Evidence map›Paper›PMID 39260996›Full record

ArticleMethods in enzymology2024

Radical-relay C(sp

Qun Zhao, Jinyan Rui, Xiongyi Huang

Abstract read
In one paragraph

Article in Methods in enzymology, 2024. 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

3 authors.

Qun ZhaoSchool of Biotechnology and Key Laboratory of Industrial Biotechnology of Ministry of Education, Jiangnan University, Wuxi, P.R. China. Electronic address: qunzhao@jiangnan.edu.cn.
Jinyan RuiDepartment of Chemistry, Johns Hopkins University, Baltimore, MD, United States.
Xiongyi HuangDepartment of Chemistry, Johns Hopkins University, Baltimore, MD, United States. Electronic address: xiongyi@jhu.edu.

Funding

A Chemo-Mimetic Platform to Reprogram Metalloenzymes for Non-Natural Biocatalytic C-H Functionalization ReactionsR35GM147639 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Xiongyi Huang · 2022 to 2026
$2.1M
Expanding the chemistry of life: New enzymatic platforms for synthesis of bioactive organofluorinesR00GM129419 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HUANG, XIONGYI · 2020 to 2022
$747k
NIGMS NIH HHS R00 GM129419NIGMS NIH HHS R35 GM147639
6 · The paper itself

Abstract

Nonheme iron enzymes are versatile biocatalysts for a broad range of unique and powerful transformations, such as hydroxylation, chlorination, and epimerization as well as cyclization/ring-opening of organic molecules. Beyond their native biological functions, these enzymes are robust for engineering due to their structural diversity and high evolvability. Based on enzyme promiscuity and directed evolution as well as inspired by synthetic organic chemistry, nonheme iron enzymes can be repurposed to catalyze reactions previously only accessible with synthetic catalysts. To this end, our group has engineered a series of nonheme iron enzymes to employ non-natural radical-relay mechanisms for new-to-nature radical transformations. In particular, we have demonstrated that a nonheme iron enzyme, (4-hydroxyphenyl)pyruvate dioxygenase from streptomyces avermitilis (SavHppD), can be repurposed to enable abiological radical-relay process to access C(sp

Indexed as

BiocatalysisProtein EngineeringStreptomyces4-Hydroxyphenylpyruvate DioxygenaseAzidesBacterial ProteinsNonheme Iron Proteins4-Hydroxyphenylpyruvate DioxygenaseAzidesBacterial ProteinsNonheme Iron Proteinsazidationbiocatalysisdirected evolutionNonhemeradical-relay

Identifiers

PMID39260996
PMCPMC12202082

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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.