메뉴 건너뛰기




Volumn 398, Issue 2, 2010, Pages 194-198

Functional reconstitution of monomeric CYP3A4 with multiple cytochrome P450 reductase molecules in Nanodiscs

Author keywords

Cytochrome P450; Nanodisc; P450 reductase

Indexed keywords

CYTOCHROME P450 3A4; CYTOCHROME P450 REDUCTASE; MONOMER; NANODISC; OLEOYLPALMITOYLLECITHIN; PHOSPHATIDYLCHOLINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TESTOSTERONE; UNCLASSIFIED DRUG;

EID: 77955056487     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.06.058     Document Type: Article
Times cited : (36)

References (29)
  • 1
    • 33846473252 scopus 로고    scopus 로고
    • Cytochrome P450 systems-biological variations of electron transport chains
    • Hannemann F., Bichet A., Ewen K.M., Bernhardt R. Cytochrome P450 systems-biological variations of electron transport chains. Biochim. Biophys. Acta 2007, 1770:330-344.
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 330-344
    • Hannemann, F.1    Bichet, A.2    Ewen, K.M.3    Bernhardt, R.4
  • 3
    • 0031543466 scopus 로고    scopus 로고
    • Reconstitution premixes for assays using purified recombinant human cytochrome P450, NADPH-cytochrome P450 reductase, and cytochrome b5
    • Shaw P.M., Hosea N.A., Thompson D.V., Lenius J.M., Guengerich F.P. Reconstitution premixes for assays using purified recombinant human cytochrome P450, NADPH-cytochrome P450 reductase, and cytochrome b5. Arch. Biochem. Biophys. 1997, 348:107-115.
    • (1997) Arch. Biochem. Biophys. , vol.348 , pp. 107-115
    • Shaw, P.M.1    Hosea, N.A.2    Thompson, D.V.3    Lenius, J.M.4    Guengerich, F.P.5
  • 5
    • 33645101080 scopus 로고    scopus 로고
    • An evaluation of methods for the reconstitution of cytochromes P450 and NADPH P450 reductase into lipid vesicles
    • Reed J.R., Kelley R.W., Backes W.L. An evaluation of methods for the reconstitution of cytochromes P450 and NADPH P450 reductase into lipid vesicles. Drug Metab. Dispos. 2006, 34:660-666.
    • (2006) Drug Metab. Dispos. , vol.34 , pp. 660-666
    • Reed, J.R.1    Kelley, R.W.2    Backes, W.L.3
  • 7
    • 27144459868 scopus 로고    scopus 로고
    • Kinetics of dithionite-dependent reduction of cytochrome P450 3A4: heterogeneity of the enzyme caused by its oligomerization
    • Davydov D.R., Fernando H., Baas B.J., Sligar S.G., Halpert J.R. Kinetics of dithionite-dependent reduction of cytochrome P450 3A4: heterogeneity of the enzyme caused by its oligomerization. Biochemistry 2005, 44:13902-13913.
    • (2005) Biochemistry , vol.44 , pp. 13902-13913
    • Davydov, D.R.1    Fernando, H.2    Baas, B.J.3    Sligar, S.G.4    Halpert, J.R.5
  • 8
    • 75649112318 scopus 로고    scopus 로고
    • Electron transfer in the complex of membrane-bound human cytochrome P450 3A4 with the flavin domain of P450BM-3: the effect of oligomerization of the heme protein and intermittent modulation of the spin equilibrium
    • Davydov D.R., Sineva E.V., Sistla S., Davydova N.Y., Frank D.J., Sligar S.G., Halpert J.R. Electron transfer in the complex of membrane-bound human cytochrome P450 3A4 with the flavin domain of P450BM-3: the effect of oligomerization of the heme protein and intermittent modulation of the spin equilibrium. Biochim. Biophys. Acta 2010, 1797:378-390.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 378-390
    • Davydov, D.R.1    Sineva, E.V.2    Sistla, S.3    Davydova, N.Y.4    Frank, D.J.5    Sligar, S.G.6    Halpert, J.R.7
  • 10
    • 77951903021 scopus 로고    scopus 로고
    • Membrane protein assembly into Nanodiscs
    • Bayburt T.H., Sligar S.G. Membrane protein assembly into Nanodiscs. FEBS Lett. 2010, 584:1721-1727.
    • (2010) FEBS Lett. , vol.584 , pp. 1721-1727
    • Bayburt, T.H.1    Sligar, S.G.2
  • 12
    • 34147112191 scopus 로고    scopus 로고
    • Cooperativity in cytochrome P450 3A4: linkages in substrate binding, spin state, uncoupling, and product formation
