ReviewFrontiers in chemistry2024
Catalytic divergencies in the mechanism of L-arginine hydroxylating nonheme iron enzymes.
Review in Frontiers in chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Mechanistic Elucidation of BBOX-Catalyzed Hydroxylation and THP-Induced Oxidative Rearrangement via QM/MM Calculations.Molecules (Basel, Switzerland) · 2026Article
- l-Arg@ZY-FeNanoscale advances · 2026Article
- Metabolic Origin, Role and Fate of the Denaturant Guanidine.Microbial biotechnology · 2025Article
- Promiscuity in Molecular Mimics of the Cysteine Dioxygenase: Effects of Selenium in the Substrate and Cobalt as the Central Metal Ion.Angewandte Chemie (International ed. in English) · 2025Article
- Substrate Epoxidation Catalyzed by the Nonheme Iron Dioxygenase Dapdiamide Biosynthesis Enzyme C. Why Is the Substrate Tethered?Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Article
- Three distinct strategies lead to programmable aliphatic C-H oxidation in bicyclomycin biosynthesis.Nature communications · 2025Article
- An Active Site Tyr Residue Guides the Regioselectivity of Lysine Hydroxylation by Nonheme Iron Lysine-4-hydroxylase Enzymes through Proton-Coupled Electron Transfer.Journal of the American Chemical Society · 2024Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many enzymes in nature utilize a free arginine (L-Arg) amino acid to initiate the biosynthesis of natural products. Examples include nitric oxide synthases, which generate NO from L-Arg for blood pressure control, and various arginine hydroxylases involved in antibiotic biosynthesis. Among the groups of arginine hydroxylases, several enzymes utilize a nonheme iron(II) active site and let L-Arg react with dioxygen and
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Registered trials
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