Active-site structure of a β-hydroxylase in antibiotic biosynthesis
Van V Vu1, Thomas M Makris, John D Lipscomb
1Department of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455, USA.
Abstract:
X-ray absorption and resonance Raman spectroscopies show that CmlA, the β-hydroxylase of the chloramphenicol biosynthetic pathway, contains a (micro-oxo)-(micro-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.
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