Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 392, Issue 2, Pages 498-510Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2009.07.021
Keywords
X-ray crystallography; protein structure; Rieske protein; nonheme oxygenase; xenobiotic degradation
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Funding
- U.S. Department of Energy [DE-AC02-06CH11357]
- National Institutes of Health
- National Center for Research Resources [RR007707]
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Dicamba (3,6-dichloro-2-methoxybenzoic acid) is a widely used herbicide that is efficiently degraded by soil microbes. These microbes use a novel Rieske nonheme oxygenase, dicamba monooxygenase (DMO), to catalyze the oxidative demethylation of dicamba to 3,6-dichlorosalicylic acid (DCSA) and formaldehyde. We have determined the crystal structures of DMO in the free state, bound to its substrate dicamba, and bound to the product DCSA at 2 10-1.75 angstrom resolution. The structures show that the DMO active site uses a combination of extensive hydrogen bonding and steric interactions to correctly orient chlorinated, ortho-substituted benzoic-acid-like substrates for catalysis. Unlike other Rieske aromatic oxygenases, DMO oxygenates the exocyclic methyl group, rather than the aromatic ring, of its substrate. This first crystal structure of a Rieske demethylase shows that the Rieske oxygenase structural scaffold can be co-opted to perform varied types of reactions on xenobiotic substrates. (C) 2009 Elsevier Ltd. All rights reserved.
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