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Novel evidence of cytochrome P450-catalyzed oxidation of phenanthrene in Phanerochaete chrysosporium under ligninolytic conditions

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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−1 in the microsomal fraction) by phenanthrene. The microsomal P450 degraded phenanthrene with a NADPH-dependent activity of 0.44 ± 0.02 min−1. 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.

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Abbreviations

ABTS:

2,2′-azinobis-(3-ethylbenzthiazoline-6-sulfonate)

HPLC:

High performance liquid chromatography

LiP:

Lignin peroxidase

LN:

Low nitrogen

MnP:

Manganese-dependent peroxidase

P420:

Cytochrome P420

P450:

Cytochrome P450

PAHs:

Polycyclic aromatic hydrocarbons

PB:

Piperonyl butoxide

PDA:

Potato dextrose agar

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Acknowledgement

This work was supported by National Nature Science Foundation of China (Admission No. 30400012 and 20737001) and Special Fund of State Key Joint Laboratory of Environment Simulation and Pollution Control (Nos. 08Z02ESPCT and 09Y03ESPCT).

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Ning, D., Wang, H., Ding, C. et al. Novel evidence of cytochrome P450-catalyzed oxidation of phenanthrene in Phanerochaete chrysosporium under ligninolytic conditions. Biodegradation 21, 889–901 (2010). https://doi.org/10.1007/s10532-010-9349-9

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