reactions represents a rapidly advancing research area. Such reactions, those typically catalyzed by small molecule catalysts, are of significant interest in synthetic chemistry. This mini-review explores the role of porphyrins in both enzyme-catalyzed natural and unnatural organic reactions, with a focus on their use as cofactors in engineered metalloenzymes.

Indexed as

Artificial metalloenzymesCofactorsEnzyme-catalyzedOrganic reactionsPorphyrins

Identifiers

PMID41221500
PMCPMC12602113

What OpenQuestion holds

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Registered trials

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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.