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

Van V. Vu, Thomas M. Makris, John D. Lipscomb, Lawrence Que

Research output: Contribution to journalArticlepeer-review

17 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)6938-6941
Number of pages4
JournalJournal of the American Chemical Society
Issue number18
StatePublished - May 11 2011


Dive into the research topics of 'Active-site structure of a β-hydroxylase in antibiotic biosynthesis'. Together they form a unique fingerprint.

Cite this