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Literature summary for 1.14.20.15 extracted from

  • Srnec, M.; Solomon, E.I.
    Frontier molecular orbital contributions to Chlorination versus hydroxylation selectivity in the non-heme iron halogenase SyrB2 (2017), J. Am. Chem. Soc., 139, 2396-2407 .
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Pseudomonas syringae pv. syringae Q9RBY6
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Pseudomonas syringae pv. syringae B301D Q9RBY6
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the ability of an Fe(IV)-O intermediate in SyrB2 to perform chlorination vs. hydroxylation is computationally evaluated for different substrates. Differential contribution of the two frontier molecular orbitals to chlorination vs. hydroxylation selectivity in SyrB2 is related to a reaction mechanism that involves two asynchronous transfers: electron transfer from the substrate radical to the iron center followed by late ligand (Cl- or OH-) transfer to the substrate Pseudomonas syringae pv. syringae ?
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additional information the ability of an Fe(IV)-O intermediate in SyrB2 to perform chlorination vs. hydroxylation is computationally evaluated for different substrates. Differential contribution of the two frontier molecular orbitals to chlorination vs. hydroxylation selectivity in SyrB2 is related to a reaction mechanism that involves two asynchronous transfers: electron transfer from the substrate radical to the iron center followed by late ligand (Cl- or OH-) transfer to the substrate Pseudomonas syringae pv. syringae B301D ?
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 ?

Synonyms

Synonyms Comment Organism
SyrB2
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 Pseudomonas syringae pv. syringae