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.