Metabolism of polychlorinated dibenzo-p-dioxins by cytochrome P450 BM-3 and its mutant

Woro Sulistyaningdyah; Jun Ogawa; Qing-Shan Li; Raku Shinkyo; Toshiyuki Sakaki; Inouye, Kuniyo; Schmid, Rolf; Sakayu Shimizu
December 2004
Biotechnology Letters;Dec2004, Vol. 26 Issue 24, p1857
Academic Journal
The metabolism of polychlorinated dibenzo-p-dioxins by cytochrome P450 BM-3 fromBacillus megateriumand a mutant enzyme of it (AL4V; Ala74Gly, Phe87Val, Leu188Gln triple mutant) was examined. Both purified enzymes metabolized 1-monochloro-, 2,3-dichloro-, and 2,3,7-trichloro-dibenzo-p-dioxin, but not 2,3,7,8-tetrachloro-dibenzo-p-dioxin. The mutant AL4V had 2-12 times higher activity than the wild-type P450 BM-3 towards polychlorinated dibenzo-p-dioxins. The products were hydroxylated at an unsubstituted position and/or showing migration of the chloride and were less toxic derivatives with lower than 10% toxicity of the original compounds.


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