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Volumn 258, Issue 3, 1998, Pages 1040-1049

Differential redox and electron-transfer properties of purified yeast, plant and human NADPH-cytochrome P-450 reductases highly modulate cytochrome P-450 activities

Author keywords

Kinetic property; NADPH cytochrome P 450 reductase; P 450 interaction; Redox potential

Indexed keywords

CYTOCHROME P450; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE;

EID: 0344573107     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2581040.x     Document Type: Article
Times cited : (27)

References (71)
  • 1
    • 0018730079 scopus 로고
    • Multiplicity of mammalian microsomal cytochromes P-450
    • Lu, A. Y. & West, S. B. (1979) Multiplicity of mammalian microsomal cytochromes P-450. Pharmacol. Rev. 31, 277-295.
    • (1979) Pharmacol. Rev. , vol.31 , pp. 277-295
    • Lu, A.Y.1    West, S.B.2
  • 2
    • 0018820633 scopus 로고
    • NADPH cytochrome P-450 reductase and its role in the mixed function oxidase reaction
    • Strobel, H. W., Dignam, J. D. & Gum, J. R. (1980) NADPH cytochrome P-450 reductase and its role in the mixed function oxidase reaction, Pharmacol Ther. 8, 525-537.
    • (1980) Pharmacol Ther. , vol.8 , pp. 525-537
    • Strobel, H.W.1    Dignam, J.D.2    Gum, J.R.3
  • 3
    • 73649173283 scopus 로고
    • Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver
    • Williams, C. H. & Kamin, H. (1962) Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver, J. Biol. Chem. 237, 587-595.
    • (1962) J. Biol. Chem. , vol.237 , pp. 587-595
    • Williams, C.H.1    Kamin, H.2
  • 4
    • 73849173955 scopus 로고
    • Hepatic triphosphopyridine nucleotide cytochrome c reductase: Isolation, characterization and kinetic studies
    • Phillips, A. H. & Langdon, R. G. (1962) Hepatic triphosphopyridine nucleotide cytochrome c reductase: isolation, characterization and kinetic studies, J. Biol. Chem. 237, 2652-2660.
    • (1962) J. Biol. Chem. , vol.237 , pp. 2652-2660
    • Phillips, A.H.1    Langdon, R.G.2
  • 5
    • 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. & Masters, B. 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.4
  • 6
    • 0018801347 scopus 로고
    • Cytochrome b5 reduction by NADPH-cytochrome P-450 reductase
    • Enoch, H. G. & Strittmatter, P. (1979) Cytochrome b5 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
  • 8
    • 0027954308 scopus 로고
    • Catalytic selectivity of human cytochrome P450 enzymes: Relevance to drug metabolism and toxicity
    • Guengerich, F. P. (1994) Catalytic selectivity of human cytochrome P450 enzymes: relevance to drug metabolism and toxicity, Toxicol. Lett. 70, 133-138.
    • (1994) Toxicol. Lett. , vol.70 , pp. 133-138
    • Guengerich, F.P.1
  • 9
    • 0025081393 scopus 로고
    • NADPH-cytochrome P-450 oxidoreductase gene organization correlates with structural domains of the protein
    • Porter, T. D., Beck, T. W. & Kasper, C. B. (1990) NADPH-cytochrome P-450 oxidoreductase gene organization correlates with structural domains of the protein, Biochemistry 29, 9814-9818.
    • (1990) Biochemistry , vol.29 , pp. 9814-9818
    • Porter, T.D.1    Beck, T.W.2    Kasper, C.B.3
  • 10
    • 0021956406 scopus 로고
    • Chromosomal assignments of genes coding for components of the mixed-function oxidase system in mice. Genetic localization of the cytochrome P-450PCN and P-450PB gene families and the nadph-cytochrome P-450 oxidoreductase and epoxide hydratase genes
    • Simmons, D. L., Lalley, P. A. & Kasper, C. B. (1985) Chromosomal assignments of genes coding for components of the mixed-function oxidase system in mice. Genetic localization of the cytochrome P-450PCN and P-450PB gene families and the nadph-cytochrome P-450 oxidoreductase and epoxide hydratase genes, J. Biol. Chem. 260, 515-521.
