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• W2040988891 abstract "The presence of cytochrome P-450 and P-450-mediated benzo(a)pyrene hydroxylase activity in both microsomal and soluble fractions of the white rot fungus Phanerochaete chrysosporium was shown. The reduced carbon monoxide difference spectrum showed maxima at 448-450 and 452-454 nm for microsomal and cytosolic fractions, respectively. Both P-450 fractions produced a Type I substrate binding spectrum on addition of benzo(a)pyrene. Activity for benzo(a)pyrene hydroxylation was NADPH dependent and inhibited by carbon monoxide. Km values for activity showed a difference between the cellular fractions with a Km of 89 microM for microsomal P-450 and 400 microM for cytosolic P-450. The Vmax values observed were 0.83 nmol min-1 (nmol microsomal P-450)-1 and 0.4 nmol min-1 (nmol cytosolic P-450)-1. The results indicate that P-450-mediated benzo(a)pyrene hydroxylase activity could play a role in xenobiotic transformation by this fungus beside the known ligninolytic exocellular enzymes." @default.
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• W2040988891 date "1996-01-01" @default.
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• W2040988891 title "Evidence for cytochrome P-450 and P-450-mediated benzo(a) pyrene hydroxylation in the white rot fungus<i>Phanerochaete chrysosporium</i>" @default.
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• W2040988891 doi "https://doi.org/10.1111/j.1574-6968.1996.tb07965.x" @default.
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