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D P Barr

Publications and source records attributed to D P Barr.

25 records · Page 2Linked to original sources
PubMed1992

Use of white rot fungi in the degradation of environmental chemicals.

White rot fungi have been shown to mineralize a wide variety of environmental pollutants. These fungi secrete a number of enzymes that are involved in its unique ability to degrade lignin, the structural component of woody plants. Lignin is a very complex heteropolymer that can only be degraded by white rot fungi. Degradation is complete without energy value to the fungus. The evolution of this ability has apparently given the organism the ability to degrade structurally diverse and normally very recalcitrant environmental pollutants such as DDT, PCB, benzo(a)pyrene, TNT, etc. Some of the major enzymes that are secreted by the fungi are peroxidases with unique properties. In addition to their ability to catalyze a wide variety of oxidations, they can also catalyze indirect oxidations and reductions. The fungi synthesize and secrete hydrogen peroxide to activate the peroxidases, veratryl alcohol to serve as a free radical intermediate for indirect oxidations, and electron donors, such as oxalate, which with veratryl alcohol catalyze reductions. Reductions are often required for subsequent oxidation of chemicals by the peroxidases. The enzymes can also reduce molecular oxygen.

Basidiomycota↗
PubMedDate not supplied

Reaction of cytochrome P450 with cumene hydroperoxide: ESR spin-trapping evidence for the homolytic scission of the peroxide O-O bond by ferric cytochrome P450 1A2.

ESR spin trapping was used to investigate the reaction of rabbit cytochrome P450 (P450) 1A2 with cumene hydroperoxide. Cumene hydroperoxide-derived peroxyl, alkoxyl, and carbon-centered radicals were formed and trapped during the reaction. The relative contributions of each radical adduct to the composite ESR spectrum were influenced by the concentration of the spin trap. Computer simulation of the experimental data obtained at various 5,5-dimethyl-1-pyrroline N-oxide (DMPO) concentrations was used to quantitate the contributions of each radical adduct to the composite ESR spectrum. The alkoxyl radical was the initial radical produced during the reaction. Experiments with 2-methyl-2-nitrosopropane identified the carbon-centered adducts as those of the methyl radical, hydroxymethyl radical, and a secondary carbon-centered radical. The reaction did not require NADPH-cytochrome P450 reductase or NADPH. It is concluded that the reaction involves the initial homolytic scission of the peroxide O-O bond to produce the cumoxyl radical. Methyl radicals were produced from the beta-scission of the cumoxyl radical. The peroxyl adduct was not observed in the absence of molecular oxygen. We conclude that the DMPO peroxyl radical adduct detected in the presence of oxygen was due to the methylperoxyl radical formed by the reaction of the methyl radical with oxygen. At a higher P450 concentration, a protein-derived radical adduct was also detected.

Animals↗