    • (1985) J. Biol. Chem. , vol.260 , pp. 515-521
    • Simmons, D.L.1    Lalley, P.A.2    Kasper, C.B.3
  • 11
    • 0000593265 scopus 로고
    • Purification and properties of sweet potato NADPH-cytochrome c(P450) reductase
    • Fujita, M. & Asahi, T. (1985) Purification and properties of sweet potato NADPH-cytochrome c(P450) reductase, Plant Cell Physiol. 26, 397-405.
    • (1985) Plant Cell Physiol. , vol.26 , pp. 397-405
    • Fujita, M.1    Asahi, T.2
  • 13
    • 0029186729 scopus 로고
    • Two messenger RNAs are encoding for NADPH-cytochrome P450 reductase in Helianthus tuberosus tubes tissues
    • Lesot, A., Hasenfratz, M. P., Batard, Y., Durst, F. & Benveniste, I. (1995) Two messenger RNAs are encoding for NADPH-cytochrome P450 reductase in Helianthus tuberosus tubes tissues, Plant Physiol. Biochem. 33, 751-757.
    • (1995) Plant Physiol. Biochem. , vol.33 , pp. 751-757
    • Lesot, A.1    Hasenfratz, M.P.2    Batard, Y.3    Durst, F.4    Benveniste, I.5
  • 14
    • 0031464795 scopus 로고    scopus 로고
    • Differentially regulated NADPH:Cytochrome P450 oxidoreductases in parsley
    • Koopmann, E. & Hahlbrock, K. (1997) Differentially regulated NADPH:cytochrome P450 oxidoreductases in parsley, Proc. Natl Acad. Sci. USA 94, 14954-14959.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 14954-14959
    • Koopmann, E.1    Hahlbrock, K.2
  • 15
    • 0030852872 scopus 로고    scopus 로고
    • Cloning, yeast expression, and characterization of the coupling of two distantly related Arabidopsis thaliana NADPH-cytochrome P450 reductases with P450 CYP73A5
    • Urban, P., Mignotte, C., Kazmaier, M., Delorme, F. & Pompon, D. (1997) Cloning, yeast expression, and characterization of the coupling of two distantly related Arabidopsis thaliana NADPH-cytochrome P450 reductases with P450 CYP73A5, J. Biol. Chem. 272, 19176-19186.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19176-19186
    • Urban, P.1    Mignotte, C.2    Kazmaier, M.3    Delorme, F.4    Pompon, D.5
  • 16
    • 0024410210 scopus 로고
    • Coding nucleotide. 5′ regulatory and deduced amino acid sequences of P450BM-3, a single peptide cytochrome P-450:NADPH-P-450 reductase from Bacillus megaterium
    • Ruettinger, R. T., Wen, L. P. & Fulco, A. J. (1989) Coding nucleotide. 5′ regulatory and deduced amino acid sequences of P450BM-3, a single peptide cytochrome P-450:NADPH-P-450 reductase from Bacillus megaterium, J. Biol. Chem. 264, 10987-10995.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10987-10995
    • Ruettinger, R.T.1    Wen, L.P.2    Fulco, A.J.3
  • 17
    • 0026795405 scopus 로고
    • Structurally and functionally conserved regions of cytochrome P-450 reductase as targets for DNA amplification by the polymerase chain reaction
    • Miles, J. S. (1992) Structurally and functionally conserved regions of cytochrome P-450 reductase as targets for DNA amplification by the polymerase chain reaction, Biochem. J. 287, 195-200.
