메뉴 건너뛰기




Volumn 5, Issue 8, 2010, Pages 767-776

FMN binding site of yeast NADPH-cytochrome P450 reductase exposed at the surface is highly specific

Author keywords

[No Author keywords available]

Indexed keywords

ALLOXAZINE; CYTOCHROME P450 REDUCTASE; DIMETHYLALLOXAZINE; FLAVINE ADENINE NUCLEOTIDE; FLAVINE MONONUCLEOTIDE; FLAVINE NUCLEOTIDE; GLYCEROPHOSPHATE; PHOSPHATE; PYROPHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RIBOFLAVIN; UNCLASSIFIED DRUG;

EID: 77955905534     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb100055v     Document Type: Article
Times cited : (8)

References (43)
  • 1
    • 0034652257 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and enzymological characterization of human squalene monooxygenase
    • Laden, B. P., Tang, Y., and Porter, T. D. (2000) Cloning, heterologous expression, and enzymological characterization of human squalene monooxygenase Arch. Biochem. Biophys. 374, 381-388
    • (2000) Arch. Biochem. Biophys. , vol.374 , pp. 381-388
    • Laden, B.P.1    Tang, Y.2    Porter, T.D.3
  • 2
    • 0016641043 scopus 로고
    • Solubilization and partial characterization of rat liver squalene epoxidase
    • Ono, T. and Bloch, K. (1975) Solubilization and partial characterization of rat liver squalene epoxidase J. Biol. Chem. 250, 1571-1579
    • (1975) J. Biol. Chem. , vol.250 , pp. 1571-1579
    • Ono, T.1    Bloch, K.2
  • 3
    • 0015501157 scopus 로고
    • Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system
    • Schacter, B. A., Nelson, E. B., Marver, H. S., and Masters, B. S. S. (1972) Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system J. Biol. Chem. 247, 3601-3607
    • (1972) J. Biol. Chem. , vol.247 , pp. 3601-3607
    • Schacter, B.A.1    Nelson, E.B.2    Marver, H.S.3    Masters, B.S.S.4
  • 4
    • 0019877474 scopus 로고
    • Evidence for a new physiological role of hepatic NADPH:ferricytochrome (P-450) oxidoreductase. Direct electron input to the microsomal fatty acid chain elongation system
    • Ilan, Z., Ilan, R., and Cinti, D. L. (1981) Evidence for a new physiological role of hepatic NADPH:ferricytochrome (P-450) oxidoreductase. Direct electron input to the microsomal fatty acid chain elongation system J. Biol. Chem. 256, 10066-10072
    • (1981) J. Biol. Chem. , vol.256 , pp. 10066-10072
    • Ilan, Z.1    Ilan, R.2    Cinti, D.L.3
  • 5
    • 0018801347 scopus 로고
    • 5 reduction by NADPH-cytochrome P-450 reductase
    • 5 reduction by NADPH-cytochrome P-450 reductase J. Biol. Chem. 254, 8976-8981
    • (1979) J. Biol. Chem. , vol.254 , pp. 8976-8981
    • Enoch, H.G.1    Strittmatter, P.2
  • 6
    • 0022878676 scopus 로고
    • Characterization of a catalytically self-sufficient 119,000-dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium
    • Narhi, L. O. and Fulco, A. J. (1986) Characterization of a catalytically self-sufficient 119,000-dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium J. Biol. Chem. 261, 7160-7169
    • (1986) J. Biol. Chem. , vol.261 , pp. 7160-7169
    • Narhi, L.O.1    Fulco, A.J.2
  • 7
    • 2442552990 scopus 로고    scopus 로고
    • Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: Flavocytochrome homologues of P450 BM3 from Bacillus megaterium