    • Denisov I.G., Baas B.J., Grinkova Y.V., Sligar S.G. Cooperativity in cytochrome P450 3A4: linkages in substrate binding, spin state, uncoupling, and product formation. J. Biol. Chem. 2007, 282:7066-7076.
    • (2007) J. Biol. Chem. , vol.282 , pp. 7066-7076
    • Denisov, I.G.1    Baas, B.J.2    Grinkova, Y.V.3    Sligar, S.G.4
  • 13
    • 35448960897 scopus 로고    scopus 로고
    • Obligatory intermolecular electron-transfer from FAD to FMN in dimeric P450BM-3
    • Kitazume T., Haines D.C., Estabrook R.W., Chen B., Peterson J.A. Obligatory intermolecular electron-transfer from FAD to FMN in dimeric P450BM-3. Biochemistry 2007, 46:11892-11901.
    • (2007) Biochemistry , vol.46 , pp. 11892-11901
    • Kitazume, T.1    Haines, D.C.2    Estabrook, R.W.3    Chen, B.4    Peterson, J.A.5
  • 14
    • 66449111327 scopus 로고    scopus 로고
    • Structure and function of an NADPH-cytochrome P450 oxidoreductase in an open conformation capable of reducing cytochrome P450
    • Hamdane D., Xia C., Im S.C., Zhang H., Kim J.J., Waskell L. Structure and function of an NADPH-cytochrome P450 oxidoreductase in an open conformation capable of reducing cytochrome P450. J. Biol. Chem. 2009, 284:11374-11384.
    • (2009) J. Biol. Chem. , vol.284 , pp. 11374-11384
    • Hamdane, D.1    Xia, C.2    Im, S.C.3    Zhang, H.4    Kim, J.J.5    Waskell, L.6
  • 15
    • 1642382983 scopus 로고    scopus 로고
    • Directed self-assembly of monodisperse phospholipid bilayer Nanodiscs with controlled size
    • Denisov I.G., Grinkova Y.V., Lazarides A.A., Sligar S.G. Directed self-assembly of monodisperse phospholipid bilayer Nanodiscs with controlled size. J. Am. Chem. Soc. 2004, 126:3477-3487.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3477-3487
    • Denisov, I.G.1    Grinkova, Y.V.2    Lazarides, A.A.3    Sligar, S.G.4
  • 16
    • 4444297536 scopus 로고    scopus 로고
    • Homotropic cooperativity of monomeric cytochrome P450 3A4 in a nanoscale native bilayer environment
    • Baas B.J., Denisov I.G., Sligar S.G. Homotropic cooperativity of monomeric cytochrome P450 3A4 in a nanoscale native bilayer environment. Arch. Biochem. Biophys. 2004, 430:218-228.
    • (2004) Arch. Biochem. Biophys. , vol.430 , pp. 218-228
    • Baas, B.J.1    Denisov, I.G.2    Sligar, S.G.3
  • 17
    • 0027223881 scopus 로고
    • Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme
    • Gillam E.M., Baba T., Kim B.R., Ohmori S., Guengerich F.P. Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme. Arch. Biochem. Biophys. 1993, 305:123-131.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 123-131
    • Gillam, E.M.1    Baba, T.2    Kim, B.R.3    Ohmori, S.4    Guengerich, F.P.5
  • 18
    • 33747736671 scopus 로고    scopus 로고
    • The ferrous-dioxygen intermediate in human cytochrome P450 3A4: substrate dependence of formation of decay kinetics
    • Denisov I.G., Grinkova Y.V., Baas B.J., Sligar S.G. The ferrous-dioxygen intermediate in human cytochrome P450 3A4: substrate dependence of formation of decay kinetics. J. Biol. Chem. 2006, 281:23313-23318.
    • (2006) J. Biol. Chem. , vol.281 , pp. 23313-23318
    • Denisov, I.G.1    Grinkova, Y.V.2    Baas, B.J.3    Sligar, S.G.4
  • 20
    • 0019321102 scopus 로고
    • Interactions of cytochrome P-450, NADPH-cytochrome P-450 reductase, phospholipid, and substrate in the reconstituted liver microsomal enzyme system
    • French J.S., Guengerich F.P., Coon M.J. Interactions of cytochrome P-450, NADPH-cytochrome P-450 reductase, phospholipid, and substrate in the reconstituted liver microsomal enzyme system. J. Biol. Chem. 1980, 255:4112-4119.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4112-4119
    • French, J.S.1    Guengerich, F.P.2    Coon, M.J.3
  • 21
    • 0018802951 scopus 로고
    • Hydrodynamic characterization of highly purified and functionally active liver microsomal cytochrome P-450
    • Guengerich F.P., Holladay L.A. Hydrodynamic characterization of highly purified and functionally active liver microsomal cytochrome P-450. Biochemistry 1979, 18:5442-5449.