    • (1992) Biochem. J. , vol.287 , pp. 195-200
    • Miles, J.S.1
  • 18
    • 0029867362 scopus 로고    scopus 로고
    • Candida maltosa NADPH-cytochrome P450 reductase: Cloning of a full-length cDNA, heterologous expression in Saccharomyces cerevisiae and function of the N-terminal region for membrane anchoring and proliferation of the endoplasmic reticulum
    • Kargel, E., Menzel, R., Honeck, H., Vogel, F., Bohmer, A. & Schunck, W. H. (1996) Candida maltosa NADPH-cytochrome P450 reductase: cloning of a full-length cDNA, heterologous expression in Saccharomyces cerevisiae and function of the N-terminal region for membrane anchoring and proliferation of the endoplasmic reticulum. Yeast 12, 333-348.
    • (1996) Yeast , vol.12 , pp. 333-348
    • Kargel, E.1    Menzel, R.2    Honeck, H.3    Vogel, F.4    Bohmer, A.5    Schunck, W.H.6
  • 19
    • 0024322441 scopus 로고
    • Disruption of the Saccharomyces cerevisiae gene for NADPH-cytochrome P450 reductase causes increased sensitivity to ketoconazole
    • Sutter, T. R. & Loper, J. C. (1989) Disruption of the Saccharomyces cerevisiae gene for NADPH-cytochrome P450 reductase causes increased sensitivity to ketoconazole, Biochem. Biophys. Res. Commun. 160, 1257-1266.
    • (1989) Biochem. Biophys. Res. Commun. , vol.160 , pp. 1257-1266
    • Sutter, T.R.1    Loper, J.C.2
  • 20
    • 0023899268 scopus 로고
    • Primary structure of Saccharomyces cerevisiae NADPH-cytochrome P450 reductase deduced from nucleotide sequence of its cloned gene
    • Yabusaki, Y., Murakami, H. & Ohkawa, H. (1988) Primary structure of Saccharomyces cerevisiae NADPH-cytochrome P450 reductase deduced from nucleotide sequence of its cloned gene, J. Biochem. (Tokyo) 103, 1004-1010.
    • (1988) J. Biochem. (Tokyo) , vol.103 , pp. 1004-1010
    • Yabusaki, Y.1    Murakami, H.2    Ohkawa, H.3
  • 21
    • 0029099231 scopus 로고
    • Cloning and characterization of the NADPH cytochrome P450 oxidoreductase gene from the filamentous fungus Aspergillus niger
    • Van den Brink, H. J., Van Zeijl, C. M., Brons, J. F., Van den Hondel, C. A. & Van Gorcom, R. F. (1995) Cloning and characterization of the NADPH cytochrome P450 oxidoreductase gene from the filamentous fungus Aspergillus niger, DNA Cell Biol. 14, 719-729.
    • (1995) DNA Cell Biol. , vol.14 , pp. 719-729
    • Van Den Brink, H.J.1    Van Zeijl, C.M.2    Brons, J.F.3    Van Den Hondel, C.A.4    Van Gorcom, R.F.5
  • 22
    • 0027630948 scopus 로고
    • Isolation and characterization of a cDNA clone from Catharanthus roseus encoding NADPH:Cytochrome P-450 reductase, an enzyme essential for reactions catalysed by cytochrome P-450 mono-oxygenases in plants
    • Meijer, A. H., Lopes, C. M., Voskuilen, J. T., de Waals, A., Verpoorte, R. & Hoge, J. H. (1993) Isolation and characterization of a cDNA clone from Catharanthus roseus encoding NADPH:cytochrome P-450 reductase, an enzyme essential for reactions catalysed by cytochrome P-450 mono-oxygenases in plants, Plant J. 4, 47-60.
