Reconstitution of liver monooxygenase system in solution from cytochrome P-450 and NADPH-specific flavoprotein monomers

Biochemical and Biophysical Research Communications
G I BachmanovaA I Archakov

Abstract

Microsomal monooxygenase system was reconstituted in the presence of non-ionic detergent Emulgen 913 from cytochrome P-450 and NADPH-specific flavoprotein isolated from phenobarbital-induced rabbit liver microsomes. At Emulgen 913 concentration of 0.05 g/l mixed complex between flavoprotein and cytochrome was formed with 5: 5 protein molar ratio and molecular weight of 700 kD. The 2-hour incubation of the enzymes with 0.25 g/l Emulgen 913 at 4 degrees C was accompanied by dissociation of protein oligomers to monomers. The reconstituted systems containing flavoprotein and cytochrome as mixed complexes or monomers were able to catalyze NADPH-dependent cytochrome P-450 reduction and benzphetamine N-demethylation. Taking into consideration the effective concentrations of the enzymes the apparent second order rate constants of these reactions with monomers were 100 times those with complexes.

Citations

Jan 1, 1994·Free Radical Biology & Medicine·I I Karuzina, A I Archakov
May 1, 1989·European Journal of Biochemistry· Uvarov VYuA I Archakov
Sep 17, 1990·FEBS Letters·K N Myasoedova, P Berndt

Related Concepts

Cytochrome P-450 CYP2B (lung microsomal)
Metazoa
Cytochrome P-450 Oxygenase
Flavoproteins
Alloenzymes
Mathematics
Microsomes, Liver
NADP
Oxidoreductases, N-Demethylating
Oxygenases

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