Evidence map›Paper›PMID 40739871›Full record

ArticleAngewandte Chemie (International ed. in English)2025

The Natural Redox Cofactor Pyrroloquinoline Quinone (PQQ) Enables Photocatalytic Radical Cyclizations.

Srishti B Bahukhandi, Andreas S Klein, Ghulam Mustafa, Maria Weyh, Alexandra Walter, Erling Thyrhaug, Jürgen Hauer, Golo Storch, Cathleen Zeymer

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Designing Enzymatic Reactivity with an Expanded Palette.Chembiochem : a European journal of chemical biology · 2025
    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

9 authors.

Srishti B BahukhandiCenter for Functional Protein Assemblies & Department of Bioscience, TUM School of Natural Sciences, Technical University of Munich (TUM), 85748, Garching, Germany.ORCID 0000-0002-2668-7483
Andreas S KleinCenter for Functional Protein Assemblies & Department of Bioscience, TUM School of Natural Sciences, Technical University of Munich (TUM), 85748, Garching, Germany.ORCID 0000-0001-8075-3480
Ghulam MustafaCenter for Functional Protein Assemblies & Department of Bioscience, TUM School of Natural Sciences, Technical University of Munich (TUM), 85748, Garching, Germany.
Maria WeyhCenter for Functional Protein Assemblies & Department of Bioscience, TUM School of Natural Sciences, Technical University of Munich (TUM), 85748, Garching, Germany.ORCID 0000-0002-5792-2298
Alexandra WalterDepartment of Chemistry, TUM School of Natural Sciences, Technical University of Munich (TUM), 85748, Garching, Germany.
Erling ThyrhaugDepartment of Chemistry, TUM School of Natural Sciences, Technical University of Munich (TUM), 85748, Garching, Germany.ORCID 0000-0001-8634-9606
Jürgen HauerDepartment of Chemistry, TUM School of Natural Sciences, Technical University of Munich (TUM), 85748, Garching, Germany.ORCID 0000-0002-6874-6138
Golo StorchDepartment of Chemistry, TUM School of Natural Sciences, Technical University of Munich (TUM), 85748, Garching, Germany.ORCID 0000-0002-6747-3035
Cathleen ZeymerCenter for Functional Protein Assemblies & Department of Bioscience, TUM School of Natural Sciences, Technical University of Munich (TUM), 85748, Garching, Germany.ORCID 0000-0001-7138-381X

Funding

German Research Foundation (SFB/Transregio 325) 444632635
6 · The paper itself

Abstract

Photoenzymatic catalysis facilitates stereoselective new-to-nature chemistry under mild conditions. In addition to the rational design of artificial photoenzymes, naturally occurring redox enzymes can be repurposed to promote photoredox catalysis in the chiral protein environment. Here, we show that enzymes utilizing the pyrroloquinoline quinone (PQQ) cofactor expand the toolbox of photobiocatalysis. PQQ absorbs visible light and is capable of single-electron transfer. It thus exhibits mechanistic similarities to flavin cofactors, which are widely used for photoenzymatic approaches. First, we established the trimethyl ester PQQMe

Indexed as

PQQ CofactorCatalysisCyclizationFree RadicalsMolecular StructureOxidation-ReductionPhotochemical ProcessesFree RadicalsPQQ CofactorBiocatalysisPhotoenzymePhotoredox catalysisPyrroloquinoline quinoneRadical reactions

Identifiers

PMID40739871
PMCPMC12462760

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.