BIOMAT Database Logo BIOMAT Database Logo

[Inhibitory action of divalent copper compounds on cumene hydroperoxide oxidative demethylation of N,N-dimethylaniline by cytochrome P-450]. 1980

V P Kurchenko, and S A Usanov, and D I Metelitsa

The inhibitory action of divalent copper compounds on hydroperoxide-dependent oxidative demethylation of N,N-demethylaniline involving rabbit liver microsomes and highly purified cytochrome P-450 has been studied. CuCl2 is a non-competitive inhibitor, whereas copper tyrosine and lysine complexes are characterized by a mixed type inhibition. The inhibitory action of copper complexes is based on a decrease of cumene hydroperoxide concentration. The reaction results in formation of RO and RO2 radicals destroying cytochrome P-450 CuCl2 (0,001 M) also destroys cytochrome P-450 in the absence of cumene hydroperoxide; the destruction process is characterized by two phases with different rate constants. The nature of the inhibitory action of CuCl2 on N,N-demethylaniline oxidation by hydroperoxides is discussed.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008862 Microsomes, Liver Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough. Liver Microsomes,Liver Microsome,Microsome, Liver
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D010545 Peroxides A group of compounds that contain a bivalent O-O group, i.e., the oxygen atoms are univalent. They can either be inorganic or organic in nature. Such compounds release atomic (nascent) oxygen readily. Thus they are strong oxidizing agents and fire hazards when in contact with combustible materials, especially under high-temperature conditions. The chief industrial uses of peroxides are as oxidizing agents, bleaching agents, and initiators of polymerization. (From Hawley's Condensed Chemical Dictionary, 11th ed) Peroxide
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D003300 Copper A heavy metal trace element with the atomic symbol Cu, atomic number 29, and atomic weight 63.55. Copper-63,Copper 63
D003577 Cytochrome P-450 Enzyme System A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism. Cytochrome P-450,Cytochrome P-450 Enzyme,Cytochrome P-450-Dependent Monooxygenase,P-450 Enzyme,P450 Enzyme,CYP450 Family,CYP450 Superfamily,Cytochrome P-450 Enzymes,Cytochrome P-450 Families,Cytochrome P-450 Monooxygenase,Cytochrome P-450 Oxygenase,Cytochrome P-450 Superfamily,Cytochrome P450,Cytochrome P450 Superfamily,Cytochrome p450 Families,P-450 Enzymes,P450 Enzymes,Cytochrome P 450,Cytochrome P 450 Dependent Monooxygenase,Cytochrome P 450 Enzyme,Cytochrome P 450 Enzyme System,Cytochrome P 450 Enzymes,Cytochrome P 450 Families,Cytochrome P 450 Monooxygenase,Cytochrome P 450 Oxygenase,Cytochrome P 450 Superfamily,Enzyme, Cytochrome P-450,Enzyme, P-450,Enzyme, P450,Enzymes, Cytochrome P-450,Enzymes, P-450,Enzymes, P450,Monooxygenase, Cytochrome P-450,Monooxygenase, Cytochrome P-450-Dependent,P 450 Enzyme,P 450 Enzymes,P-450 Enzyme, Cytochrome,P-450 Enzymes, Cytochrome,Superfamily, CYP450,Superfamily, Cytochrome P-450,Superfamily, Cytochrome P450
D000814 Aniline Compounds Compounds that include the aminobenzene structure. Phenylamine,Phenylamines,Anilines,Compounds, Aniline
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001555 Benzene Derivatives Organic compounds derived from BENZENE. Derivatives, Benzene

Related Publications

V P Kurchenko, and S A Usanov, and D I Metelitsa
Cumene hydroperoxide supported demethylation of N,N-dimethylaniline by cytochrome P-450 from adrenal cortex mitochondria.
January 1982, Acta biologica et medica Germanica,
V P Kurchenko, and S A Usanov, and D I Metelitsa
Oxidative N-demethylation of N,N-dimethylaniline by purified isozymes of cytochrome P-450.
July 1989, Biochemical pharmacology,
V P Kurchenko, and S A Usanov, and D I Metelitsa
Cumene hydroperoxide effected hydroperoxidation by cytochrome P-450.
April 1985, Archives of biochemistry and biophysics,
V P Kurchenko, and S A Usanov, and D I Metelitsa
[O-demethylation kinetics of anisole and p-chloroanisole by cumene hydroperoxide and cytochrome P-450 of liver microsomes].
November 1977, Biokhimiia (Moscow, Russia),
V P Kurchenko, and S A Usanov, and D I Metelitsa
Comparative studies on the cumene hydroperoxide- and NADPH-supported N-oxidation of 4-chloroaniline by cytochrome P-450.
June 1983, The Biochemical journal,
V P Kurchenko, and S A Usanov, and D I Metelitsa
The role of cytochrome P-450 in the dual pathways of N-demethylation of N,N-dimethylaniline by hepatic microsomes.
January 1984, Xenobiotica; the fate of foreign compounds in biological systems,
V P Kurchenko, and S A Usanov, and D I Metelitsa
Radical mechanism of aminopyrine oxidation by cumene hydroperoxide catalyzed by purified liver microsomal cytochrome P-450.
December 1980, Archives of biochemistry and biophysics,
V P Kurchenko, and S A Usanov, and D I Metelitsa
[Effects of phospholipids on oxidative demethylation of dimethylcyclohexylamine by cumene hydroperoxide involving methemoglobin].
December 1981, Biokhimiia (Moscow, Russia),
V P Kurchenko, and S A Usanov, and D I Metelitsa
Chemiluminescence of luminol caused by interaction of cytochrome P-450 and cytochrome C with cumene hydroperoxide: comparative studies.
January 1985, Biomedica biochimica acta,
V P Kurchenko, and S A Usanov, and D I Metelitsa
The mechanism of cumene hydroperoxide-dependent lipid peroxidation: the function of cytochrome P-450.
November 1986, Archives of biochemistry and biophysics,
Copied contents to your clipboard!