[Oxidative modification of cytochrome P-450 during its function. II. Study of the mechanism of cytochrome P-450 LM2 inactivation in a soluble reconstructed monooxygenase system].
Inactivation of cytochrome P-450 LM2 induced by hydrogen peroxide formed in the active site of the enzyme was studied. Catalase did not protect cytochrome P-450 LM2 from inactivation during its operation in a soluble reconstituted system. The hemoprotein inactivation in this system was found to depend on the ratio of hemo- to flavoproteins. It was demonstrated that cytochrome P-450 LM2 inactivation during catalysis is accompanied by cleavage of the hemoprotein molecule. It is probable that this fact plays a key role in regulation of enzyme decay.
Tret'iakova
L Z
LZ
Adrianov
N V
NV
Voronin
E M
EM
Dovgiĭ
A I
AI
Skotselias
E D
ED
Archakov
A I
AI
D000818:Animals; D001665:Binding Sites; D002848:Chromatography, DEAE-Cellulose; D065607:Cytochrome P-450 Enzyme Inhibitors; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D005420:Flavoproteins / Q000378:metabolism; D006420:Hemeproteins / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000494:pharmacology; D007525:Isoelectric Focusing; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D010084:Oxidation-Reduction; D011817:Rabbits
D065607:Cytochrome P-450 Enzyme Inhibitors; D005420:Flavoproteins; D006420:Hemeproteins; D003577:Cytochrome P-450 Enzyme System; D006861:Hydrogen Peroxide; D006899:Mixed Function Oxygenases
Okislitel'naia modifikatsiia tsitokhorma P-450 pri ego rabote. II. Issledovanie mekhanizma inaktivatsii tsitokhroma P-450 LM2 v rastvorimoĭ rekonstruirovannoĭ monooksigenaznoĭ sisteme.