Involvement of cytochrome P450 in pentachlorophenol transformation in a white rot fungus Phanerochaete chrysosporium.
Identifieur interne : 000401 ( Main/Curation ); précédent : 000400; suivant : 000402Involvement of cytochrome P450 in pentachlorophenol transformation in a white rot fungus Phanerochaete chrysosporium.
Auteurs : Daliang Ning [République populaire de Chine] ; Hui WangSource :
- PloS one [ 1932-6203 ] ; 2012.
Descripteurs français
- KwdFr :
- Anisoles (métabolisme), Biotransformation (MeSH), Butoxyde de pipéronyle (pharmacologie), Cytochrome P-450 enzyme system (composition chimique), Cytochrome P-450 enzyme system (métabolisme), Hydroquinones (métabolisme), Inhibiteurs des enzymes du cytochrome P-450 (MeSH), Microsomes (effets des médicaments et des substances chimiques), Microsomes (enzymologie), Méthylation (MeSH), Oxydoréduction (MeSH), Pentachlorophénol (métabolisme), Phanerochaete (effets des médicaments et des substances chimiques), Phanerochaete (enzymologie), Polluants environnementaux (métabolisme), Protéines fongiques (antagonistes et inhibiteurs), Protéines fongiques (composition chimique), Protéines fongiques (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Protéines fongiques.
- composition chimique : Cytochrome P-450 enzyme system, Protéines fongiques.
- effets des médicaments et des substances chimiques : Microsomes, Phanerochaete.
- enzymologie : Microsomes, Phanerochaete.
- métabolisme : Anisoles, Cytochrome P-450 enzyme system, Hydroquinones, Pentachlorophénol, Polluants environnementaux, Protéines fongiques.
- pharmacologie : Butoxyde de pipéronyle.
- Biotransformation, Inhibiteurs des enzymes du cytochrome P-450, Méthylation, Oxydoréduction.
English descriptors
- KwdEn :
- Anisoles (metabolism), Biotransformation (MeSH), Cytochrome P-450 Enzyme Inhibitors (MeSH), Cytochrome P-450 Enzyme System (chemistry), Cytochrome P-450 Enzyme System (metabolism), Environmental Pollutants (metabolism), Fungal Proteins (antagonists & inhibitors), Fungal Proteins (chemistry), Fungal Proteins (metabolism), Hydroquinones (metabolism), Methylation (MeSH), Microsomes (drug effects), Microsomes (enzymology), Oxidation-Reduction (MeSH), Pentachlorophenol (metabolism), Phanerochaete (drug effects), Phanerochaete (enzymology), Piperonyl Butoxide (pharmacology).
- MESH :
- chemical , antagonists & inhibitors : Fungal Proteins.
- chemical , chemistry : Cytochrome P-450 Enzyme System, Fungal Proteins.
- chemical , metabolism : Anisoles, Cytochrome P-450 Enzyme System, Environmental Pollutants, Fungal Proteins, Hydroquinones, Pentachlorophenol.
- drug effects : Microsomes, Phanerochaete.
- enzymology : Microsomes, Phanerochaete.
- chemical , pharmacology : Piperonyl Butoxide.
- Biotransformation, Cytochrome P-450 Enzyme Inhibitors, Methylation, Oxidation-Reduction.
Abstract
The occurrence of cytochrome P450 and P450-mediated pentachlorophenol oxidation in a white rot fungus Phanerochaete chrysosporium was demonstrated in this study. The carbon monoxide difference spectra indicated induction of P450 (103±13 pmol P450 per mg protein in the microsomal fraction) by pentachlorophenol. The pentachlorophenol oxidation by the microsomal P450 was NADPH-dependent at a rate of 19.0±1.2 pmol min(-1) (mg protein)(-1), which led to formation of tetrachlorohydroquinone and was significantly inhibited by piperonyl butoxide (a P450 inhibitor). Tetrachlorohydroquinone was also found in the cultures, while the extracellular ligninases which were reported to be involved in tetrachlorohydroquinone formation were undetectable. The formation of tetrachlorohydroquinone was not detectable in the cultures added with either piperonyl butoxide or cycloheximide (an inhibitor of de novo protein synthesis). These results revealed the pentachlorophenol oxidation by induced P450 in the fungus, and it should be the first time that P450-mediated pentachlorophenol oxidation was demonstrated in a microorganism. Furthermore, the addition of the P450 inhibitor to the cultures led to obvious increase of pentachlorophenol, suggesting that the relationship between P450 and pentachlorophenol methylation is worthy of further research.
DOI: 10.1371/journal.pone.0045887
PubMed: 23029295
PubMed Central: PMC3447798
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pubmed:23029295Le document en format XML
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<front><div type="abstract" xml:lang="en">The occurrence of cytochrome P450 and P450-mediated pentachlorophenol oxidation in a white rot fungus Phanerochaete chrysosporium was demonstrated in this study. The carbon monoxide difference spectra indicated induction of P450 (103±13 pmol P450 per mg protein in the microsomal fraction) by pentachlorophenol. The pentachlorophenol oxidation by the microsomal P450 was NADPH-dependent at a rate of 19.0±1.2 pmol min(-1) (mg protein)(-1), which led to formation of tetrachlorohydroquinone and was significantly inhibited by piperonyl butoxide (a P450 inhibitor). Tetrachlorohydroquinone was also found in the cultures, while the extracellular ligninases which were reported to be involved in tetrachlorohydroquinone formation were undetectable. The formation of tetrachlorohydroquinone was not detectable in the cultures added with either piperonyl butoxide or cycloheximide (an inhibitor of de novo protein synthesis). These results revealed the pentachlorophenol oxidation by induced P450 in the fungus, and it should be the first time that P450-mediated pentachlorophenol oxidation was demonstrated in a microorganism. Furthermore, the addition of the P450 inhibitor to the cultures led to obvious increase of pentachlorophenol, suggesting that the relationship between P450 and pentachlorophenol methylation is worthy of further research.</div>
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<Abstract><AbstractText>The occurrence of cytochrome P450 and P450-mediated pentachlorophenol oxidation in a white rot fungus Phanerochaete chrysosporium was demonstrated in this study. The carbon monoxide difference spectra indicated induction of P450 (103±13 pmol P450 per mg protein in the microsomal fraction) by pentachlorophenol. The pentachlorophenol oxidation by the microsomal P450 was NADPH-dependent at a rate of 19.0±1.2 pmol min(-1) (mg protein)(-1), which led to formation of tetrachlorohydroquinone and was significantly inhibited by piperonyl butoxide (a P450 inhibitor). Tetrachlorohydroquinone was also found in the cultures, while the extracellular ligninases which were reported to be involved in tetrachlorohydroquinone formation were undetectable. The formation of tetrachlorohydroquinone was not detectable in the cultures added with either piperonyl butoxide or cycloheximide (an inhibitor of de novo protein synthesis). These results revealed the pentachlorophenol oxidation by induced P450 in the fungus, and it should be the first time that P450-mediated pentachlorophenol oxidation was demonstrated in a microorganism. Furthermore, the addition of the P450 inhibitor to the cultures led to obvious increase of pentachlorophenol, suggesting that the relationship between P450 and pentachlorophenol methylation is worthy of further research.</AbstractText>
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