    • Gustafsson, M. C. U., Roitel, O., Marshall, K. R., Noble, M. A., Chapman, S. K., Pessegueiro, A., Fulco, A. J., Cheesman, M. R., Wachenfeldt, C., and Munro, A. W. (2004) Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium Biochemistry 43, 5474-5487
    • (2004) Biochemistry , vol.43 , pp. 5474-5487
    • Gustafsson, M.C.U.1    Roitel, O.2    Marshall, K.R.3    Noble, M.A.4    Chapman, S.K.5    Pessegueiro, A.6    Fulco, A.J.7    Cheesman, M.R.8    Wachenfeldt, C.9    Munro, A.W.10
  • 8
    • 0034671918 scopus 로고    scopus 로고
    • Fusarium oxysporum fatty-acid subterminal hydroxylase (CYP505) is a membrane-bound eukaryotic counterpart of Bacillus megaterium cytochrome P450BM3
    • Kitazume, T., Takaya, N., Nakayama, N., and Shoun, H. (2000) Fusarium oxysporum fatty-acid subterminal hydroxylase (CYP505) is a membrane-bound eukaryotic counterpart of Bacillus megaterium cytochrome P450BM3 J. Biol. Chem. 275, 39734-39740
    • (2000) J. Biol. Chem. , vol.275 , pp. 39734-39740
    • Kitazume, T.1    Takaya, N.2    Nakayama, N.3    Shoun, H.4
  • 9
    • 0025802065 scopus 로고
    • Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase
    • Bredt, D. S., Hwang, P. M., Glatt, C. E., Lowenstein, C., Reed, R. R., and Snyder, S. H. (1991) Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase Nature 351, 714-718
    • (1991) Nature , vol.351 , pp. 714-718
    • Bredt, D.S.1    Hwang, P.M.2    Glatt, C.E.3    Lowenstein, C.4    Reed, R.R.5    Snyder, S.H.6
  • 12
    • 0024462430 scopus 로고
    • Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase
    • Ostrowski, J., Barber, M. J., Rueger, D. C., Miller, B. E., Siegel, L. M., and Kredich, N. M. (1989) Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase J. Biol. Chem. 264, 15796-15808
    • (1989) J. Biol. Chem. , vol.264 , pp. 15796-15808
    • Ostrowski, J.1    Barber, M.J.2    Rueger, D.C.3    Miller, B.E.4    Siegel, L.M.5    Kredich, N.M.6
  • 14
    • 27544432713 scopus 로고    scopus 로고
    • Structure and function of NADPH-cytochrome P450 reductase and nitric oxide synthase reductase domain
    • DOI 10.1016/j.bbrc.2005.08.043, PII S0006291X05017134
    • Iyanagi, T. (2005) Structure and function of NADPH-cytochrome P450 reductase and nitric oxide synthase reductase domain Biochem. Biophys. Res. Commun. 338, 520-528 (Pubitemid 41540598)
    • (2005) Biochemical and Biophysical Research Communications , vol.338 , Issue.1 , pp. 520-528
    • Iyanagi, T.1
  • 15
    • 27544462706 scopus 로고    scopus 로고
    • The journey from NADPH-cytochrome P450 oxidoreductase to nitric oxide synthases
    • Masters, B. S. (2005) The journey from NADPH-cytochrome P450 oxidoreductase to nitric oxide synthases Biochem. Biophys. Res. Commun. 338, 507-519
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 507-519
    • Masters, B.S.1
  • 17
    • 67650096940 scopus 로고    scopus 로고
    • Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase
    • Aigrain, L., Pompon, D., Morera, S., and Truan, G. (2009) Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase EMBO Rep 10, 742-747
    • (2009) EMBO Rep , vol.10 , pp. 742-747
    • Aigrain, L.1    Pompon, D.2    Morera, S.3    Truan, G.4
  • 18
    • 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., and Waskell, L. (2009) Structure and function of an NADPH-cytochrome P450 oxidoreductase in an open conformation capable of reducing cytochrome P450 J. Biol. Chem. 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