    • (1993) Plant J. , vol.4 , pp. 47-60
    • Meijer, A.H.1    Lopes, C.M.2    Voskuilen, J.T.3    De Waals, A.4    Verpoorte, R.5    Hoge, J.H.6
  • 23
    • 0027406832 scopus 로고
    • Purification, characterization and cDNA cloning of an NADPH-cytochrome P450 reductase from mung bean
    • Shet, M. S., Sathasivan, K., Arlotto, M. A., Mehdy, M. C. & Estabrook, R. W. (1993) Purification, characterization and cDNA cloning of an NADPH-cytochrome P450 reductase from mung bean, Proc. Natl Acad. Sci. USA 90, 2890-2894.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 2890-2894
    • Shet, M.S.1    Sathasivan, K.2    Arlotto, M.A.3    Mehdy, M.C.4    Estabrook, R.W.5
  • 24
    • 0031000922 scopus 로고    scopus 로고
    • Drosophila melanogaster NADPH-cytochrome P450 oxidoreductase: Pronounced expression in antennae may be related to odorant clearance
    • Hovemann, B. T., Sehlmeyer, F. & Malz, J. (1997) Drosophila melanogaster NADPH-cytochrome P450 oxidoreductase: pronounced expression in antennae may be related to odorant clearance, Gene (Amst.) 189, 213-219.
    • (1997) Gene (Amst.) , vol.189 , pp. 213-219
    • Hovemann, B.T.1    Sehlmeyer, F.2    Malz, J.3
  • 25
    • 0027615917 scopus 로고
    • The cDNA and deduced protein sequence of house fly NADPH-cytochrome P450 reductase
    • Koener, J. F., Carino, F. A. & Feyereisen, R. (1993) The cDNA and deduced protein sequence of house fly NADPH-cytochrome P450 reductase, Insect Biochem. Mol. Biol. 23, 439-447.
    • (1993) Insect Biochem. Mol. Biol. , vol.23 , pp. 439-447
    • Koener, J.F.1    Carino, F.A.2    Feyereisen, R.3
  • 26
    • 0023665680 scopus 로고
    • Structural comparison between the trout and mammalian hydrophilic domain of NADPH-cytochrome P-450 reductase
    • Urenjak, J., Linder, D. & Lumper, L. (1987) Structural comparison between the trout and mammalian hydrophilic domain of NADPH-cytochrome P-450 reductase, J. Chromatogr. 397, 123-136.
    • (1987) J. Chromatogr. , vol.397 , pp. 123-136
    • Urenjak, J.1    Linder, D.2    Lumper, L.3
  • 27
    • 0022798555 scopus 로고
    • Molecular cloning and sequence analysis of full-length cDNA for rabbit liver NADPH-cytochrome P-450 reductase mRNA
    • Katagiri, M., Murakami, H., Yabusaki, Y., Sugiyama, T., Okamoto, M., Yamano, T. & Ohkawa, H. (1986) Molecular cloning and sequence analysis of full-length cDNA for rabbit liver NADPH-cytochrome P-450 reductase mRNA, J. Biochem. (Tokyo) 100, 945-954.
    • (1986) J. Biochem. (Tokyo) , vol.100 , pp. 945-954
    • Katagiri, M.1    Murakami, H.2    Yabusaki, Y.3    Sugiyama, T.4    Okamoto, M.5    Yamano, T.6    Ohkawa, H.7
  • 28
    • 0013569329 scopus 로고
    • Coding nucleotide sequence of rat NADPH-cytochrome P-450 oxidoreductase cDNA and identification of flavin-binding domains
    • Porter, T. D. & Kasper, C. B. (1985) Coding nucleotide sequence of rat NADPH-cytochrome P-450 oxidoreductase cDNA and identification of flavin-binding domains, Proc. Natl Acad. Sci. USA 82, 973-977.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 973-977
    • Porter, T.D.1    Kasper, C.B.2
  • 29
    • 0026464935 scopus 로고
    • Molecular cloning and sequence analysis of guinea-pig NADPH-cytochrome P-450 oxidoreductase
    • Ohgiya, S., Goda, T., Ishizaki, K., Kamataki, T. & Shinriki, N. (1992) Molecular cloning and sequence analysis of guinea-pig NADPH-cytochrome P-450 oxidoreductase, Biochim. Biophys. Acta 1171, 103-105.
