Diverse substrate range of a Flavobacterium pentachlorophenol hydroxylase and reaction stoichiometries. |
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| Authors: | L Xun E Topp C S Orser |
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| Affiliation: | Department of Bacteriology and Biochemistry, University of Idaho, Moscow 83843. |
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| Abstract: | 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. |
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