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Structural Basis for Halogenation by Iron- And 2-oxo-glutarate-dependent Enzyme WelO5

Structural Basis for Halogenation by Iron- And 2-oxo-glutarate-dependent Enzyme WelO5

Andrew J Mitchell, Qin Zhu, Ailiena O Maggiolo, Nikhil R Ananth, Matthew L Hillwig, Xinyu Liu, Amie K Boal

Nat Chem Biol. 2016 Aug;12(8):636-40.

PMID: 27348090

Abstract:

A 2.4-Å-resolution X-ray crystal structure of the carrier-protein-independent halogenase WelO5 in complex with its welwitindolinone precursor substrate, 12-epi-fischerindole U, reveals that the C13 chlorination target is proximal to the anticipated site of the oxo group in a presumptive cis-halo-oxo-iron(IV) (haloferryl) intermediate. Prior study of related halogenases forecasts substrate hydroxylation in this active-site configuration, but X-ray crystallographic verification of C13 halogenation in single crystals mandates that ligand dynamics must reposition the oxygen ligand to enable the observed outcome. S189A WelO5 produces a mixture of halogenation and hydroxylation products, showing that an outer-sphere hydrogen-bonding group orchestrates ligand movements to achieve a configuration that promotes halogen transfer.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
LS7411319	4arm-PEG40K-Succinimidyl Glutarate			Price
LS7411395	8arm-PEG40K-Succinimidyl Glutarate			Price

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