Degradation of 2,4-dichlorophenol by the lignin-degrading fungus Phanerochaete chrysosporium

Abstract

Under secondary metabolic conditions the white rot basidiomycete Phanerochaete chrysosporium mineralizes 2,4-dichlorophenol (I). The pathway for the degradation of 2,4-dichlorophenol (I) was elucidated by the characterization of fungal metabolites and of oxidation products generated by purified lignin peroxidase and manganese peroxidase. The multistep pathway involves the oxidative dechlorination of 2,4-dichlorophenol (I) to yield 1,2,4,5-tetrahydroxybenzene (VIII). The intermediate 1,2,4,5-tetrahydroxybenzene (VIII) is ring cleaved to produce, after subsequent oxidation, malonic acid. In the first step of the pathway, 2,4-dichlorophenol (I) is oxidized to 2-chloro-1,4-benzoquinone (II) by either manganese peroxidase or lignin peroxidase. 2-Chloro-1,4-benzoquinone (II) is then reduced to 2-chloro-1,4-hydroquinone (III), and the latter is methylated to form the lignin peroxidase substrate 2-chloro-1,4-dimethoxybenzene (IV). 2-Chloro-1,4-dimethoxybenzene (IV) is oxidized by lignin peroxidase to generate 2,5-dimethoxy-1,4-benzoquinone (V), which is reduced to 2,5-dimethoxy-1,4-hydroquinone (VI). 2,5-Dimethoxy-1,4-hydroquinone (VI) is oxidized by either peroxidase to generate 2,5-dihydroxy-1,4-benzoquinone (VII) which is reduced to form the tetrahydroxy intermediate 1,2,4,5-tetrahydroxybenzene (VIII). In this pathway, the substrate is oxidatively dechlorinated by lignin peroxidase or manganese peroxidase in a reaction which produces a p-quinone. The p-quinone intermediate is then recycled by reduction and methylation reactions to regenerate an intermediate which is again a substrate for peroxidase-catalyzed oxidative dechlorination. This unique pathway apparently results in the removal of both chlorine atoms before ring cleavage occurs.