    • (1979) Biochemistry , vol.18 , pp. 5442-5449
    • Guengerich, F.P.1    Holladay, L.A.2
  • 22
    • 0017894518 scopus 로고
    • Studies on the rate-limiting enzyme component in the microsomal monooxygenase system. Incorporation of purified NADPH-cytochrome c reductase and cytochrome P-450 into rat liver microsomes
    • Miwa G.T., West S.B., Lu A.Y. Studies on the rate-limiting enzyme component in the microsomal monooxygenase system. Incorporation of purified NADPH-cytochrome c reductase and cytochrome P-450 into rat liver microsomes. J. Biol. Chem. 1978, 253:1921-1929.
    • (1978) J. Biol. Chem. , vol.253 , pp. 1921-1929
    • Miwa, G.T.1    West, S.B.2    Lu, A.Y.3
  • 23
  • 24
    • 0017801794 scopus 로고
    • Purified liver microsomal NADPH-cytochrome P-450 reductase. Spectral characterization of oxidation-reduction states
    • Vermilion J.L., Coon M.J. Purified liver microsomal NADPH-cytochrome P-450 reductase. Spectral characterization of oxidation-reduction states. J. Biol. Chem. 1978, 253:2694-2704.
    • (1978) J. Biol. Chem. , vol.253 , pp. 2694-2704
    • Vermilion, J.L.1    Coon, M.J.2
  • 25
    • 12844261851 scopus 로고    scopus 로고
    • Interactions of mammalian cytochrome P450, NADPH-cytochrome P450 reductase, and cytochrome b(5) enzymes
    • Shimada T., Mernaugh R.L., Guengerich F.P. Interactions of mammalian cytochrome P450, NADPH-cytochrome P450 reductase, and cytochrome b(5) enzymes. Arch. Biochem. Biophys. 2005, 435:207-216.
    • (2005) Arch. Biochem. Biophys. , vol.435 , pp. 207-216
    • Shimada, T.1    Mernaugh, R.L.2    Guengerich, F.P.3
  • 26
    • 0021707118 scopus 로고
    • The association of cytochrome P-450 and NADPH-cytochrome P-450 reductase in phospholipid membranes
    • Miwa G.T., Lu A.Y. The association of cytochrome P-450 and NADPH-cytochrome P-450 reductase in phospholipid membranes. Arch. Biochem. Biophys. 1984, 234:161-166.
    • (1984) Arch. Biochem. Biophys. , vol.234 , pp. 161-166
    • Miwa, G.T.1    Lu, A.Y.2
  • 27
    • 73649109571 scopus 로고    scopus 로고
    • Domain motion in cytochrome P 450 reductase: conformational equilibria revealed by NMR and small-angle X-ray scattering
    • Ellis J., Gutierrez A., Barsukov I.L., Huang W.-C., Grossmann J.G., Roberts G.C.K. Domain motion in cytochrome P 450 reductase: conformational equilibria revealed by NMR and small-angle X-ray scattering. J. Biol. Chem. 2009, 284:36628-36637.
    • (2009) J. Biol. Chem. , vol.284 , pp. 36628-36637
    • Ellis, J.1    Gutierrez, A.2    Barsukov, I.L.3    Huang, W.-C.4    Grossmann, J.G.5    Roberts, G.C.K.6
  • 28
    • 26844498754 scopus 로고    scopus 로고
    • The dimeric form of flavocytochrome P450 BM3 is catalytically functional as a fatty acid hydroxylase
    • Neeli R., Girvan H.M., Lawrence A., Warren M.J., Leys D., Scrutton N.S., Munro A.W. The dimeric form of flavocytochrome P450 BM3 is catalytically functional as a fatty acid hydroxylase. FEBS Lett. 2005, 579:5582-5588.
    • (2005) FEBS Lett. , vol.579 , pp. 5582-5588
    • Neeli, R.1    Girvan, H.M.2    Lawrence, A.3    Warren, M.J.4    Leys, D.5    Scrutton, N.S.6    Munro, A.W.7
  • 29
    • 0029012009 scopus 로고
    • CYP3A4 expressed by insect cells infected with a recombinant baculovirus containing both CYP3A4 and human NADPH-cytochrome P450 reductase is catalytically similar to human liver microsomal CYP3A4
    • Lee C.A., Kadwell S.H., Kost T.A., Serabjit-Singh C.J. CYP3A4 expressed by insect cells infected with a recombinant baculovirus containing both CYP3A4 and human NADPH-cytochrome P450 reductase is catalytically similar to human liver microsomal CYP3A4. Arch. Biochem. Biophys. 1995, 319:157-167.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 157-167
    • Lee, C.A.1    Kadwell, S.H.2    Kost, T.A.3    Serabjit-Singh, C.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.