A two-component tetrachlorohydroquinone reductive dehalogenase system from the lignin-degrading basidiomycete Phanerochaete chrysosporium.

Tetrachloro-1,4-hydroquinone (TClHQ) is an intermediate in the degradation of pentachlorophenol by the lignin-degrading basidiomycete Phanerochaete chrysosporium. Two enzymes required for the reductive dehalogenation of TClHQ to trichlorohydroquinone (TrClHQ) were identified in cell-free extracts of P. chrysosporium. In the presence of GSH, a membrane-bound enzyme converted TClHQ to the glutathionyl conjugate of TrClHQ (GS-TrClHQ). This membrane-bound glutathione transferase was specific for GSH as a cosubstrate. In the second step of the reductive dehalogenation reaction, a soluble enzyme fraction converted GS-TrClHQ to TrClHQ in the presence of GSH, cysteine, or dithiothreitol. Thus, this second enzyme appears to be a GS-conjugate reductase. These two enzyme fractions, working in tandem, also reductively dehalogenated TrClHQ and 2,6-dichlorohydroquinone, which are intermediates in the degradation of chlorophenols by this organism. Copyright 1999 Academic Press.