Work

Active-Site Structure of a β-Hydroxylase in Antibiotic Biosynthesis

Year: 2011

Type: article

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.

Source: Journal of the American Chemical Society

DOI: 10.1021/ja201822v

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

Institutions: University of Minnesota, University of Minnesota System

Language: English

Topic: Metal-Catalyzed Oxygenation Mechanisms

Subfield: Inorganic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of General Medical Sciences

Awards: G321655610, G4321279440, Synthetic Models and Spectroscopy of Metal-Oxo Proteins, Methane Monoxygenase Structure and Function, G8723391352