ArticleJournal of the American Chemical Society2017
Visualizing the Reaction Cycle in an Iron(II)- and 2-(Oxo)-glutarate-Dependent Hydroxylase.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 141 citations in OpenAlex.
- Experimental and Computational Elucidation of C(sp3)-H Fluorination Barriers in an Iron(II)- and 2-Oxoglutarate-Dependent Halogenase.Journal of the American Chemical Society · 2026Article
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- Mechanistic Elucidation of BBOX-Catalyzed Hydroxylation and THP-Induced Oxidative Rearrangement via QM/MM Calculations.Molecules (Basel, Switzerland) · 2026Article
- Total Synthesis of (+)-12-The Journal of organic chemistry · 2026Article
- tRNA-deacylase-directed discovery of biosynthetic pathways.Nature chemistry · 2026Article
- Dynamic metal coordination controls chemoselectivity in a radical halogenase.Nature chemical biology · 2026Article
- A highly dynamic mononuclear non-heme iron enzyme for the two-step isonitrile biosynthesis.Nature communications · 2026Article
- Mechanistic insights into the selective oxidation of D-arginine by the nonheme iron-dependent viomycin biosynthesis enzyme VioC.iScience · 2025Article
- Unusual O-H Activation-Initiated C-C Bond Cleavage Reaction by a Nonheme Fe Enzyme in Antifungal Nucleoside Biosynthesis.Journal of the American Chemical Society · 2025Article
- Tracing the stepwise Darwinian evolution of a plant halogenase.Science advances · 2025Article
- Three distinct strategies lead to programmable aliphatic C-H oxidation in bicyclomycin biosynthesis.Nature communications · 2025Article
- Discovery of Noncanonical Iron and 2-Oxoglutarate Dependent Enzymes Involved in C-C and C-N Bond Formation in Biosynthetic Pathways.ACS bio & med chem Au · 2025Review
- Influence of the second coordination sphere on OJournal of inorganic biochemistry · 2025Article
- Comparison of a Nonheme Iron Cyclopropanase with a Homologous Hydroxylase Reveals Mechanistic Features Associated with Distinct Reaction Outcomes.Journal of the American Chemical Society · 2025Article
- Human prolyl hydroxylase domain 2 reacts with OScientific reports · 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
- An Unusual Ferryl Intermediate and Its Implications for the Mechanism of Oxacyclization by the Loline-Producing Iron(II)- and 2-Oxoglutarate-Dependent Oxygenase, LolO.Biochemistry · 2024Article
- 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
- Electronic structure of metal oxide dications with ammonia ligands and their reactivity towards the selective conversion of methane to methanol.Frontiers in chemistry · 2024Article
3 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
Abstract
Iron(II)- and 2-(oxo)-glutarate-dependent oxygenases catalyze diverse oxidative transformations that are often initiated by abstraction of hydrogen from carbon by iron(IV)-oxo (ferryl) complexes. Control of the relative orientation of the substrate C-H and ferryl Fe-O bonds, primarily by direction of the oxo group into one of two cis-related coordination sites (termed inline and offline), may be generally important for control of the reaction outcome. Neither the ferryl complexes nor their fleeting precursors have been crystallographically characterized, hindering direct experimental validation of the offline hypothesis and elucidation of the means by which the protein might dictate an alternative oxo position. Comparison of high-resolution X-ray crystal structures of the substrate complex, an Fe(II)-peroxysuccinate ferryl precursor, and a vanadium(IV)-oxo mimic of the ferryl intermediate in the l-arginine 3-hydroxylase, VioC, reveals coordinated motions of active site residues that appear to control the intermediate geometries to determine reaction outcome.
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