Frontier Molecular Orbital Contributions to Chlorination versus Hydroxylation Selectivity in the Non-Heme Iron Halogenase SyrB2
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چکیده
منابع مشابه
Substrate positioning controls the partition between halogenation and hydroxylation in the aliphatic halogenase, SyrB2.
The alpha-ketoglutarate-dependent hydroxylases and halogenases employ similar reaction mechanisms involving hydrogen-abstracting Fe(IV)-oxo (ferryl) intermediates. In the halogenases, the carboxylate residue from the His(2)(Asp/Glu)(1) "facial triad" of iron ligands found in the hydroxylases is replaced by alanine, and a halide ion (X(-)) coordinates at the vacated site. Halogenation is thought...
متن کاملFirst-principles study of non-heme Fe(II) halogenase SyrB2 reactivity.
We present here a computational study of reactions at a model complex of the SyrB2 enzyme active site. SyrB2, which chlorinates L-threonine in the syringomycin biosynthetic pathway, belongs to a recently discovered class of alpha-ketoglutarate (alphaKG), non-heme Fe(II)-dependent halogenases that share many structural and chemical similarities with hydroxylases. Namely, halogenases and hydroxyl...
متن کاملWhy does the enzyme SyrB2 chlorinate, but does not hydroxylate, saturated hydrocarbons? A density functional theory (DFT) study.
Syringomycin halogenase (SyrB2) is a non-heme Fe(II)/alpha-ketoglutarate (alphaKG)-dependent enzyme which catalyses halogenation of saturated hydrocarbons, but unlike other closely related enzymes, does not catalyse the corresponding hydroxylation reaction. We have carried out density functional theory (DFT) calculations to try to understand this specificity. Calculations which include only the...
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This work presents the first detailed study on mechanistic aspects of halide oxidation by non-heme iron complexes. We show that while iron(III)-hydroperoxo complexes oxidise halides via oxygen atom transfer, the corresponding iron(IV)-oxo complex reacts via electron transfer.
متن کاملDichlorination and bromination of a threonyl-S-carrier protein by the non-heme Fe(II) halogenase SyrB2.
Biosynthetic tailoring of nonribosomal peptide and polyketide natural products can enhance their biological activities. Tailoring enzymes can introduce alkyl, acyl, or glycosyl groups onto natural product scaffolds and can oxidize or halogenate biosynthetic intermediates. Chlorinated and brominated molecules make up more than 95% of the more than 4500 known halogenated metabolites. Chloro and b...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2017
ISSN: 0002-7863,1520-5126
DOI: 10.1021/jacs.6b11995