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Cytochrome P450 oxidoreductase

Crespi, C.L. and Miller, V.P. (1997) The R144C change in the CYP2C9 2 allele alters interaction ofthe cytochrome P450 with NADPH cytochrome P450 oxidoreductase. Pharmacogenetics, 7 (3), 203-210. [Pg.239]

Fig. 21.2 TROSY (left) and SEA-TROSY (right) 1sN, H correlation spectra of 0.5 mM 2H/,5N-la-beled cytochrome P450 oxidoreductase from rat liver (95% H20, 5% D20 7=303 K, pH = 7.5). Fig. 21.2 TROSY (left) and SEA-TROSY (right) 1sN, H correlation spectra of 0.5 mM 2H/,5N-la-beled cytochrome P450 oxidoreductase from rat liver (95% H20, 5% D20 7=303 K, pH = 7.5).
U-2H/15N and U-2H/15N/13C-labeled cytochrome P450 oxidoreductase from rat liver, lacking the N terminal 56 residues and the C-terminal WS sequence. The TROSY spectrum was obtained with the same pulse scheme but without the SEA... [Pg.462]

Fig. 21.4 Three-dimensional structure of the enzyme cytochrome P450 oxidoreductase. The cofactors FAD and FMN are depicted in light blue. Loop regions are represented by cylindrical rods (yellow) a-helices and /(-sheets (in white) are represented by ribbons and arrows, respectively. Resonance assignments for the residues located in the key loops regions [30] highlighted in purple and red were obtained with a 3D SEA-HNCA-TROSY experiment. Fig. 21.4 Three-dimensional structure of the enzyme cytochrome P450 oxidoreductase. The cofactors FAD and FMN are depicted in light blue. Loop regions are represented by cylindrical rods (yellow) a-helices and /(-sheets (in white) are represented by ribbons and arrows, respectively. Resonance assignments for the residues located in the key loops regions [30] highlighted in purple and red were obtained with a 3D SEA-HNCA-TROSY experiment.
In 2004, three groups demonstrated that the condition was caused by mutations in cytochrome P450 oxidoreductase, the essential redox partner for microsomal hydroxylases. Fluck and co-workers [17] were the first to publish, followed soon after... [Pg.582]

Adachi M, Tachibana K, Asakura Y, Yamamoto T, Hanaki K, Oka A (2004) Compound heterozygous mutations of cytochrome P450 oxidoreductase gene (POR) in two patients with Ant-ley-Bixler syndrome. Am J Med Genet A 128 333-339... [Pg.600]

Fan LQ, Coley J, Miller RT, Cattley RC, Corton JC. Opposing mechanisms of NADPH-cytochrome P450 oxidoreductase regulation by peroxisome prolif-erators. Biochem Pharmacol 2003 65 949 959. [Pg.194]

Mikalsen A, Capellmann M, Alexander J. 1995. The role of iron chelators and oxygen in the reduced nicotinamide adenine dinucleotide phosphate-cytochrome P450 oxidoreductase-dependent chromium(VI) reduction. Analyst 120 935-938. [Pg.444]

Smith, G. C. M., Tew, D. G., and Wolf, C. R. 1994. Dissection of Nadph-Cytochrome P450 Oxidoreductase into Distinct Functional Domains. Proc. Natl Acad. Sci., 91, 8710-8714. [Pg.307]

Monooxygenation reactions involve the reduction of one atom of molecular oxygen to water and the incorporation of the other oxygen atom into the substrate [Eq. (9.1)]. The electrons involved in the reduction of CYP are transferred from NADPH by another enzyme called NADPH-cytochrome P450 oxidoreductase (CYPOR). [Pg.148]

Shiota, N., Nagasawa, A., Sakaki, T., Yabusaki, Y., and Ohkawa, H. 1994. Herbicide-resistant tobacco plants expressing the fused enzyme between rat cytochrome P4501al (Cyplal) and yeast NADPH-cytochrome P450 oxidoreductase. Plant Physiol., 106, 17-23. [Pg.260]

Smith, G.C.M., D.G. Tew, and C.R. Wolf (1994). Dissection of NADPH-cytochrome P450 oxidoreductase Into distinct functional domains. Proc. Natl. Acad. Sci. USA 91, 8710-8714. [Pg.139]

