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- Title
Novel evidence of cytochrome P450-catalyzed oxidation of phenanthrene in Phanerochaete chrysosporium under ligninolytic conditions.
- Authors
Ning, Daliang; Wang, Hui; Ding, Chang; Lu, Huijie
- Abstract
The presence of cytochrome P450 and P450-mediated phenanthrene oxidation in the white rot fungus Phanerochaete chrysosporium under ligninolytic condition was first demonstrated in this study. The carbon monoxide difference spectra indicated induction of P450 (130 pmol mg in the microsomal fraction) by phenanthrene. The microsomal P450 degraded phenanthrene with a NADPH-dependent activity of 0.44 ± 0.02 min. One of major detectable metabolites of phenanthrene in the ligninolytic cultures and microsomal fractions was identified as phenanthrene trans-9,10-dihydrodiol. Piperonyl butoxide, a P450 inhibitor which had no effect on manganese peroxidase activity, significantly inhibited phenanthrene degradation and the trans-9,10-dihydrodiol formation in both intact cultures and microsomal fractions. Furthermore, phenanthrene was also efficiently degraded by the extracellular fraction with high manganese peroxidase activity. These results indicate important roles of both manganese peroxidase and cytochrome P450 in phenanthrene metabolism by ligninolytic P. chrysosporium.
- Subjects
CYTOCHROME P-450; PHANEROCHAETE; POLYCYCLIC aromatic hydrocarbons; PHENANTHRENE; CARBON monoxide spectra; ENZYME kinetics
- Publication
Biodegradation, 2010, Vol 21, Issue 6, p889
- ISSN
0923-9820
- Publication type
Article
- DOI
10.1007/s10532-010-9349-9