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research-article

Confirmation of oxidative dehalogenation of pentachlorophenol by a Flavobacterium pentachlorophenol hydroxylase.

Department of Bacteriology and Biochemistry, University of Idaho, Moscow 83843.

ABSTRACT

Pentachlorophenol (PCP) hydroxylase purified from Flavobacterium sp. strain ATCC 39723 converted PCP or 2,3,5,6-tetrachlorophenol to tetrachloro-p-hydroquinone (TeCH) with the co-consumption of O2 and NADPH. The purified enzyme incorporated 18O from 18O2 but not from H218O into the reaction end product TeCH. The results clearly demonstrate that PCP is oxidatively converted to TeCH by a monooxygenase-type enzyme from Flavobacterium sp. strain ATCC 39723.

This article has been cited by other articles:

• Dai, M., Rogers, J. B., Warner, J. R., Copley, S. D. (2003). A Previously Unrecognized Step in Pentachlorophenol Degradation in Sphingobium chlorophenolicum Is Catalyzed by Tetrachlorobenzoquinone Reductase (PcpD). J. Bacteriol. 185: 302-310 [Abstract] [Full Text]  
• Cai, M., Xun, L. (2002). Organization and Regulation of Pentachlorophenol-Degrading Genes in Sphingobium chlorophenolicum ATCC 39723. J. Bacteriol. 184: 4672-4680 [Abstract] [Full Text]