Evidence map›Paper›PMID 39115259›Full record

ArticleJournal of the American Chemical Society2024

A De Novo Metalloenzyme for Cerium Photoredox Catalysis.

Andreas Sebastian Klein, Florian Leiss-Maier, Rahel Mühlhofer, Benedikt Boesen, Ghulam Mustafa, Hannah Kugler, Cathleen Zeymer

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Reprogramming NAD(P)Angewandte Chemie (International ed. in English) · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  13. Designing and Engineering Enzymes for New-to-Nature Photobiocatalysis.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

7 authors.

Andreas Sebastian 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
Florian Leiss-MaierCenter for Functional Protein Assemblies & Department of Bioscience, TUM School of Natural Sciences, Technical University of Munich (TUM), 85748 Garching, Germany.ORCID 0000-0002-0641-973X
Rahel MühlhoferCenter for Functional Protein Assemblies & Department of Bioscience, TUM School of Natural Sciences, Technical University of Munich (TUM), 85748 Garching, Germany.ORCID 0009-0008-7033-8521
Benedikt BoesenCenter for Functional Protein Assemblies & Department of Bioscience, TUM School of Natural Sciences, Technical University of Munich (TUM), 85748 Garching, Germany.ORCID 0000-0003-1010-3671
Ghulam MustafaCenter for Functional Protein Assemblies & Department of Bioscience, TUM School of Natural Sciences, Technical University of Munich (TUM), 85748 Garching, Germany.ORCID 0000-0002-1085-5163
Hannah KuglerCenter for Functional Protein Assemblies & Department of Bioscience, TUM School of Natural Sciences, Technical University of Munich (TUM), 85748 Garching, Germany.
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

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cerium photoredox catalysis has emerged as a powerful strategy to activate molecules under mild conditions. Radical intermediates are formed using visible light and simple complexes of the earth-abundant lanthanide. Here, we report an artificial photoenzyme enabling this chemistry inside a protein. We utilize a de novo designed protein scaffold that tightly binds lanthanide ions in its central cavity. Upon visible-light irradiation, the cerium-dependent enzyme catalyzes the radical C-C bond cleavage of 1,2-diols in aqueous solution. Protein engineering led to variants with improved photostability and metal binding behavior. The photoenzyme cleaves a range of aromatic and aliphatic substrates, including lignin surrogates. Surface display of the protein scaffold on

Indexed as

CeriumMetalloproteinsOxidation-ReductionPhotochemical ProcessesBiocatalysisCatalysisEscherichia coliLightModels, MolecularCeriumMetalloproteins

Identifiers

PMID39115259
PMCPMC11440500

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.