Protein Information

Name cytochrome P450 (protein family or complex)
Synonyms cytochrome P450; cytochrome P 450; CYP450; CYP 450

Compound Information

Name sodium azide
CAS sodium azide

Reference List

PubMed Abstract RScore(About this table)
7517501 Lee CK, Munoz JA, Fulp C, Chang KM, Rogers JC, Borgerding MF, Doolittle DJ: Inhibitory activity of cigarette-smoke condensate on the mutagenicity of heterocyclic amines. Mutat Res. 1994 Jul;322(1):21-32.

However, CSC had no effect on the activity of direct-acting mutagens (2-nitrofluorene, sodium azide, 4-nitro-1,2-phenylenediamine, 4-nitroquinoline N-oxide and methyl methanesulfonate).
CSC exhibited a potent inhibitory effect on the cytochrome P-450 dependent monooxygenases, ethoxyresorufin O-deethylase and B [a] P hydroxylase.
2(0,0,0,2) Details
11166292 Nelli S, McIntosh L, Martin W: Role of copper ions and cytochrome P450 in the vasodilator actions of the nitroxyl anion generator, Angeli's salt, on rat aorta. Eur J Pharmacol. 2001 Feb 2;412(3):281-9.

2(0,0,0,2) Details
8415911 Zaidi SI, Agarwal R, Eichler G, Rihter BD, Kenney ME, Mukhtar H: Photodynamic effects of new silicon phthalocyanines: in vitro studies utilizing rat hepatic microsomes and human erythrocyte ghosts as model membrane sources. Photochem Photobiol. 1993 Aug;58(2):204-10.

Of the newly synthesized Pc, two showed significant destruction of cytochrome P-450 and monooxygenase activities, and enhancement of lipid peroxidation, when added to microsomal suspension followed by irradiation with approximately 675 nm light.
Sodium azide, histidine, and 2,5-dimethylfuran, the quenchers of singlet oxygen, afforded highly significant protection against SiPc IV- and SiPc V-mediated photodynamic effects.
2(0,0,0,2) Details
8033320 Li Y, Trush MA, Yager JD: DNA damage caused by reactive oxygen species originating from a copper-dependent oxidation of the 2-hydroxy catechol of estradiol. Carcinogenesis. 1994 Jul;15(7):1421-7.

It has previously been proposed that redox cycling between catechol estrogens and their quinones, mediated by cytochrome P450, could lead to the generation of free radicals that would subsequently cause oxidative damage to DNA and proteins that might have a role in hormonal carcinogenesis.
The appearance of strand breaks was also blocked by catalase and inhibited by the singlet oxygen scavengers sodium azide and 2,2,6,6-tetramethyl-4-piperidone.
1(0,0,0,1) Details
12112443 Bendayan R, Lee G, Bendayan M: Functional expression and localization of P-glycoprotein at the blood brain barrier. Microsc Res Tech. 2002 Jun 1;57(5):365-80.

In addition, results from functional studies show that the accumulation of the P-glycoprotein substrate digoxin by RBE4 monolayer cells is significantly enhanced in the presence of standard P-glycoprotein inhibitors (verapamil, cyclosporin A, PSC 833), protease inhibitors (saquinavir, ritonavir, indinavir), and the metabolic inhibitor, sodium azide.
However, results from molecular biology, immunocytochemistry, biochemistry, and transport studies show that the cerebral endothelial cells possess an asymmetrical array of metabolic enzymes (i.e., alkaline phosphatase, cytochrome P450 enzymes, glutathione transferases) and energy-dependent efflux transport proteins (i.e., P-glycoprotein and Multidrug-resistance proteins) that are instrumental to the barrier function.
1(0,0,0,1) Details
10491304 Osada M, Ogura Y, Yasui H, Sakurai H: Involvement of singlet oxygen in cytochrome P450-dependent substrate oxidations. Biochem Biophys Res Commun. 1999 Sep 24;263(2):392-7.

The addition of beta-carotene, a quencher of singlet oxygen species ((1) O (2)), suppressed the aniline hydroxylation, while the addition of sodium azide (NaN (3)) ((1) O (2) quencher) enhanced the reaction.
2(0,0,0,2) Details
17346675 Herraiz T, Guillen H, Galisteo J: N-methyltetrahydro-beta-carboline analogs of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) neurotoxin are oxidized to neurotoxic beta-carbolinium cations by heme peroxidases. Biochem Biophys Res Commun. 2007 Apr 27;356(1):118-23. Epub 2007 Feb 26.

Neither, cytochrome P-450 2D6 or a mixture of six P450 enzymes carried out this oxidation in a significant manner.
Peroxidase inhibitors (hydroxylamine, sodium azide, and ascorbic acid) highly reduced or abolished this oxidation.
1(0,0,0,1) Details
9390169 Reinke LA, Moore DR, McCay PB: Mechanisms for metabolism of ethanol to 1-hydroxyethyl radicals in rat liver microsomes. Arch Biochem Biophys. 1997 Dec 1;348(1):9-14.


HER formation was almost abolished by the combination of superoxide dismutase and deferoxamine in both buffers, suggesting little enzymatic HER formation by the cytochrome P450 enzymes.
1(0,0,0,1) Details
9644252 Matsunaga I, Yamada M, Kusunose E, Miki T, Ichihara K: Further characterization of hydrogen peroxide-dependent fatty acid alpha-hydroxylase from Sphingomonas paucimobilis. J Biochem. 1998 Jul;124(1):105-10.

