Defluorination of 4-fluorophenol by Cytochrome P450BM3-F87G: Activation by long Chain Fatty Aldehydes.
- UNCG Author/Contributor (non-UNCG co-authors, if there are any, appear on document)
- Gregory M. Raner, Associate Professor and Graduate Director (Creator)
- Institution
- The University of North Carolina at Greensboro (UNCG )
- Web Site: http://library.uncg.edu/
Abstract: Cytochrome P450BM3-F87G catalyzed the oxidative defluorination of 4-fluorophenol, followed by reduction of the resulting benzoquinone to hydroquinone via the NADPH P450-reductase activity of the enzyme. The k catand K m for this reaction were 71 ± 5 min-1 and 9.5 ± 1.3 mM, respectively. Co-incubation of the reaction mixture with long chain aldehydes stimulated the defluorination reaction, with the 2,3-unsaturated aldehyde, 2-decenal producing a 12-fold increase in catalytic efficiency. At 150 µM aldehyde, k cat increased to 158 ± 4, while K m decreased to 1.8 ± 0.2. The effects of catalase, glutathione and ascorbate on the reaction were all consistent with a direct oxygen insertion mechanism, as opposed to a radical mechanism. The study demonstrates the potential use of P450BM3 mutants in oxidative defluorination reactions, and characterizes the novel stimulatory action of straight chain aldehydes on this activity.
Defluorination of 4-fluorophenol by Cytochrome P450BM3-F87G: Activation by long Chain Fatty Aldehydes.
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Created on 6/17/2013
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Additional Information
- Publication
- Language: English
- Date: 2012
- Keywords
- aldehydes, cytochrome p450, defluorination, fluorophenol, biotechnology