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Crystal Structures of Cyclohexanone Monooxygenase Reveal Complex Domain Movements and a Sliding Cofactor

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Departments of Biochemistry and Microbiology & Immunology, McGill University, 3649 Prom Sir William Osler, Bellini Pavilion, Room 466, Montreal, QC, Canada H3G 0B1, Biotechnology Research Institute, National Research Council Canada, 6100 Royalmount Avenue, Montreal, QC, Canada H4P 2R2, Department of Life Science & Biotechnology and ORDIST, Kansai University, Suita, Osaka, 564-8680, Japan, and Process Technology Research Laboratories, Daiichi Sankyo Co. Ltd, Kasai R&D Center, 1-16-13, Kitakasai Edogawa-ku, Tokyo 134-8630, Japan
[email protected]; [email protected]
†McGill University.
‡National Research Council Canada.
§Kansai University.
∥Daiichi Sankyo Co. Ltd.
Cite this: J. Am. Chem. Soc. 2009, 131, 25, 8848–8854
Publication Date (Web):April 22, 2009
https://doi.org/10.1021/ja9010578
Copyright © 2009 American Chemical Society
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    Abstract

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    Cyclohexanone monooxygenase (CHMO) is a flavoprotein that carries out the archetypical Baeyer−Villiger oxidation of a variety of cyclic ketones into lactones. Using NADPH and O2 as cosubstrates, the enzyme inserts one atom of oxygen into the substrate in a complex catalytic mechanism that involves the formation of a flavin-peroxide and Criegee intermediate. We present here the atomic structures of CHMO from an environmental Rhodococcus strain bound with FAD and NADP+ in two distinct states, to resolutions of 2.3 and 2.2 Å. The two conformations reveal domain shifts around multiple linkers and loop movements, involving conserved arginine 329 and tryptophan 492, which effect a translation of the nicotinamide resulting in a sliding cofactor. Consequently, the cofactor is ideally situated and subsequently repositioned during the catalytic cycle to first reduce the flavin and later stabilize formation of the Criegee intermediate. Concurrent movements of a loop adjacent to the active site demonstrate how this protein can effect large changes in the size and shape of the substrate binding pocket to accommodate a diverse range of substrates. Finally, the previously identified BVMO signature sequence is highlighted for its role in coordinating domain movements. Taken together, these structures provide mechanistic insights into CHMO-catalyzed Baeyer−Villiger oxidation.

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    Cloning, overexpression, purification, mutagenesis, and substrate profiling of CHMO. This material is available free of charge via the Internet at http://pubs.acs.org.

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