Peroxidase-catalyzed oxidation of chlorophenols to polychlorinated dibenzo-p-dioxins and dibenzofurans.
Chlorophenols are transformed in vitro to polychlorinated dibenzo-p-dioxins and dibenzofurans (PCDD/Fs) by peroxidase-catalyzed oxidations. This is demonstrated with bovine lactoperoxidase as well as horseradish peroxidase, and with 3,4,5- and 2,4,5-trichlorophenol (TrCP). The yield of total PCDD/Fs with lactoperoxidase was 11 micrograms per g 345-TrCP and 10 micrograms per g 245-TrCP, of which 2,3,7,8-substituted PCDD/Fs constituted 8.5 and 2.2 micrograms/g, respectively, corresponding to 0.85 and 1.2 micrograms/g of Nordic TCDD-equivalents.
Oberg
L G
LG
Department of Medical Biochemistry and Biophysics, University of Umeå, Sweden.
Glas
B
B
Swanson
S E
SE
Rappe
C
C
Paul
K G
KG
D000818:Animals; D002417:Cattle; D002733:Chlorophenols / Q000378:metabolism*; D006735:Horseradish Peroxidase / Q000494:pharmacology; D007784:Lactoperoxidase / Q000494:pharmacology; D010084:Oxidation-Reduction; D000072317:Polychlorinated Dibenzodioxins / Q000031:analogs & derivatives* / Q000378:metabolism
D002733:Chlorophenols; D000072317:Polychlorinated Dibenzodioxins; D006735:Horseradish Peroxidase; D007784:Lactoperoxidase