Reprogramming nonheme iron enzymes for abiotic alkene trifluoromethylazidation.

James G Zhang, Xiongyi Huang

Abstract read

In one paragraph

Article in Methods in enzymology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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4 · The record

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5 · Who and what money

Authors and funding

2 authors.

James G ZhangDepartment 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

NIGMS NIH HHS R35 GM147639

6 · The paper itself

Abstract

In nature, nonheme iron enzymes catalyze a variety of chemical transformations, such as hydroxylation, halogenation, desaturation, and oxidative cyclizations, through the activation of dioxygen. Beyond their native functions, these enzymes can also serve as versatile biocatalysts for new-to-nature metal-catalyzed reactions. In particular, we evolved the nonheme iron oxygenase, hydroxymandelate synthase from Amycolatopsis orientalis (AoHMS), to catalyze an enantioselective alkene trifluoromethylazidation reaction using hypervalent iodine(III) reagents as a source of trifluoromethyl (-CF

Indexed as

AlkenesBacterial ProteinsNonheme Iron ProteinsOxygenasesProtein EngineeringActinobacteriaBiocatalysisGas Chromatography-Mass SpectrometryHalogenationHigh-Throughput Screening AssaysIronAlkenesBacterial ProteinsIronNonheme Iron ProteinsOxygenasesHigh-throughput screeningNonheme iron enzymeTrifluoromethylation

Identifiers

PMID41047206

DOI10.1016/bs.mie.2025.06.041

PMCPMC13186632

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