title: EM-field effect upon properties of NADPH-cytochrome P-450 reductase with model substrates.
abstract: Artificial substrates, including ferricyanide and dichlorophenol indophenol (IP), are frequently used to model the activity of NADPH-cytochrome P-450 reductase, in the xenobiotic-metabolic pathway catalyzed by the P-450 complex. Here, the two oxidants were compared in a microsomal preparation from chicken liver. Low-energy 9.14 GHz perturbation affected both reactions similarly, though the IP reaction may be more sensitive to extremely low energy levels. The reactions of the two oxidants differed from each other in their response to the prior incubation of the microsomes with carbon monoxide and to the presence of superoxide dismutase. The mechanics of the reduction of ferricyanide and the reduction of IP are not identical and the electron-flow paths may be dissimilar. Microwave effect cannot be attributed a temperature change in the reaction medium; it appears to occur at the level of the electron-flow path across the dual-flavin reductase.
authors.affiliation: Department of Biochemistry, NJAES, Rutgers University, New Brunswick 08903.
authors.forename: H D
authors.initials: HD
authors.lastname: Brown
authors.forename: S K
authors.initials: SK
authors.lastname: Chattopadhyay
mesh_terms: D000818:Animals; D002248:Carbon Monoxide / Q000378:metabolism / Q000494:pharmacology; D002645:Chickens; D055590:Electromagnetic Phenomena; D005260:Female; D008862:Microsomes, Liver / Q000201:enzymology*; D008872:Microwaves; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism* / Q000528:radiation effects; D013482:Superoxide Dismutase / Q000494:pharmacology
chemical_list: D002248:Carbon Monoxide; D013482:Superoxide Dismutase; D009251:NADPH-Ferrihemoprotein Reductase