Hydroxylation of phenol to catechol by Candida tropicalis: involvement of cytochrome P450
Language English Country Slovakia Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
14661729
Knihovny.cz E-resources
- MeSH
- Biodegradation, Environmental MeSH
- Candida tropicalis enzymology growth & development MeSH
- Water Pollutants, Chemical metabolism MeSH
- Water Purification methods MeSH
- Phenol metabolism MeSH
- Hydroxylation MeSH
- Catechols metabolism MeSH
- Coenzymes metabolism MeSH
- Microsomes enzymology MeSH
- Industrial Waste prevention & control MeSH
- Cytochrome P-450 Enzyme System metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- catechol MeSH Browser
- Water Pollutants, Chemical MeSH
- Phenol MeSH
- Catechols MeSH
- Coenzymes MeSH
- Industrial Waste MeSH
- Cytochrome P-450 Enzyme System MeSH
Microsomal preparations isolated from yeast Candida tropicalis (C. tropicalis) grown on three different media with or without phenol were isolated and characterized for the content of cytochrome P450 (CYP) (EC 1.14.15.1). While no CYP was detected in microsomes of C. tropicalis grown on glucose as the carbon source, evidence was obtained for the presence of the enzyme in the microsomes of C. tropicalis grown on media containing phenol. Furthermore, the activity of NADPH: CYP reductase, another enzyme of the microsomal CYP-dependent system, was markedly higher in cells grown on phenol. Microsomes of these cells oxidized phenol. The major metabolite formed from phenol by microsomes of C. tropicalis was characterized by UV/vis absorbance and mass spectroscopy as well as by the chromatographic properties on HPLC. The characteristics are identical to those of catechol. The formation of catechol was inhibited by CO, the inhibitor of CYP, and correlated with the content of cytochrome P450 in microsomes. These results, the first report showing the ring hydroxylation of phenol to catechol with the microsomal enzyme system of C. tropicalis, strongly suggest that CYP-catalyzed reactions are responsible for this hydroxylation. The data demonstrate the progress in resolving the enzymes responsible for the first step of phenol degradation by the C. tropicalis strain.
