Verification of the role of PCP 4-monooxygenase in chlorine elimination from pentachlorophenol by Flavobacterium sp. strain ATCC 39723
| Autor: | Cleston C. Lange, Schneider Bj, Orser Cs |
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| Rok vydání: | 1996 |
| Předmět: |
DNA
Bacterial Oxygenase Pentachlorophenol Restriction Mapping Biophysics Flavoprotein Biochemistry Flavobacterium Mixed Function Oxygenases chemistry.chemical_compound Escherichia coli Cloning Molecular Molecular Biology Gene chemistry.chemical_classification biology Chemistry Mutagenesis Cell Biology Monooxygenase Recombinant Proteins Blotting Southern Kinetics Enzyme FAD binding biology.protein Chlorine Plasmids |
| Zdroj: | Biochemical and biophysical research communications. 219(1) |
| ISSN: | 0006-291X |
| Popis: | The bacterial enzyme PCP 4-monooxygenase from Flavobacterium sp. strain ATCC 39723 catalyzes the oxygenolytic removal of the first chlorine from pentachlorophenol. PCP 4-monooxygenase is an FAD binding, NADPH requiring oxygenase, with similar functional domains as other bacterial flavoprotein monooxygenases specific for phenolic substrates. However, the definitive proof for the singular role of an oxygenolytic elimination of the primary chlorine from pentachlorophenol by Flavobacterium sp. has awaited the development of a genetic system whereby targeted mutagenesis via allelic exchange could be carried out with the corresponding gene from PCP 4-monoxygenase, pcpB. We report the development of a genetic system for Flavobacterium sp. strain ATCC 39723, and its application in targeted mutagenesis of the pcpB allele for elimination of PCP 4-monooxygenase activity. |
| Databáze: | OpenAIRE |
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