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  • Title: [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].
    Author: Tret'iakova LZ, Adrianov NV, Voronin EM, Dovgiĭ AI, Skotselias ED, Archakov AI.
    Journal: Biokhimiia; 1991 Jul; 56(7):1200-8. PubMed ID: 1932347.
    Abstract:
    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.
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