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RECORD NUMBER: 21 OF 43

OLS Field Name OLS Field Data
Main Title Oxidative Degradation of Phenanthrene by the Ligninolytic Fungus 'Phanerochaete chrysosposium'.
Author Hammel, K. E. ; Gai, W. Z. ; Green, B. ; Moen, M. A. ;
CORP Author Forest Products Lab., Madison, WI. ;State Univ. of New York Coll. of Environmental Science and Forestry, Syracuse.;Environmental Protection Agency, Cincinnati, OH. Risk Reduction Engineering Lab.
Publisher c1992
Year Published 1992
Report Number EPA-R-813530; EPA/600/J-93/192;
Stock Number PB93-199511
Additional Subjects Lignin ; Biodegradation ; Phenanthrenes ; Oxidation ; Nitrogen ; Catalysis ; Environmental pollutants ; Reprints ; Phanerochaete chrysosporium ; Phenanthrene quinones ; Lignin peroxidases
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NTIS  PB93-199511 Most EPA libraries have a fiche copy filed under the call number shown. Check with individual libraries about paper copy. NTIS 08/23/1993
Collation 9p
Abstract
The ligninolytic fungus Phanerochaete chrysosporium oxidized phenanthrene and phenanthrene-9,10-quinone (PQ) at their C-9 and C-10 positions to give a ring-fission product, 2,2'-diphenic acid (DPA), which was identified in chromatographic and isotope dilution experiments. DPA formation from phenanthrene was somewhat greater in low-nitrogen (ligninolytic) cultures than in high-nitrogen (nonligninolytic) cultures and did not occur in uninoculated cultures. The oxidation of PQ to DPA involved both fungal and abiotic mechanisms, was unaffected by the level of nitrogen added, and was significantly faster than the cleavage of phenanthrene to DPA. Phenanthrene-trans-9,10-dihydrodiol, which was previously shown to be the principal phenanthrene metabolite in nonligninolytic P. chrysosporium cultures, was not formed in the ligninolytic cultures employed here. These results suggest that phenanthrene degradation by ligninolytic P. chrysosporium proceeds in order from phenanthrene -> PQ -> DPA, involves both ligninolytic and nonligninolytic enzymes, and is not initiated by a classical microsomal cytochrome P-450. The extracellular lignin peroxidases of P. chrysosporium were not able to oxidize phenanthrene in vitro and therefore are also unlikely to catalyze the first step of phenanthrene degradation in vivo. Both phenanthrene and PQ were mineralized to similar extents by the fungus, which supports the intermediacy of PQ in phenanthrene degradation, but both compounds were mineralized significantly less than the structurally related lignin peroxidase substrate pyrene was. (Copyright (c) 1992, American Society for Microbiology.)