    • (1992) Biochim. Biophys. Acta , vol.1171 , pp. 103-105
    • Ohgiya, S.1    Goda, T.2    Ishizaki, K.3    Kamataki, T.4    Shinriki, N.5
  • 30
    • 0028334566 scopus 로고
    • Mouse NADPH-cytochrome P-450 oxidoreductase: Molecular cloning and functional expression in yeast
    • Ohgiya, S., Shinriki, N., Kamataki, T. & Ishizaki, K. (1994) Mouse NADPH-cytochrome P-450 oxidoreductase: molecular cloning and functional expression in yeast, Biochim. Biophys. Acta 1186, 137-141.
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 137-141
    • Ohgiya, S.1    Shinriki, N.2    Kamataki, T.3    Ishizaki, K.4
  • 31
    • 0022448326 scopus 로고
    • Complete structure of the hydrophilic domain in the porcine NADPH-cytochrome P-450 reductase
    • Vogel, F. & Lumper, L. (1986) Complete structure of the hydrophilic domain in the porcine NADPH-cytochrome P-450 reductase, Biochem. J. 236, 871-878.
    • (1986) Biochem. J. , vol.236 , pp. 871-878
    • Vogel, F.1    Lumper, L.2
  • 32
    • 0024420756 scopus 로고
    • Structural and functional analysis of NADPH-cytochrome P-450 reductase from human liver: Complete sequence of human enzyme and NADPH-binding sites
    • Haniu, M., McManus, M. E., Birkett, D. J., Lee, T. D. & Shively, J. E. (1989) Structural and functional analysis of NADPH-cytochrome P-450 reductase from human liver: complete sequence of human enzyme and NADPH-binding sites, Biochemistry 28, 8639-8645.
    • (1989) Biochemistry , vol.28 , pp. 8639-8645
    • Haniu, M.1    McManus, M.E.2    Birkett, D.J.3    Lee, T.D.4    Shively, J.E.5
  • 34
    • 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. & Kim, J. (1997) Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes, Proc. Natl Acad. Sci. USA 94, 8411-8416.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 8411-8416
    • Wang, M.1    Roberts, D.L.2    Paschke, R.3    Shea, T.M.4    Masters, B.5    Kim, J.6
  • 35
    • 0017801794 scopus 로고
    • Purified liver microsomal NADPH-cytochrome P-450 reductase (spectral characterization of oxidation-reduction states)
    • Vermilion, J. L. & 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
  • 36
    • 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. & 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
  • 37
    • 0020479374 scopus 로고
    • Oxidation-reduction states of FMN and FAD in NADPH-cytochrome P-450 reductase during reduction by NADPH
    • Oprian, D. D. & Coon, M. J. (1982) Oxidation-reduction states of FMN and FAD in NADPH-cytochrome P-450 reductase during reduction by NADPH, J. Biol. Chem. 257, 8935-8944.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8935-8944
    • Oprian, D.D.1    Coon, M.J.2
  • 38
    • 0028106174 scopus 로고
    • Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains
    • Smith, G. C., Tew. D. G. & Wolf, C. R. (1994) Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains, Proc. Natl Acad. Sci. USA 91, 8710-8714.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8710-8714
    • Smith, G.C.1    Tew, D.G.2    Wolf, C.R.3
  • 39
    • 0016364533 scopus 로고
    • Redox properties of the reduced nicotinamide adenine dinucleotide phosphate-cytochrome P450 and reduced nicotinamide adenine dinucleotide-cytochrome b5 reductases
    • Iyanagi, T., Makino, N. & Mason, H. S. (1974) Redox properties of the reduced nicotinamide adenine dinucleotide phosphate-cytochrome P450 and reduced nicotinamide adenine dinucleotide-cytochrome b5 reductases, Biochemistry 13, 1701-1710.
