Diverse substrate range of a Flavobacterium pentachlorophenol hydroxylase and reaction stoichiometries.

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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Xun L,Topp E,Orser CS

doi

10.1128/jb.174.9.2898-2902.1992

keywords:

subject

Has Abstract

pub_date

1992-05-01 00:00:00

pages

2898-902

issue

9

eissn

0021-9193

issn

1098-5530

journal_volume

174

pub_type

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