Journal article
Characterization of 2,6-Dichloro-p-hydroquinone 1,2-Dioxygenase (PcpA) of Sphingomonas chlorophenolica ATCC 39723
Biochemical and biophysical research communications, Vol.266(2), pp.322-325
12/20/1999
Handle:
https://hdl.handle.net/2376/106203
PMID: 10600501
Abstract
Pentachlorophenol (PCP) is a general biocide and a major environmental pollutant. The initial steps of PCP degradation by Sphingomonas chlorophenolica ATCC 39723 have been studied and characterized. Two enzymes are responsible for converting PCP to 2,6-dichloro-p-hydroquinone (2,6-DiCH) which is a common metabolic intermediate of the biodegradation of polychlorinated phenols. 2,6-DiCH is degraded by PcpA from strain ATCC 39723, but the reaction end product has been misidentified as 6-chlorohydroxyquinol and has been elusive to detection. We report here the overproduction of PcpA in Escherichia coli and the demonstration of quantitative conversion of 2,6-DiCH to 2-chloromaleylacetate with the coconsumption of one equivalent O2 and release of one equivalent Cl− by purified PcpA. On the basis of the reaction stoichiometry, the enzyme is proposed to be 2,6-DiCH 1,2-dioxygenase.
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Details
- Title
- Characterization of 2,6-Dichloro-p-hydroquinone 1,2-Dioxygenase (PcpA) of Sphingomonas chlorophenolica ATCC 39723
- Creators
- Luying XunJan BohuslavekMian Cai
- Publication Details
- Biochemical and biophysical research communications, Vol.266(2), pp.322-325
- Academic Unit
- Molecular Biosciences, School of
- Publisher
- Elsevier Inc
- Identifiers
- 99900546995301842
- Language
- English
- Resource Type
- Journal article