    • (1974) Biochemistry , vol.13 , pp. 1701-1710
    • Iyanagi, T.1    Makino, N.2    Mason, H.S.3
  • 40
    • 0023034992 scopus 로고
    • Preparation and characterization of FAD-dependent NADPH-cytochrome P-450 reductase
    • Kurzban, G. P. & Strobel, H. W. (1986) Preparation and characterization of FAD-dependent NADPH-cytochrome P-450 reductase, J. Biol. Chem. 261, 7824-7830.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7824-7830
    • Kurzban, G.P.1    Strobel, H.W.2
  • 41
    • 0026611022 scopus 로고
    • P450 BM-3-reduction by NADPH and sodium dithionite
    • Peterson, J. A. & Boddupalli, S. S. (1992) P450 BM-3-reduction by NADPH and sodium dithionite, Arch. Biochem. Biophys. 294, 654-661.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 654-661
    • Peterson, J.A.1    Boddupalli, S.S.2
  • 42
    • 0028335241 scopus 로고
    • Affinity isolation and characterization of cytochrome-P450-102 (BM-3) from barbiturate-induced Bacillus megaterium
    • Black, S. D., Linger, M. H., Freck, L. C., Kazemi, S. & Galbraith, J. A. (1994) Affinity isolation and characterization of cytochrome-P450-102 (BM-3) from barbiturate-induced Bacillus megaterium, Arch. Biochem. Biophys. 310, 126-133.
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 126-133
    • Black, S.D.1    Linger, M.H.2    Freck, L.C.3    Kazemi, S.4    Galbraith, J.A.5
  • 44
    • 0030014679 scopus 로고    scopus 로고
    • The flavoprotein domain of P450BM-3: Expression, purification, and properties of the flavin adenine dinucleotide- and flavin mononucleotide-binding subdomains
    • Sevrioukova, I., Truan, G. & Peterson, J. A. (1996) The flavoprotein domain of P450BM-3: expression, purification, and properties of the flavin adenine dinucleotide- and flavin mononucleotide-binding subdomains, Biochemistry 35, 7528-7535.
    • (1996) Biochemistry , vol.35 , pp. 7528-7535
    • Sevrioukova, I.1    Truan, G.2    Peterson, J.A.3
  • 45
    • 0018786123 scopus 로고
    • Preparation of homogenous NADPH cytochrome c (P-450) reductase from house flies using affinity chromatography techniques
    • Mayer, R. T. & Durrant, J. L. (1979) Preparation of homogenous NADPH cytochrome c (P-450) reductase from house flies using affinity chromatography techniques, J. Biol. Chem. 254, 756-761.
    • (1979) J. Biol. Chem. , vol.254 , pp. 756-761
    • Mayer, R.T.1    Durrant, J.L.2
  • 46
    • 0018706810 scopus 로고
    • Studies on NADPH-cytochrome c reductase I: Isolation and several properties of the crystalline enzyme from ale yeast
    • Tryon, E., Cress, M. C., Hamada, M. & Kuby, S. A. (1979) Studies on NADPH-cytochrome c reductase I: Isolation and several properties of the crystalline enzyme from ale yeast, Arch. Biochem. Biophys. 197, 104-118.
    • (1979) Arch. Biochem. Biophys. , vol.197 , pp. 104-118
    • Tryon, E.1    Cress, M.C.2    Hamada, M.3    Kuby, S.A.4
  • 47
    • 0028519121 scopus 로고
    • Purification and partial characterization of NADPH-cytochrome c reductase from Petunia hybrida flowers
    • Menting, J. G., Cornish, E. & Scopes, R. K. (1994) Purification and partial characterization of NADPH-cytochrome c reductase from Petunia hybrida flowers, Plant Physiol. 106, 643-650.
