The Catalytic Product of Pentachlorophenol 4-Monooxygenase is Tetra-chlorohydroquinone rather than Tetrachlorobenzoquinone
نویسندگان
چکیده
Pentachlorophenol 4-monooxygenase (PcpB) catalyzes the hydroxylation of pentachlorophenol in the pentachlorophenol biodegradation pathway in Sphingobium chlorophenolicum. Previous studies from two different research groups proposed oppositely that the catalytic product of PcpB was tetrachlorohydroquinone (TCHQ) and tetrachlorobenzoquinone (TCBQ). We re-examined the identity of the catalytic product of PcpB, because TCHQ and TCBQ are present in a redox-equilibrium in aqueous solutions and the chemical reagents NADPH, ethyl acetate and glutathione used for the product detection in the previous studies may shift the redox-equilibrium. In this study, we investigated the effects of NADPH, ethyl acetate and glutathione on the redox-equilibrium and product distribution. Under newly designed experimental conditions, we confirmed unambiguously that the catalytic product of PcpB is TCHQ instead of TCBQ. We also propose that TCBQ may be produced non-specifically by peroxidases within the bacterial cells and that TCBQ reductase (PcpD) might act as a self-protective rather than a PCP-degradation enzyme.
منابع مشابه
Biochemical Characterization of the Tetrachlorobenzoquinone Reductase Involved in the Biodegradation of Pentachlorophenol
Pentachlorophenol (PCP), a xenobiocide used to preserve lumbers, is a major environmental pollutant in North America. In spite of an expected high resistance to biodegradation, a number of aquatic and soil bacteria can degrade PCP. In this study, we cloned, expressed and purified tetrachlorobenzoquinone reductase (PcpD), the second enzyme in the PCP biodegradation pathway in Sphingobium chlorop...
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ورودعنوان ژورنال:
- The Open Microbiology Journal
دوره 2 شماره
صفحات -
تاریخ انتشار 2008