  • 19
    • 73649109571 scopus 로고    scopus 로고
    • Domain motion in cytochrome P450 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., and Roberts, G. C. (2009) Domain motion in cytochrome P450 reductase: conformational equilibria revealed by NMR and small-angle x-ray scattering J. Biol. Chem. 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.6
  • 20
    • 33644795666 scopus 로고    scopus 로고
    • A second FMN binding site in yeast NADPH-cytochrome P450 reductase suggests a mechanism of electron transfer by diflavin reductases
    • Lamb, D. C., Kim, Y., Yermalitskaya, L. V., Yermalitsky, V. N., Lepesheva, G. I., Kelly, S. L., Waterman, M. R., and Podust, L. M. (2006) A second FMN binding site in yeast NADPH-cytochrome P450 reductase suggests a mechanism of electron transfer by diflavin reductases Structure 14, 51-61
    • (2006) Structure , vol.14 , pp. 51-61
    • Lamb, D.C.1    Kim, Y.2    Yermalitskaya, L.V.3    Yermalitsky, V.N.4    Lepesheva, G.I.5    Kelly, S.L.6    Waterman, M.R.7    Podust, L.M.8
  • 21
    • 0030873316 scopus 로고    scopus 로고
    • Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes
    • Wang, M., Roberts, D. L., Paschke, R., Shea, T. M., Masters, B. S., and Kim, J. J. (1997) Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes Proc. Natl. Acad. Sci. U.S.A. 94, 8411-8416
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 8411-8416
    • Wang, M.1    Roberts, D.L.2    Paschke, R.3    Shea, T.M.4    Masters, B.S.5    Kim, J.J.6
  • 22
    • 0023028914 scopus 로고
    • Localization of cytochrome c -binding domain on NADPH-cytochrome P-450 reductase
    • Nisimoto, Y. (1986) Localization of cytochrome c -binding domain on NADPH-cytochrome P-450 reductase J. Biol. Chem. 261, 14232-14239
    • (1986) J. Biol. Chem. , vol.261 , pp. 14232-14239
    • Nisimoto, Y.1
  • 23
    • 0023821815 scopus 로고
    • 5, cytochrome c, and cytochrome P-450 interactions with NADPH-cytochrome P-450 reductase in phospholipid vesicles
    • 5, cytochrome c, and cytochrome P-450 interactions with NADPH-cytochrome P-450 reductase in phospholipid vesicles Biochemistry 27, 5869-5876
    • (1988) Biochemistry , vol.27 , pp. 5869-5876
    • Nisimoto, Y.1    Otsuka-Murakami, H.2
  • 24
    • 0028805425 scopus 로고
    • Role of acidic residues in the interaction of NADPH-cytochrome P450 oxidoreductase with cytochrome P450 and cytochrome c
    • Shen, A. L. and Kasper, C. B. (1995) Role of acidic residues in the interaction of NADPH-cytochrome P450 oxidoreductase with cytochrome P450 and cytochrome c J. Biol. Chem. 270, 27475-27480
    • (1995) J. Biol. Chem. , vol.270 , pp. 27475-27480
    • Shen, A.L.1    Kasper, C.B.2
  • 25
    • 0035800760 scopus 로고    scopus 로고
    • NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer
    • Hubbard, P. A., Shen, A. L., Paschke, R., Kasper, C. B., and Kim, J. J. (2001) NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer J. Biol. Chem. 276, 29163-29170
    • (2001) J. Biol. Chem. , vol.276 , pp. 29163-29170
    • Hubbard, P.A.1    Shen, A.L.2    Paschke, R.3    Kasper, C.B.4    Kim, J.J.5
  • 26
    • 0017801794 scopus 로고
    • Purified liver microsomal NADPH-cytochrome P-450 reductase. Spectral characterization of oxidation-reduction states
