Evidence map›Paper›PMID 35036041›Full record

ArticleACS catalysis2022

Photobiocatalytic Oxyfunctionalization with High Reaction Rate using a Baeyer-Villiger Monooxygenase from

Elif Erdem, Lenny Malihan-Yap, Leen Assil-Companioni, Hanna Grimm, Giovanni Davide Barone, Carole Serveau-Avesque, Agnes Amouric, Katia Duquesne, Véronique de Berardinis, Yagut Allahverdiyeva and 2 more

Open access · hybridAbstract read
In one paragraph

Article in ACS catalysis, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.0field-weighted citation impact, top 7% of its field
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

16 citing papers in PubMed, 45 citations in OpenAlex.

  1. Toward Sustainability: Intensification of Light-Driven Whole Cell Biocatalysis.Chembiochem : a European journal of chemical biology · 2026
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  2. Optimising COMicrobial cell factories · 2025
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  14. Light-driven biocatalytic oxidation.Chemical science · 2022
    Review
  15. Article
  16. 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

12 authors at 3 institutions in 4 countries.

Elif ErdemInstitute of Molecular Biotechnology, Graz University of Technology, NAWI Graz, Petersgasse 14, 8010 Graz, Austria.ORCID https://orcid.org/0000-0003-1411-9793
Lenny Malihan-YapInstitute of Molecular Biotechnology, Graz University of Technology, NAWI Graz, Petersgasse 14, 8010 Graz, Austria.
Leen Assil-CompanioniInstitute of Molecular Biotechnology, Graz University of Technology, NAWI Graz, Petersgasse 14, 8010 Graz, Austria.
Hanna GrimmInstitute of Molecular Biotechnology, Graz University of Technology, NAWI Graz, Petersgasse 14, 8010 Graz, Austria.
Giovanni Davide BaroneInstitute of Molecular Biotechnology, Graz University of Technology, NAWI Graz, Petersgasse 14, 8010 Graz, Austria.
Carole Serveau-AvesqueAix Marseille Univ, CNRS, Centrale Marseille, iSm2 UMR7313, 13397 Marseille, France.
Agnes AmouricAix Marseille Univ, CNRS, Centrale Marseille, iSm2 UMR7313, 13397 Marseille, France.
Katia DuquesneAix Marseille Univ, CNRS, Centrale Marseille, iSm2 UMR7313, 13397 Marseille, France.
Véronique de BerardinisGénomique métabolique, Genoscope, Institut François Jacob, CEA, CNRS, Univ Evry, Université Paris-Saclay, 91057 Evry, France.
Yagut AllahverdiyevaMolecular Plant Biology Unit, Department of Life Technologies, Faculty of Technology, University of Turku, Turku 20014, Finland.
Véronique AlphandAix Marseille Univ, CNRS, Centrale Marseille, iSm2 UMR7313, 13397 Marseille, France.ORCID https://orcid.org/0000-0001-6855-7292
Robert KouristInstitute of Molecular Biotechnology, Graz University of Technology, NAWI Graz, Petersgasse 14, 8010 Graz, Austria.ORCID https://orcid.org/0000-0002-2853-3525
Institute of Molecular Biotechnology · ATCentre National de la Recherche Scientifique · FRUniversity of Turku · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Baeyer-Villiger monooxygenases (BVMOs) catalyze the oxidation of ketones to lactones under very mild reaction conditions. This enzymatic route is hindered by the requirement of a stoichiometric supply of auxiliary substrates for cofactor recycling and difficulties with supplying the necessary oxygen. The recombinant production of BVMO in cyanobacteria allows the substitution of auxiliary organic cosubstrates with water as an electron donor and the utilization of oxygen generated by photosynthetic water splitting. Herein, we report the identification of a BVMO from

Identifiers

PMID35036041
PMCPMC8751089
OpenAlexW4200342105

What OpenQuestion holds

Textmetadata
LicenceCC BY
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 OpenQuestion graph.