    • (1994) Plant Physiol. , vol.106 , pp. 643-650
    • Menting, J.G.1    Cornish, E.2    Scopes, R.K.3
  • 48
    • 0025123903 scopus 로고
    • Histochemical and biochemical changes in skeletal muscles of rhabdomyolysis-sensitive racehorses following exertion. III: Elevated activity of various antioxidant enzymes
    • Meijer, A. E. & Van den Hoven, R. (1990) Histochemical and biochemical changes in skeletal muscles of rhabdomyolysis-sensitive racehorses following exertion. III: Elevated activity of various antioxidant enzymes, Acta Histochem. 89, 113-119.
    • (1990) Acta Histochem. , vol.89 , pp. 113-119
    • Meijer, A.E.1    Van Den Hoven, R.2
  • 49
    • 0029974618 scopus 로고    scopus 로고
    • Purification and characterization of an NADPH-cytochrome P450 (cytochrome c) reductase from spearmint (Mentha spicata) glandular trichomes
    • Ponnamperuma, K. & Croteau, R. (1996) Purification and characterization of an NADPH-cytochrome P450 (cytochrome c) reductase from spearmint (Mentha spicata) glandular trichomes, Arch. Biochem. Biophys. 329, 9-16.
    • (1996) Arch. Biochem. Biophys. , vol.329 , pp. 9-16
    • Ponnamperuma, K.1    Croteau, R.2
  • 50
    • 0018786505 scopus 로고
    • Detergent-solubilized NADPH-cytochrome c (P-450) reductase from the higher plant, Catharanthus roseus. Purification and characterization
    • Madyastha, K. M. & Coscia, C. J. (1979) Detergent-solubilized NADPH-cytochrome c (P-450) reductase from the higher plant, Catharanthus roseus. Purification and characterization, J. Biol. Chem. 254, 2419-2427.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2419-2427
    • Madyastha, K.M.1    Coscia, C.J.2
  • 51
    • 0023049367 scopus 로고
    • Purification and characterization of the NADPH-cytochrome P-450 (cytochrome c) reductase from higher-plant microsomal fraction
    • Benveniste, I., Gabriac, B. & Durst, F. (1986) Purification and characterization of the NADPH-cytochrome P-450 (cytochrome c) reductase from higher-plant microsomal fraction, Biochem. J. 235, 365-373.
    • (1986) Biochem. J. , vol.235 , pp. 365-373
    • Benveniste, I.1    Gabriac, B.2    Durst, F.3
  • 52
    • 0029776005 scopus 로고    scopus 로고
    • Yeast expression of animal and plant P450s in optimized redox environments
    • Pompon, D., Louerat, B., Bronine, A. & Urban, P. (1996) Yeast expression of animal and plant P450s in optimized redox environments, Methods Enzymol. 272, 51-64.
    • (1996) Methods Enzymol. , vol.272 , pp. 51-64
    • Pompon, D.1    Louerat, B.2    Bronine, A.3    Urban, P.4
  • 53
    • 0017088267 scopus 로고
    • Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography
    • Yasukochi, Y. & Masters, B. S. S. (1976) Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography, J. Biol. Chem. 251, 5337-5344.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5337-5344
    • Yasukochi, Y.1    Masters, B.S.S.2
  • 54
    • 0017057951 scopus 로고
    • Properties of electrophoretically homogeneous phenobarbital-inducible and beta-naphthoflavone-inducible forms of liver microsomal cytochrome P-450
    • Haugen, D. A. & Coon, M. J. (1976) properties of electrophoretically homogeneous phenobarbital-inducible and beta-naphthoflavone-inducible forms of liver microsomal cytochrome P-450, J. Biol. Chem. 251, 7929-7939.
