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 journalArticle

13 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)6938-6941
Number of pages4
JournalJournal of the American Chemical Society
Volume133
Issue number18
DOIs
StatePublished - May 11 2011

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Biosynthesis
methane monooxygenase
Antibiotics
Mixed Function Oxygenases
Catalytic Domain
Ligands
Anti-Bacterial Agents
Raman Spectrum Analysis
Biosynthetic Pathways
X ray absorption
Chloramphenicol
Raman spectroscopy
Methane
Iron
Enzymes
X-Rays
Oxygen

Cite this

Active-site structure of a β-hydroxylase in antibiotic biosynthesis. / Vu, Van V.; Makris, Thomas M.; Lipscomb, John D.; Que, Lawrence.

In: Journal of the American Chemical Society, Vol. 133, No. 18, 11.05.2011, p. 6938-6941.

Research output: Contribution to journalArticle

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