Among cytochrome P450 inhibitors, SKF-525A markedly inhibited the activity at the concentration of 2 mM, but CO did not.
Potassium cyanide and sodium azide inhibited the FAAH activity in a concentration-dependent manner.
1(0,0,0,1) Details
10569638 Goldman R, Claycamp GH, Sweetland MA, Sedlov AV, Tyurin VA, Kisin ER, Tyurina YY, Ritov VB, Wenger SL, Grant SG, Kagan VE: Myeloperoxidase-catalyzed redox-cycling of phenol promotes lipid peroxidation and thiol oxidation in HL-60 cells. Free Radic Biol Med. 1999 Nov;27(9-10):1050-63.


Unlike biotransformation by cytochrome P450 enzymes, peroxidases activate most substrates by one-electron oxidation via radical intermediates.
1(0,0,0,1) Details
8625450 Barcelo S, Gardiner JM, Gescher A, Chipman JK: CYP2E1-mediated mechanism of anti-genotoxicity of the broccoli constituent sulforaphane. Carcinogenesis. 1996 Feb;17(2):277-82.

We investigated the ability of sulforaphane to also inhibit the phase I enzyme cytochrome P450 isoenzyme 2E1 (CYP2E1), which is responsible for activation of several carcinogens, including dialkylnitrosamines.
Sulforaphane was unable to inhibit mutagenicity of sodium azide (5 micrograms/plate), a direct acting mutagen, in the Salmonella assay.
1(0,0,0,1) Details
16930212 Zimatkin SM, Pronko SP, Vasiliou V, Gonzalez FJ, Deitrich RA: Enzymatic mechanisms of ethanol oxidation in the brain. . Alcohol Clin Exp Res. 2006 Sep;30(9):1500-5.


RESULTS: The catalase inhibitors sodium azide (5 mM) and aminotriazole (5 mM) as well as CYP2E1 inhibitors diallyl sulfide (2 mM) and beta-phenethyl isothiocyanate (0.1 mM) lowered significantly the accumulation of the ethanol-derived AC and acetate in brain homogenates.
0(0,0,0,0) Details
9794700 Haber PS, Apte MV, Applegate TL, Norton ID, Korsten MA, Pirola RC, Wilson JS: Metabolism of ethanol by rat pancreatic acinar cells. J Lab Clin Med. 1998 Oct;132(4):294-302.


Phenanthroline (an inhibitor of classes I through III isoenzymes of alcohol dehydrogenase (ADH)) inhibited pancreatic ethanol oxidation by 90%, but 4-methylpyrazole (a class I and II ADH inhibitor), carbon monoxide (a cytochrome P450 inhibitor), and sodium azide (a catalase inhibitor) had no effect.
0(0,0,0,0) Details
12616597 Castro GD, Delgado de Layno AM, Costantini MH, Castro JA: Rat breast microsomal biotransformation of ethanol to acetaldehyde but not to free radicals: its potential role in the association between alcohol drinking and breast tumor promotion. Teratog Carcinog Mutagen. 2003;Suppl 1:61-70.


It is inhibited by diethyldithiocarbamate (DDTC), sodium azide, and diphenyleneiodonium (DPI) but not by desferrioxamine, which suggests a possible role of a non-iron copper-requiring flavoenzyme.
0(0,0,0,0) Details
9918136 Williams JA, Stone EM, Millar BC, Gusterson BA, Grover PL, Phillips DH: Determination of the enzymes responsible for activation of the heterocyclic amine 2-amino-3-methylimidazo [4,5-f] quinoline in the human breast. Pharmacogenetics. 1998 Dec;8(6):519-28.


Adduct formation in stimulated neutrophils was inhibited 80% by the myeloperoxidase inhibitor sodium azide (1 mM) but was not affected by proadifen (100 microM), indomethacin (100 microM), or eicosatetraynoic acid (100 microM), inhibitors of cytochrome P450, prostaglandin synthetase, and lipoxygenase, respectively.
0(0,0,0,0) Details
8929553 Bednar MM, Balazy M, Murphy M, Booth C, Fuller SP, Barton A, Bingham J, Golding L, Gross CE: Peroxynitrite augments fMLP-stimulated chemiluminescence by neutrophils in human whole blood. J Leukoc Biol. 1996 Nov;60(5):619-24.


Both sodium azide and taurine significantly inhibited LDCL (93% inhibition with 100 microM azide, 52% inhibition with 10 mM taurine).
0(0,0,0,0) Details
7867972 Karuzina II, Archakov AI: Hydrogen peroxide-mediated inactivation of microsomal cytochrome P450 during monooxygenase reactions. Free Radic Biol Med. 1994 Dec;17(6):557-67.

The acceleration of cytochrome P450 loss in the presence of catalase inhibitors (sodium azide, hydroxylamine) indicates that hydrogen peroxide is involved in hemoprotein degradation.
88(1,1,1,8) Details
17520814 Tian L, Yang XW, Wang Y, Xu W: [Characteristics of uptake, transport and efflux of Z- and E-ajoenes in Caco-2 cell monolayers in vitro]. Yao Xue Xue Bao. 2007 Jan;42(1):87-92.

The metabolism of Z- and E-ajoenes in Caco-2 cell monolayers can be partially inhibited by vitamin C as an anti-oxidant, metyrapone as an inhibitor to subtype CYP3A of cytochrome P450 drug metabolism enzymes, and sodium azide as an inhibitor to ATP production.
82(1,1,1,2) Details