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)
The University of North Carolina at Greensboro (UNCG )
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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.

Additional Information

Language: English
Date: 2012
aldehydes, cytochrome p450, defluorination, fluorophenol, biotechnology

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