Shen, A.L., K.A. O Leary, and C.B. Kasper (2002). Association of multiple developmental defects and embryonic lethality with loss of microsomal NADPH-cytochrome P450 oxidoreductase. J. Biol. Chem. 277, 6536-6541. [Pg.140]

Shen, A.L. and C.B. Kasper (1996). Role of Ser457 of NADPH-cytochrome P450 oxidoreductase in catalysis and control of FAD oxidation-reduction potential. Biochemistry iS, 9451-9459. [Pg.142]

Yadav, J.S. and J.C. Loper (2000). Cytochrome P450 oxidoreductase gene and its differentially terminated cDNAs from the white-rot fungus... [Pg.614]

THE CYPs CYPs are heme proteins (Figure 3-1). The heme iron binds oxygen in the CYP active site, where oxidation of substrates occurs. Electrons are supplied by the enzyme NADPH-cytochrome P450 oxidoreductase and its cofactor, NADPH. Metabolism of a substrate by a CYP consumes one molecule of and produces an oxidized substrate and a molecule of water. Depending on the nature of the substrate, the reaction for some CYPs is partially uncoupled, consuming more than substrate metabolized and producing activated oxygen or. The is usually converted to water by the enzyme superoxide dismutase. [Pg.45]

Fig. 2.2 Evolutionary origins of the structures of NADPH-cytochrome P450 oxidoreductase POR) and the neuronal NOS (tiNOS) reductase domain cyan), shown by overlays of the ribbon struetures of Desulfovibrto vulgaris flavodoxin (Fid) and spinach ferredoxin-NADP-oxidoreductase FNK). a Structures of Fid and FNR. b POR with flavin mononucleotide FMN) and flavin adenine dinucleotide FAD) highlighted with red sticks. The... Fig. 2.2 Evolutionary origins of the structures of NADPH-cytochrome P450 oxidoreductase POR) and the neuronal NOS (tiNOS) reductase domain cyan), shown by overlays of the ribbon struetures of Desulfovibrto vulgaris flavodoxin (Fid) and spinach ferredoxin-NADP-oxidoreductase FNK). a Structures of Fid and FNR. b POR with flavin mononucleotide FMN) and flavin adenine dinucleotide FAD) highlighted with red sticks. The...
Fig. 2.5 Top panel, a Model of a complex between P450 and NADPH-cytochrome P450 oxidoreductase (FOR). A complex of P450 (red) and Mol A of the hinge-deletion mutant of POR(ATGEE), denoted as PORT e [53]). the flavin mononucleotide (FMN) domain (blue) and flavin adenine dinucleotide (FAD) domain (yellow)] and an enlarged view showing the relative orientation of the EMN and heme, b and c Open-book representation of molecular surface at the interface of P450 (b) and the EMN domain of POR (c). Five salt-bridge pairs are shown with same let-... Fig. 2.5 Top panel, a Model of a complex between P450 and NADPH-cytochrome P450 oxidoreductase (FOR). A complex of P450 (red) and Mol A of the hinge-deletion mutant of POR(ATGEE), denoted as PORT e [53]). the flavin mononucleotide (FMN) domain (blue) and flavin adenine dinucleotide (FAD) domain (yellow)] and an enlarged view showing the relative orientation of the EMN and heme, b and c Open-book representation of molecular surface at the interface of P450 (b) and the EMN domain of POR (c). Five salt-bridge pairs are shown with same let-...

See other pages where Cytochrome P450 oxidoreductase is mentioned: [Pg.461]    [Pg.462]    [Pg.191]    [Pg.173]    [Pg.114]    [Pg.98]    [Pg.140]    [Pg.141]    [Pg.373]    [Pg.557]    [Pg.562]    [Pg.563]    [Pg.44]    [Pg.847]    [Pg.472]    [Pg.622]    [Pg.33]    [Pg.33]    [Pg.34]    [Pg.35]    [Pg.37]    [Pg.37]    [Pg.45]   
See also in sourсe #XX -- [ Pg.472 ]




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Cytochrome P450

Cytochrome P450 oxidoreductase (POR

Cytochrome P450s

Oxidoreductase

Oxidoreductases cytochromes

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