Evidence map›Paper›PMID 41883849›Full record

ArticleChemical science2026

Enantioselective electrophilic α-fluorination catalyzed by an artificial metalloenzyme.

Jinmeng Yu, Chang Wang, Wenhao Hu, Huan Wang, Jing Zhao, Hui-Jie Pan

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Article in Chemical science, 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
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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

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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

6 authors.

Jinmeng YuState Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), ChemBioMed Interdisciplinary Research Center at Nanjing University, School of Chemistry and Chemical Engineering, Nanjing University Nanjing 210023 P. R. China huijie.pan@nju.edu.cn.
Chang WangState Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), ChemBioMed Interdisciplinary Research Center at Nanjing University, School of Chemistry and Chemical Engineering, Nanjing University Nanjing 210023 P. R. China huijie.pan@nju.edu.cn.
Wenhao HuState Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), ChemBioMed Interdisciplinary Research Center at Nanjing University, School of Chemistry and Chemical Engineering, Nanjing University Nanjing 210023 P. R. China huijie.pan@nju.edu.cn.
Huan WangState Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), ChemBioMed Interdisciplinary Research Center at Nanjing University, School of Chemistry and Chemical Engineering, Nanjing University Nanjing 210023 P. R. China huijie.pan@nju.edu.cn.ORCID https://orcid.org/0000-0003-1585-6760
Jing ZhaoState Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), ChemBioMed Interdisciplinary Research Center at Nanjing University, School of Chemistry and Chemical Engineering, Nanjing University Nanjing 210023 P. R. China huijie.pan@nju.edu.cn.ORCID https://orcid.org/0000-0001-5177-5699
Hui-Jie PanState Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), ChemBioMed Interdisciplinary Research Center at Nanjing University, School of Chemistry and Chemical Engineering, Nanjing University Nanjing 210023 P. R. China huijie.pan@nju.edu.cn.ORCID https://orcid.org/0000-0003-3737-3524

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluorine incorporation profoundly influences the properties of pharmaceuticals and imaging agents, yet enzymatic C-F bond formation remains exceedingly rare. Here we report an enantioselective electrophilic α-fluorination catalyzed by an artificial metalloenzyme assembled from a biotinylated Cu(ii) Lewis acid cofactor embedded in streptavidin. Targeted mutagenesis of residues S112 and K121 yielded variants delivering up to 95% ee. Substrate scope studies revealed distinct steric and electronic influences on both reactivity and selectivity. Docking and molecular dynamics simulations indicate that precise cofactor positioning and steric shielding from K121Q govern the approach of the electrophilic fluorinating reagent, accounting for the observed enantioselectivity. These findings demonstrate that electrophilic fluorination chemistry can be engineered into protein environments and highlight the broader potential of artificial metalloenzymes to enable new-to-nature biotransformations.

Identifiers

PMID41883849
PMCPMC13011859

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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.