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PMID: 1512208 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Confirmation of oxidative dehalogenation of pentachlorophenol by a Flavobacterium pentachlorophenol hydroxylase.

Journal of bacteriology ·Vol. 174 ·No. 17 ·1992-09-00 ·Pages 5745-7

Xun L, Topp E, Orser CS

Abstract

Pentachlorophenol (PCP) hydroxylase purified from Flavobacterium sp. strain ATCC 39723 converted PCP or 2,3,5,6-tetrachlorophenol to tetrachloro-p-hydroquinone (TeCH) with the co-consumption of O2 and NADPH. The purified enzyme incorporated 18O from 18O2 but not from H218O into the reaction end product TeCH. The results clearly demonstrate that PCP is oxidatively converted to TeCH by a monooxygenase-type enzyme from Flavobacterium sp. strain ATCC 39723.

MeSH Terms
Flavobacterium/enzymology Gas Chromatography-Mass Spectrometry Mixed Function Oxygenases/metabolism Oxidation-Reduction Pentachlorophenol/metabolism
Chemicals
Pentachlorophenol Mixed Function Oxygenases pentachlorophenol monooxygenase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Xun L
Department of Bacteriology and Biochemistry, University of Idaho, Moscow 83843.
Topp E
Orser C S
References (10)
10 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.174.17.5745-5747.1992
Published
1992-09-00
Pages
5745-7
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC206524
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.174.17.5745-5747.1992 PMC Full Text View journal details
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