ArticleJournal of the American Chemical Society2016
Electronic Structure of the Ferryl Intermediate in the α-Ketoglutarate Dependent Non-Heme Iron Halogenase SyrB2: Contributions to H Atom Abstraction Reactivity.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 91 citations in OpenAlex.
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- High-Valent Late Transition Metal-Oxo Complexes: Breaking Boundaries at the Oxo Wall and Beyond.Chemical reviews · 2026Review
- Dynamic metal coordination controls chemoselectivity in a radical halogenase.Nature chemical biology · 2026Article
- Structural basis of the promiscuity of the unusual Fe(II) and 2-oxoglutarate dependent human aspartate/asparagine-β-hydroxylase.Nature communications · 2026Article
- Can ferric-oxyl excited states explain elongated iron-oxygen bonds in heme peroxidase catalytic intermediates?Nature communications · 2026Article
- Examining Pseudohalide (NJournal of inorganic biochemistry · 2026Article
- Electronic Structure Contributions to the Reactivity of Mononuclear FeAccounts of chemical research · 2026Article
- Regio- and Stereoselective Halogenation by an Iron(II)- and 2-Oxoglutarate-Dependent Halogenase in the Biosynthesis of Halogenated Nucleosides.Journal of the American Chemical Society · 2025Article
- Revealing the catalytic mechanism of the Fe(II)/2-oxoglutarate-dependent human epigenetic modifying enzyme ALKBH5.Cell reports. Physical science · 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
- 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
- New Frontiers in Nonheme Enzymatic Oxyferryl Species.Chembiochem : a European journal of chemical biology · 2024Review
- Effects of Clinical Mutations in the Second Coordination Sphere and Remote Regions on the Catalytic Mechanism of Non-Heme Fe(II)/2-Oxoglutarate-Dependent Aspartyl Hydroxylase AspH.Chemphyschem : a European journal of chemical physics and physical chemistry · 2024Article
- Ligand engineering of tetra N-heterocyclic carbenes for boosting catalytic aziridination.Dalton transactions (Cambridge, England : 2003) · 2024Article
- Controllable Multihalogenation of a Non-native Substrate by the SyrB2 Iron Halogenase.ACS catalysis · 2024Article
- Review
- Unusual catalytic strategy by non-heme Fe(ii)/2-oxoglutarate-dependent aspartyl hydroxylase AspH.Chemical science · 2024Article
- Spectroscopic definition of ferrous active sites in non-heme iron enzymes.Methods in enzymology · 2024Article
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6 authors at 3 institutions in 2 countries.
Funding
Abstract
Low temperature magnetic circular dichroism (LT MCD) spectroscopy in combination with quantum-chemical calculations are used to define the electronic structure associated with the geometric structure of the Fe(IV)═O intermediate in SyrB2 that was previously determined by nuclear resonance vibrational spectroscopy. These studies elucidate key frontier molecular orbitals (FMOs) and their contribution to H atom abstraction reactivity. The VT MCD spectra of the enzymatic S = 2 Fe(IV)═O intermediate with Br(-) ligation contain information-rich features that largely parallel the corresponding spectra of the S = 2 model complex (TMG3tren)Fe(IV)═O (Srnec, M.; Wong, S. D.; England, J; Que, L; Solomon, E. I. Proc. Natl. Acad. Sci. USA 2012, 109, 14326-14331). However, quantitative differences are observed that correlate with π-anisotropy and oxo donor strength that perturb FMOs and affect reactivity. Due to π-anisotropy, the Fe(IV)═O active site exhibits enhanced reactivity in the direction of the substrate cavity that proceeds through a π-channel that is controlled by perpendicular orientation of the substrate C-H bond relative to the halide-Fe(IV)═O plane. Also, the increased intrinsic reactivity of the SyrB2 intermediate relative to the ferryl model complex is correlated to a higher oxyl character of the Fe(IV)═O at the transition states resulting from the weaker ligand field of the halogenase.
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