Open AccessConfirmation of oxidative dehalogenation of pentachlorophenol by a Flavobacterium pentachlorophenol hydroxylase
Author(s) -
Luying Xun,
Edward Topp,
Cindy S. Orser
Publication year - 1992
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.174.17.5745-5747.1992
Subject(s) - pentachlorophenol , flavobacterium , biology , hydroquinone , enzyme , monooxygenase , biochemistry , oxidative phosphorylation , microbiology and biotechnology , bacteria , pseudomonas , cytochrome p450 , ecology , genetics
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.