Active-site structure of a β-hydroxylase in antibiotic biosynthesis.

Abstract

X-ray absorption and resonance Raman spectroscopies show that CmlA, the β-hydroxylase of the chloramphenicol biosynthetic pathway, contains a (μ-oxo)-(μ-1,3-carboxylato)diiron(III) cluster with 6-coordinate iron centers and 3 - 4 His ligands. This active site is found within a unique β-lactamase fold and is distinct from those of soluble methane monooxygenase and related enzymes that utilize a highly conserved diiron cluster with a 2-His-4-carboxylate ligand set within a 4-helix bundle motif. These structural differences may have an impact on the nature of the activated oxygen species of the reaction cycle.

DOI: 10.1021/ja201822v

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Cite this paper

@article{Vu2011ActivesiteSO, title={Active-site structure of a β-hydroxylase in antibiotic biosynthesis.}, author={Van V Vu and Thomas M Makris and John D Lipscomb and Lawrence Que}, journal={Journal of the American Chemical Society}, year={2011}, volume={133 18}, pages={6938-41} }