ArticleBiochemistry2018
α-Amine Desaturation of d-Arginine by the Iron(II)- and 2-(Oxo)glutarate-Dependent l-Arginine 3-Hydroxylase, VioC.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 39 citations in OpenAlex.
- Review
- Mechanistic insights into the selective oxidation of D-arginine by the nonheme iron-dependent viomycin biosynthesis enzyme VioC.iScience · 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
- Uncovering the Origins of Selectivity in Non-Heme Iron Dioxygenase-Catalyzed Tropolone Biosynthesis.The journal of physical chemistry. B · 2025Article
- Machine Learning Guided Rational Design of a Non-Heme Iron-Based Lysine Dioxygenase Improves its Total Turnover Number.Chembiochem : a European journal of chemical biology · 2024Article
- Controllable Multihalogenation of a Non-native Substrate by the SyrB2 Iron Halogenase.ACS catalysis · 2024Article
- Optimized Substrate Positioning Enables Switches in the C-H Cleavage Site and Reaction Outcome in the Hydroxylation-Epoxidation Sequence Catalyzed by Hyoscyamine 6β-Hydroxylase.Journal of the American Chemical Society · 2024Article
- Probing Ferryl Reactivity in a Nonheme Iron Oxygenase Using an Expanded Genetic Code.ACS catalysis · 2024Article
- Machine learning guided rational design of a non-heme iron-based lysine dioxygenase improves its total turnover number.bioRxiv : the preprint server for biology · 2024Article
- Catalytic divergencies in the mechanism of L-arginine hydroxylating nonheme iron enzymes.Frontiers in chemistry · 2024Review
- Synergistic Binding of the Halide and Cationic Prime Substrate of l-Lysine 4-Chlorinase, BesD, in Both Ferrous and Ferryl States.Biochemistry · 2023Article
- Synergistic Binding of the Halide and Cationic Prime Substrate of the l-Lysine 4-Chlorinase, BesD, in Both Ferrous and Ferryl States.bioRxiv : the preprint server for biology · 2023Article
- Oxidative modification of free-standing amino acids by Fe(II)/αKG-dependent oxygenases.Engineering microbiology · 2023Review
- Article
- Crystal structure of the α-ketoglutarate-dependent non-heme iron oxygenase CmnC in capreomycin biosynthesis and its engineering to catalyze hydroxylation of the substrate enantiomer.Frontiers in chemistry · 2022Article
- A human protein hydroxylase that accepts D-residues.Communications chemistry · 2020Article
- Evaluation of a concerted vs. sequential oxygen activation mechanism in α-ketoglutarate-dependent nonheme ferrous enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Evidence for Modulation of Oxygen Rebound Rate in Control of Outcome by Iron(II)- and 2-Oxoglutarate-Dependent Oxygenases.Journal of the American Chemical Society · 2019Article
- Hydrogen Donation but not Abstraction by a Tyrosine (Y68) during Endoperoxide Installation by Verruculogen Synthase (FtmOx1).Journal of the American Chemical Society · 2019Article
- A New Microbial Pathway for Organophosphonate Degradation Catalyzed by Two Previously Misannotated Non-Heme-Iron Oxygenases.Biochemistry · 2019Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
When challenged with substrate analogues, iron(II)- and 2-(oxo)glutarate-dependent (Fe/2OG) oxygenases can promote transformations different from those they enact upon their native substrates. We show here that the Fe/2OG enzyme, VioC, which is natively an l-arginine 3-hydroxylase, catalyzes an efficient oxidative deamination of its substrate enantiomer, d-Arg. The reactant complex with d-Arg retains all interactions between enzyme and substrate functional groups, but the required structural adjustments and opposite configuration of C2 position this carbon more optimally than C3 to donate hydrogen (H
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