Diverse substrate range of a Flavobacterium pentachlorophenol hydroxylase and reaction stoichiometries.
An understanding of the enzymatic reactions catalyzing the degradation of substituted phenols, a major group of environmental pollutants, is required for the development of biological methods for the decontamination of halophenol-polluted sites. We found that a flavomonooxygenase, pentachlorophenol hydroxylase, isolated from a Flavobacterium sp., catalyzed a primary attack on a broad range of substituted phenols, hydroxylating the para position and removing halogen, nitro, amino, and cyano groups to produce halide, nitrite, hydroxylamine, and cyanide, respectively. Elimination of 1 mol of a halogen, nitro, or cyano group required 2 mol of NADPH, while only 1 mol of NADPH was required to remove 1 mol of an amino group or hydrogen.
Xun
L
L
Department of Bacteriology and Biochemistry, University of Idaho, Moscow 83843.
Topp
E
E
Orser
C S
CS
D000627:Aminophenols / Q000378:metabolism; D001966:Bromine / Q000378:metabolism; D002733:Chlorophenols / Q000378:metabolism; D005417:Flavobacterium / Q000201:enzymology*; D007455:Iodine / Q000378:metabolism; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D008956:Models, Chemical; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction; D010636:Phenols / Q000378:metabolism*; D013379:Substrate Specificity
D000627:Aminophenols; D002733:Chlorophenols; D010636:Phenols; D009249:NADP; D007455:Iodine; D006899:Mixed Function Oxygenases; C069781:pentachlorophenol monooxygenase; D001966:Bromine