CUMENE HYDROPEROXIDE-DEPENDENT AND NADPHDRIVEN N-OXIDATION OF p-CHLOROANILINE BY RABBIT LIVER MICROSOMAL CYTOCHROME P-450

1981 ◽  
Vol 9 (2) ◽  
pp. 357P-357P
Author(s):  
Peter Hlavica ◽  
Ines Baden
Keyword(s):  
Cumene Hydroperoxide ◽  
Rabbit Liver ◽  
Microsomal Cytochrome ◽  
Cytochrome P 450

scholarly journals Oxidation of arylcyclopropanes by rabbit liver cytochrome P-450. Mechanistic implications of a multiple oxidation

1985 ◽  
Vol 232 (1) ◽  
pp. 199-203 ◽  
Author(s):  
C J Suckling ◽  
D C Nonhebel ◽  
L Brown ◽  
K E Suckling ◽  
S Seilman ◽  
...  
Keyword(s):  
Active Site ◽  
Microsomal Fraction ◽  
Cumene Hydroperoxide ◽  
Rabbit Liver ◽  
Microsomal Cytochrome ◽  
Liver Cytochrome ◽  
Liver Microsomal Fraction ◽  
Reconstituted System ◽  
Mechanism Of Oxidation ◽  
Cytochrome P 450

The arylcyclopropanes (cyclopropylarenes) cyclopropylbenzene and diphenylcyclopropane are oxidized by rabbit liver microsomal cytochrome P-450, both by the microsomal fraction and by the purified cytochrome in a reconstituted system. The products formed, principally benzoic acid, are due to an unusual triple oxidation of the substrate, which probably remains attached to the active site during the several steps of the oxidation. Both substrates were found to be inhibitors of the cytochrome P-450-dependent O-de-ethylation of 7-ethoxycoumarin. Model oxidation studies with cumene hydroperoxide as oxidizing agent and rabbit liver microsomal fraction as source of enzyme gave similar products to the microsomal and reconstituted systems. The significance of these results in the mechanism of oxidation catalysed by cytochrome P-450 is discussed.

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