期刊
TETRAHEDRON
卷 68, 期 37, 页码 7651-7654出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.tet.2012.06.036
关键词
Chloramphenicol biosynthesis; Arylamine oxygenation; N-Oxygenation; Di-iron oxygenase
资金
- Office of Naval Research [N00014-02-1-0725]
- Department of Chemical Engineering and Biomolecular Engineering at the University of Illinois at Urbana-Champaign
- National Institutes of Health Molecular Biophysics Training Grant Program
The N-oxygenation of an amine group is one of the steps in the biosynthesis of the antibiotic chloramphenicol. The non-heme di-iron enzyme CmlI was identified as the enzyme catalyzing this reaction through bioinformatics studies and reconstitution of enzymatic activity. In vitro reconstitution was achieved using phenazine methosulfate and NADH as electron mediators, while in vivo activity was demonstrated in Escherichia coli using two substrates. Kinetic analysis showed a biphasic behavior of the enzyme. Oxidized hydroxylamine and nitroso compounds in the reaction were detected both in vitro and in vivo based on LC-MS. The active site metal was confirmed to be iron based on a ferrozine assay. These findings provide new insights into the biosynthesis of chloramphenicol and could lead to further development of CmlI as a useful biocatalyst. (C) 2012 Elsevier Ltd. All rights reserved.
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