Evidence map›Paper›PMID 42630285›Full record

ArticleNature catalysis2026

Protein-confined imidazolium intermediates enable diverse biocatalytic C-C and C-N bond formations.

Zachary Birch-Price, Amy E Hutton, Fei Zhao, Mary Ortmayer, Veronika Stoianova, Christian Merten, Colin Levy, Richard Obexer, Anthony P Green

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature catalysis, 2026. 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

9 authors.

Zachary Birch-PriceManchester Institute of Biotechnology and Department of Chemistry, The University of Manchester, Manchester, UK.ORCID 0000-0002-2024-3005
Amy E HuttonManchester Institute of Biotechnology and Department of Chemistry, The University of Manchester, Manchester, UK.
Fei ZhaoManchester Institute of Biotechnology and Department of Chemistry, The University of Manchester, Manchester, UK.ORCID 0000-0003-1841-4466
Mary OrtmayerManchester Institute of Biotechnology and Department of Chemistry, The University of Manchester, Manchester, UK.
Veronika StoianovaOrganische Chemie II, Fakultät für Chemie und Biochemie, Ruhr Universität Bochum, Bochum, Germany.ORCID 0000-0002-5492-8395
Christian MertenOrganische Chemie II, Fakultät für Chemie und Biochemie, Ruhr Universität Bochum, Bochum, Germany.ORCID 0000-0002-4106-1905
Colin LevyManchester Institute of Biotechnology and Department of Chemistry, The University of Manchester, Manchester, UK.
Richard ObexerManchester Institute of Biotechnology and Department of Chemistry, The University of Manchester, Manchester, UK.ORCID 0000-0002-4940-3543
Anthony P GreenManchester Institute of Biotechnology and Department of Chemistry, The University of Manchester, Manchester, UK.ORCID 0000-0003-0454-1798

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Developing enzymatic strategies to selectively construct C-C and C-heteroatom bonds is a major objective in modern biocatalysis. Here we combine genetic code reprogramming and laboratory evolution to establish a family of allylic transferase enzymes that can achieve a remarkable breadth of chemistry, enabling the generation of valuable motifs including γ‑butenolides, chiral amines and all-carbon quaternary centres. Our enzymes operate through the formation of electrophilic imidazolium intermediates that can be generated from reagents equipped with a

Indexed as

BiocatalysisEnzyme mechanismsX-ray crystallography

Identifiers

PMID42630285
PMCPMC13493319

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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.