Evidence map›Paper›PMID 41616059›Full record

ArticleScience advances2026

Computational rational design of unspecific peroxygenase for C-H oxidation.

Ruichen Gao, Xiaodi Fu, Zonglin Li, Zhiyao Wang, Guanjian Li, Jun Ge, Frank Hollmann, Zhanfeng Wang, Wen-Yong Lou, Xiaoling Wu

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

10 authors.

Ruichen GaoLab of Applied Biocatalysis, Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, School of Food Science and Engineering, South China University of Technology, Guangdong 510006, China.ORCID 0000-0002-5652-2225
Xiaodi FuCenter for Advanced Materials Research & Faculty of Arts and Sciences, Beijing Normal University, Zhuhai 519087, China.ORCID 0009-0006-5411-8161
Zonglin LiState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai 200237, China.ORCID 0000-0002-1729-9593
Zhiyao WangLab of Applied Biocatalysis, Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, School of Food Science and Engineering, South China University of Technology, Guangdong 510006, China.
Guanjian LiLab of Applied Biocatalysis, Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, School of Food Science and Engineering, South China University of Technology, Guangdong 510006, China.ORCID 0009-0008-4541-4027
Jun GeKey Laboratory for Industrial Biocatalysis, Ministry of Education, Department of Chemical Engineering, Tsinghua University, Beijing 100084, China.ORCID 0000-0001-5503-8899
Frank HollmannDepartment of Biotechnology, Delft University of Technology, Van der Maasweg 9, Delft 2629 HZ, Netherlands.ORCID 0000-0003-4821-756X
Zhanfeng WangCenter for Advanced Materials Research & Faculty of Arts and Sciences, Beijing Normal University, Zhuhai 519087, China.ORCID 0000-0001-6722-2298
Wen-Yong LouLab of Applied Biocatalysis, Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, School of Food Science and Engineering, South China University of Technology, Guangdong 510006, China.ORCID 0000-0003-3474-3446
Xiaoling WuLab of Applied Biocatalysis, Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, School of Food Science and Engineering, South China University of Technology, Guangdong 510006, China.ORCID 0009-0008-0248-3196

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Computational rational design has emerged as a transformative approach to engineer enzymes with tailored selectivity and efficiency. In the context of carbon-hydrogen oxidation, a key challenge in synthetic chemistry, unspecific peroxygenases (UPOs) directly oxidize unactivated carbon-hydrogen bonds using hydrogen peroxide, yet their utility is limited by low activity and imperfect selectivity. By computational rational design, this study systematically navigated vast sequence spaces to identify mutations that enhance catalytic performance of UPOs, lastly yielded UPO variants with 13-fold enhanced activity and >99% enantioselectivity, and revealed the dominant role of residue Lys

Indexed as

CarbonHydrogenMixed Function OxygenasesProtein EngineeringBiocatalysisHydrogen PeroxideModels, MolecularMutationOxidation-ReductionCarbonHydrogenHydrogen PeroxideMixed Function Oxygenasesperoxygenase

Identifiers

PMID41616059
PMCPMC12857729

What OpenQuestion holds

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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.