    • Vermilion, J. L. and Coon, M. J. (1978) Purified liver microsomal NADPH-cytochrome P-450 reductase. Spectral characterization of oxidation-reduction states J. Biol. Chem. 253, 2694-2704
    • (1978) J. Biol. Chem. , vol.253 , pp. 2694-2704
    • Vermilion, J.L.1    Coon, M.J.2
  • 27
    • 0037518367 scopus 로고    scopus 로고
    • Purification and characterization of a soluble form of rat liver NADPH-cytochrome P-450 reductase highly expressed in Escherichia coli
    • Hayashi, S., Omata, Y., Sakamoto, H., Hara, T., and Noguchi, M. (2003) Purification and characterization of a soluble form of rat liver NADPH-cytochrome P-450 reductase highly expressed in Escherichia coli Protein Expression Purif. 29, 1-7
    • (2003) Protein Expression Purif. , vol.29 , pp. 1-7
    • Hayashi, S.1    Omata, Y.2    Sakamoto, H.3    Hara, T.4    Noguchi, M.5
  • 28
    • 0020479810 scopus 로고
    • Studies on FAD- and FMN-binding domains in NADPH-cytochrome P-450 reductase from rabbit liver microsomes
    • Nisimoto, Y. and Shibata, Y. (1982) Studies on FAD- and FMN-binding domains in NADPH-cytochrome P-450 reductase from rabbit liver microsomes J. Biol. Chem. 257, 12532-12539
    • (1982) J. Biol. Chem. , vol.257 , pp. 12532-12539
    • Nisimoto, Y.1    Shibata, Y.2
  • 29
    • 0018220868 scopus 로고
    • Identification of the high and low potential flavins of liver microsomal NADPH-cytochrome P-450 reductase
    • Vermilion, J. L. and Coon, M. J. (1978) Identification of the high and low potential flavins of liver microsomal NADPH-cytochrome P-450 reductase J. Biol. Chem. 253, 8812-8819
    • (1978) J. Biol. Chem. , vol.253 , pp. 8812-8819
    • Vermilion, J.L.1    Coon, M.J.2
  • 30
    • 0033955735 scopus 로고    scopus 로고
    • Advances in surface plasmon resonance biosensor analysis
    • Rich, R. L. and Myszka, D. G. (2000) Advances in surface plasmon resonance biosensor analysis Curr. Opin. Biotechnol. 11, 54-61
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 54-61
    • Rich, R.L.1    Myszka, D.G.2
  • 31
    • 0019876543 scopus 로고
    • Separate roles for FMN and FAD in catalysis by liver microsomal NADPH-cytochrome P-450 reductase
    • Vermilion, J. L., Ballou, D. P., Massey, V., and Coon, M. J. (1981) Separate roles for FMN and FAD in catalysis by liver microsomal NADPH-cytochrome P-450 reductase J. Biol. Chem. 256, 266-277
    • (1981) J. Biol. Chem. , vol.256 , pp. 266-277
    • Vermilion, J.L.1    Ballou, D.P.2    Massey, V.3    Coon, M.J.4
  • 32
    • 0035692604 scopus 로고    scopus 로고
    • NADPH-induced oxidative damage of rat liver microsomes: Protective role of chlorpromazine and trifluoperazine
    • Khatua, A. K. and Bhattacharyya, M. (2001) NADPH-induced oxidative damage of rat liver microsomes: protective role of chlorpromazine and trifluoperazine Pol. J. Pharmacol. 53, 629-634
    • (2001) Pol. J. Pharmacol. , vol.53 , pp. 629-634
    • Khatua, A.K.1    Bhattacharyya, M.2
  • 33
    • 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., and Coon, M. J. (1980) Interactions of cytochrome P-450, NADPH-cytochrome P-450 reductase, phospholipid, and substrate in the reconstituted liver microsomal enzyme system J. Biol. Chem. 255, 4112-4119
    • (1980) J. Biol. Chem. , vol.255 , pp. 4112-4119
