Dechlorination of pentachlorophenol by membrane bound enzymes of Rhodococcus chlorophenolicus PCP-I View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1991-03

AUTHORS

J. S. Uotila, M. S. Salkinoja-Salonen, J. H. A. Apajalahti

ABSTRACT

Dechlorination (para-hydroxylation) of pentachlorophenol (PCP) and tetrachloro-para-hydroquinone (TeCH) and O-methylation of TeCH were demonstrated in cell extracts of Rhodococcus chlorophenolicus PCP-I. PCP para-hydroxylating activity was membrane bound, whereas TeCH dechlorinating enzyme was soluble. The PCP para-hydroxylating enzyme was solubilized by Triton X-100 and the requirement for both FAD and NADPH was shown. The dechlorinating activities were inducible in contrast to the constitutive TeCH O-methylating activity. The PCP para-hydroxylation was inhibited by its product TeCH, by anoxic conditions, and by different inhibitors of P450. Participation of this cytochrome in the PCP hydroxylation was confirmed by the appearance of a carbon monoxide dependent peak of absorbance at 457 nm in the membrane fraction prepared from PCP degrading cells. More... »

PAGES

25-31

References to SciGraph publications

  • 1986-10. Degradation of polychlorinated phenols by Rhodococcus chlorophenolicus in APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/bf00122422

    DOI

    http://dx.doi.org/10.1007/bf00122422

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1026822127

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/1368474


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