Evidence map›Paper›PMID 39890795›Full record

ArticleNature communications2025

Ground-state flavin-dependent enzymes catalyzed enantioselective radical trifluoromethylation.

Xinyu Duan, Dong Cui, Mengdi Wang, Chenlu Jin, Xiaochen Cai, Zhiguo Wang, Jian Xu

Abstract read
In one paragraph

Article in Nature communications, 2025. 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. Article
  2. Harnessing Photoenzymatic Systems for Intermolecular C-H Fluorination.Angewandte Chemie (International ed. in English) · 2026
    Article
  3. Review
  4. Designing and Engineering Enzymes for New-to-Nature Photobiocatalysis.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  5. Article
  6. Article
  7. 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.

Xinyu Duan *College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, China.
Dong Cui *College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, China.
Mengdi Wang *College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, China.
Chenlu JinCollege of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, China.
Xiaochen CaiCollege of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, China.
Zhiguo WangInstitute of Ageing Research, School of Basic Medical Sciences, Hangzhou Normal University, Hangzhou, China. zhgwang@aliyun.com.ORCID http://orcid.org/0000-0001-8732-4451
Jian XuCollege of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, China. jianxu@zjut.edu.cn.ORCID http://orcid.org/0000-0003-1765-9701

Funding

National Natural Science Foundation of China (National Science Foundation of China) 22171243National Natural Science Foundation of China (National Science Foundation of China) 22322705
6 · The paper itself

Abstract

The introduction of fluoroalkyl groups into pharmaceutical compounds has the potential to enhance their therapeutic properties. Nevertheless, the synthesis of enantiomerically pure C(sp³)-CF₃ compounds poses a significant challenge. Biocatalysis offers precise stereochemical control, however, the scarcity of fluorine-containing natural products makes it difficult to find enzymes capable of incorporating fluoroalkyl groups. Herein, we develop a ground-state flavin-dependent enzyme-catalyzed strategy for the radical-mediated enantioselective trifluoromethylation. Two engineered flavin-dependent enzymes are successfully developed to catalyze stereoselective hydrotrifluoromethylation and trifluoromethyl-alkyl cross-electrophile coupling reactions using trifluoromethyl thianthrenium triflate as a radical donor. Experimental investigations and computational simulations demonstrate that the reaction is initiated through single-electron transfer from the ground state flavin hydroquinone (FMN

Indexed as

FlavinsBiocatalysisCatalysisFlavin-Adenine DinucleotideMethylationStereoisomerismFlavin-Adenine DinucleotideFlavinsflavin semiquinone

Identifiers

PMID39890795
PMCPMC11785956

What OpenQuestion holds

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Registered trials

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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.