Glieder, Anton and Farinas, Edgardo T. and Arnold, Frances H. (2002) Laboratory evolution of a soluble, self-sufficient, highly active alkane hydroxylase. Nature Biotechnology, 20 (11). pp. 1135-1139. ISSN 1087-0156. https://resolver.caltech.edu/CaltechAUTHORS:20150513-102744634
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Abstract
We have converted cytochrome P450 BM-3 from Bacillus megaterium (P450 BM-3), a medium-chain (C12–C18) fatty acid monooxygenase, into a highly efficient catalyst for the conversion of alkanes to alcohols. The evolved P450 BM-3 exhibits higher turnover rates than any reported biocatalyst for the selective oxidation of hydrocarbons of small to medium chain length (C3–C8). Unlike naturally occurring alkane hydroxylases, the best known of which are the large complexes of methane monooxygenase (MMO) and membrane-associated non-heme iron alkane monooxygenase (AlkB), the evolved enzyme is monomeric, soluble, and requires no additional proteins for catalysis. The evolved alkane hydroxylase was found to be even more active on fatty acids than wild-type BM-3, which was already one of the most efficient fatty acid monooxgenases known. A broad range of substrates including the gaseous alkane propane induces the low to high spin shift that activates the enzyme. This catalyst for alkane hydroxylation at room temperature opens new opportunities for clean, selective hydrocarbon activation for chemical synthesis and bioremediation.
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| Additional Information: | © 2002 Nature Publishing Group. Received 20 March 2002; Accepted 29 August 2002. This work was supported by the National Science Foundation, the Max Kade Foundation (fellowship to A.G.), and by Maxygen. The authors also thank Nathan Dalleska for his assistance with GC/MS, and Ulrich Schwaneberg (International University, Bremen, Germany), Tom Poulos (University of California, Irvine, USA), and Andrew Munro (University of Leicester, UK) for helpful discussions. Correspondence and requests for material should be addressed to F.H.A. The authors declare that they have no competing financial interests. | |||||||||
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| Issue or Number: | 11 | |||||||||
| Record Number: | CaltechAUTHORS:20150513-102744634 | |||||||||
| Persistent URL: | https://resolver.caltech.edu/CaltechAUTHORS:20150513-102744634 | |||||||||
| Official Citation: | Glieder, A., Farinas, E. T., & Arnold, F. H. (2002). Laboratory evolution of a soluble, self-sufficient, highly active alkane hydroxylase. [10.1038/nbt744]. Nat Biotech, 20(11), 1135-1139. | |||||||||
| Usage Policy: | No commercial reproduction, distribution, display or performance rights in this work are provided. | |||||||||
| ID Code: | 57490 | |||||||||
| Collection: | CaltechAUTHORS | |||||||||
| Deposited By: | Joanne McCole | |||||||||
| Deposited On: | 13 May 2015 18:12 | |||||||||
| Last Modified: | 03 Oct 2019 08:25 |
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