    • French, J.S.1    Guengerich, F.P.2    Coon, M.J.3
  • 34
    • 0025700702 scopus 로고
    • 31P-nuclear-magnetic-resonance study of NADPH-cytochrome-P- 450 reductase and of the Azotobacter flavodoxin/ferredoxin-NADP+ reductase complex
    • 31P-nuclear-magnetic-resonance study of NADPH-cytochrome-P-450 reductase and of the Azotobacter flavodoxin/ferredoxin-NADP+ reductase complex Eur. J. Biochem. 190, 531-537
    • (1990) Eur. J. Biochem. , vol.190 , pp. 531-537
    • Bonants, P.J.1    Muller, F.2    Vervoort, J.3    Edmondson, D.E.4
  • 36
    • 0027131321 scopus 로고
    • A specific interaction between NADPH-cytochrome reductase and phosphatidylserine and phosphatidylinositol
    • Balvers, W. G., Boersma, M. G., Vervoort, J., Ouwehand, A., and Rietjens, I. M. (1993) A specific interaction between NADPH-cytochrome reductase and phosphatidylserine and phosphatidylinositol Eur. J. Biochem. 218, 1021-1029
    • (1993) Eur. J. Biochem. , vol.218 , pp. 1021-1029
    • Balvers, W.G.1    Boersma, M.G.2    Vervoort, J.3    Ouwehand, A.4    Rietjens, I.M.5
  • 37
    • 0021254565 scopus 로고
    • Interaction of liver microsomal cytochrome P-450 and NADPH-cytochrome P-450 reductase in the presence and absence of lipid
    • Muller-Enoch, D., Churchill, P., Fleischer, S., and Guengerich, F. P. (1984) Interaction of liver microsomal cytochrome P-450 and NADPH-cytochrome P-450 reductase in the presence and absence of lipid J. Biol. Chem. 259, 8174-8182
    • (1984) J. Biol. Chem. , vol.259 , pp. 8174-8182
    • Muller-Enoch, D.1    Churchill, P.2    Fleischer, S.3    Guengerich, F.P.4
  • 38
    • 2342417946 scopus 로고    scopus 로고
    • Intracellular phosphate serves as a signal for the regulation of the PHO pathway in Saccharomyces cerevisiae
    • Auesukaree, C., Homma, T., Tochio, H., Shirakawa, M., Kaneko, Y., and Harashima, S. (2004) Intracellular phosphate serves as a signal for the regulation of the PHO pathway in Saccharomyces cerevisiae J. Biol. Chem. 279, 17289-17294
    • (2004) J. Biol. Chem. , vol.279 , pp. 17289-17294
    • Auesukaree, C.1    Homma, T.2    Tochio, H.3    Shirakawa, M.4    Kaneko, Y.5    Harashima, S.6
  • 39
    • 9744270010 scopus 로고    scopus 로고
    • Protein dynamics and electrostatics in the function of p -hydroxybenzoate hydroxylase
    • Entsch, B., Cole, L. J., and Ballou, D. P. (2005) Protein dynamics and electrostatics in the function of p -hydroxybenzoate hydroxylase Arch. Biochem. Biophys. 433, 297-311
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 297-311
    • Entsch, B.1    Cole, L.J.2    Ballou, D.P.3
  • 41
    • 0032548924 scopus 로고    scopus 로고
    • The N-terminal membrane domain of yeast NADPH-cytochrome P450 (CYP) oxidoreductase is not required for catalytic activity in sterol biosynthesis or in reconstitution of CYP activity
    • Venkateswarlu, K., Lamb, D. C., Kelly, D. E., Manning, N. J., and Kelly, S. L. (1998) The N-terminal membrane domain of yeast NADPH-cytochrome P450 (CYP) oxidoreductase is not required for catalytic activity in sterol biosynthesis or in reconstitution of CYP activity J. Biol. Chem. 273, 4492-6
    • (1998) J. Biol. Chem. , vol.273 , pp. 4492-6
    • Venkateswarlu, K.1    Lamb, D.C.2    Kelly, D.E.3    Manning, N.J.4    Kelly, S.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.