Evidence map›Paper›PMID 42818196›Full record

ArticlebioRxiv : the preprint server for biology2026

A binuclear copper enzyme platform for enantioconvergent radical (pseudo)halogenation.

Xiao-Wang Chen, Oluwatosin Maryam Adeyemo, Heyu Chen, Hongda Chen, Ngoc Nguyen, Joseph Palazzo, Liu-Peng Zhao, Ken Lin, Binh Khanh Mai, Peng Liu and 2 more

Abstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 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

12 authors.

Xiao-Wang ChenDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, United States.ORCID 0009-0001-1465-0747
Oluwatosin Maryam AdeyemoJames Tarpo Jr. and Margaret Tarpo Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, United States.
Heyu ChenDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, United States.
Hongda ChenDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, United States.
Ngoc NguyenJames Tarpo Jr. and Margaret Tarpo Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, United States.
Joseph PalazzoJames Tarpo Jr. and Margaret Tarpo Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, United States.
Liu-Peng ZhaoDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, United States.
Ken LinDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, United States.
Binh Khanh MaiDepartment of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States.
Peng LiuDepartment of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States.
Shiliang TianJames Tarpo Jr. and Margaret Tarpo Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, United States.
Yang YangDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, United States.ORCID 0000-0002-4956-2034

Funding

An Evolvable Metalloenzyme Platform for Stereoselective Radical BiocatalysisR35GM147387 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI Yang Yang · 2022 to 2026
$2.0M
Deciphering the Structures and Mechanisms of Metalloproteins Involved in Human Iron HomeostasisR35GM155016 · NIGMS · PURDUE UNIVERSITY · PI Shiliang Tian · 2024 to 2026
$1.1M
NIGMS NIH HHS R35 GM147387NIGMS NIH HHS R35 GM155016
6 · The paper itself

Abstract

Despite their intriguing native metalloenzymology, naturally occurring copper enzymes remain largely underexploited for new-to-nature biocatalytic reactions. Herein, we report the systematic investigation and reprogramming of natural copper enzymes to catalyze unnatural free radical (pseudo)halogenation reaction in a highly enantioselective fashion. Evaluating Cu enzymes in the decarboxylative azidation of redox-active esters revealed activity across multiple Cu enzyme families, with type III binuclear Cu enzymes, particularly the

Identifiers

PMID42818196
PMCPMC13622139

What OpenQuestion holds

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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.