Evidence map›Paper›PMID 32451409›Full record

ArticleNature communications2020

Photoinduced monooxygenation involving NAD(P)H-FAD sequential single-electron transfer.

Simon Ernst, Stefano Rovida, Andrea Mattevi, Susanne Fetzner, Steffen L Drees

Abstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Characterization of successiveApplied and environmental microbiology · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Ultrafast photooxidation of protein-bound anionic flavin radicals.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Substrate Inhibition of 5β-ΔFrontiers in microbiology · 2021
    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

5 authors.

Simon ErnstInstitute for Molecular Microbiology and Biotechnology, University of Münster, Corrensstr. 3, 48149, Münster, Germany.
Stefano RovidaDepartment of Biology and Biotechnology "Lazzaro Spallanzani", University of Pavia, via Ferrata 9, 27100, Pavia, Italy.
Andrea MatteviDepartment of Biology and Biotechnology "Lazzaro Spallanzani", University of Pavia, via Ferrata 9, 27100, Pavia, Italy.ORCID http://orcid.org/0000-0002-9523-7128
Susanne FetznerInstitute for Molecular Microbiology and Biotechnology, University of Münster, Corrensstr. 3, 48149, Münster, Germany.ORCID http://orcid.org/0000-0002-7228-1871
Steffen L DreesInstitute for Molecular Microbiology and Biotechnology, University of Münster, Corrensstr. 3, 48149, Münster, Germany. s.drees@uni-muenster.de.ORCID http://orcid.org/0000-0001-9140-0111

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Light-dependent or light-stimulated catalysis provides a multitude of perspectives for implementation in technological or biomedical applications. Despite substantial progress made in the field of photobiocatalysis, the number of usable light-responsive enzymes is still very limited. Flavoproteins have exceptional potential for photocatalytic applications because the name-giving cofactor intrinsically features light-dependent reactivity, undergoing photoreduction with a variety of organic electron donors. However, in the vast majority of these enzymes, photoreactivity of the enzyme-bound flavin is limited or even suppressed. Here, we present a flavoprotein monooxygenase in which catalytic activity is controllable by blue light illumination. The reaction depends on the presence of nicotinamide nucleotide-type electron donors, which do not support the reaction in the absence of light. Employing various experimental approaches, we demonstrate that catalysis depends on a protein-mediated photoreduction of the flavin cofactor, which proceeds via a radical mechanism and a transient semiquinone intermediate.

Indexed as

Electron TransportBacterial ProteinsBiocatalysisCrystallography, X-RayElectron-Transferring FlavoproteinsFlavin-Adenine DinucleotideLightMixed Function OxygenasesModels, MolecularNADNADPOxidation-ReductionPhotochemical ProcessesPseudomonas aeruginosaBacterial ProteinsElectron-Transferring FlavoproteinsFlavin-Adenine DinucleotideMixed Function OxygenasesNADNADP

Identifiers

PMID32451409
PMCPMC7248105

What OpenQuestion holds

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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.