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  4. Fontimonas thermophila Alkane Monooxygenase (FtAlkB) Is an Alkyl Fluoride Dehalogenase

Fontimonas thermophila Alkane Monooxygenase (FtAlkB) Is an Alkyl Fluoride Dehalogenase

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sword-2026-04-23T19:39:39.original.xml (130 B)
Original SWORD entry document
Author(s)
Hendricks, Lauren
•
Reinhardt, Clorice R
•
Green, Tierani
•
Kunczynski, Lily
•
Roberts, August Jaunzarins
•
Miller, Naomi
•
Rafalin, Noga
•
Kulik, Heather J
•
Groves, John T
•
Austin, Rachel N
Date Issued
March 7, 2025
Journal
Journal of the American Chemical Society
Publisher
American Chemical Society
Citation
Hendricks, Lauren, Reinhardt, Clorice R, Green, Tierani, Kunczynski, Lily, Roberts, August Jaunzarins et al. 2025. "Fontimonas thermophila Alkane Monooxygenase (FtAlkB) Is an Alkyl Fluoride Dehalogenase." Journal of the American Chemical Society, 147 (11).
Version
Author's final manuscript
Abstract
Purified alkane monooxygenase (AlkB) from Fontimonas thermophila (FtAlkB) catalyzes the defluorination of 1- fluorooctane, producing octanal, which is partially reduced under the reaction conditions to generate 1-octanol. This reaction occurs preferentially at the monofluorinated methyl group, with only a minor amount of oxidation at the nonfluorinated end of the molecule. The dehalogenation chemistry is specific to 1-fluorooctane, as neither 1-chlorooctane or 1-bromooctane are dehalogenated to an appreciable extent. Furthermore, P. putida cells containing the structurally related AlkB (PpAlkB) along with the full set of genes required for alkane metabolism, utilize 1-fluorooctane as their sole source of carbon with growth rates comparable to those for cells grown with octane.
MIT Department
Massachusetts Institute of Technology. Department of Chemical Engineering
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
Persistent DSpace Link
https://hdl.handle.net/1721.1/165665
DOI of Published Version
10.1021/jacs.5c00386
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