    • (1976) J. Biol. Chem. , vol.251 , pp. 7929-7939
    • Haugen, D.A.1    Coon, M.J.2
  • 55
    • 0016696713 scopus 로고
    • Apparent dependence of interactions between cytochrome b5 and cytochrome b5 reductase upon translational diffusion in dimyristoyl lecithin liposomes
    • Strittmatter, P. & Rogers, M. J. (1975) Apparent dependence of interactions between cytochrome b5 and cytochrome b5 reductase upon translational diffusion in dimyristoyl lecithin liposomes, Proc. Natl Acad. Sci. USA 72, 2658-2661.
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 2658-2661
    • Strittmatter, P.1    Rogers, M.J.2
  • 56
    • 0026633609 scopus 로고
    • Singular value decomposition: Application to analysis of experimental data
    • Henry, E. R. & Hofrichter, J. (1992) Singular value decomposition: application to analysis of experimental data, Methods Enzymol. 210, 129-191.
    • (1992) Methods Enzymol. , vol.210 , pp. 129-191
    • Henry, E.R.1    Hofrichter, J.2
  • 57
    • 0015881843 scopus 로고
    • A rapid micromethod for determination of FMN and FAD in mixtures
    • Faeder, E. J. & Siegel, L. M. (1973) A rapid micromethod for determination of FMN and FAD in mixtures, Anal. Biochem. 53, 332-336.
    • (1973) Anal. Biochem. , vol.53 , pp. 332-336
    • Faeder, E.J.1    Siegel, L.M.2
  • 58
    • 0000415237 scopus 로고
    • On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A-IV. Isolation and properties of stable enzyme-substrate complexes
    • Steyn-Parve, E. P. & Beinert, H. (1958) On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A-IV. Isolation and properties of stable enzyme-substrate complexes, J. Biol. Chem. 233, 843-852.
    • (1958) J. Biol. Chem. , vol.233 , pp. 843-852
    • Steyn-Parve, E.P.1    Beinert, H.2
  • 59
    • 70449227895 scopus 로고
    • Oxidation of reduced diphosphopyridine nucleotide
    • Schellenberg, K. H. & Hellerman, L. (1958) Oxidation of reduced diphosphopyridine nucleotide, J. Biol. Chem. 231, 547-556.
    • (1958) J. Biol. Chem. , vol.231 , pp. 547-556
    • Schellenberg, K.H.1    Hellerman, L.2
  • 60
    • 0027936487 scopus 로고
    • Probing the putative cytochrome P450- and cytochrome c-binding sites on NADPH-cytochrome P450 reductase by anti-peptide antibodies
    • Shen, S. & Strobel, H. W. (1994) Probing the putative cytochrome P450- and cytochrome c-binding sites on NADPH-cytochrome P450 reductase by anti-peptide antibodies, Biochemistry 33, 8807-8812.
    • (1994) Biochemistry , vol.33 , pp. 8807-8812
    • Shen, S.1    Strobel, H.W.2
  • 61
    • 0028805425 scopus 로고
    • Role of acidic residues in the interaction of NADPH-cytochrome P450 oxidoreductase with cytochrome P450 and cytochrome c
    • Shen, A. L. & 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
  • 62
    • 0016364533 scopus 로고
    • Redox properties of the reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 and reduced nicotinamide adenine dinucleotide-cytochrome b5 reductases
    • Iyanagi, T., Makino, N. & Mason, H. S. (1974) Redox properties of the reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 and reduced nicotinamide adenine dinucleotide-cytochrome b5 reductases, Biochemistry 13, 1701-1710.
    • (1974) Biochemistry , vol.13 , pp. 1701-1710
    • Iyanagi, T.1    Makino, N.2    Mason, H.S.3
  • 64
    • 0028864050 scopus 로고
    • Interaction of NADPH-adrenodoxin reductase with NADP+ as studied by pulse radiolysis
    • Kobayashi, K., Miura, S., Miki, M., Ichikawa, Y. & Tagawa, S. (1995) Interaction of NADPH-adrenodoxin reductase with NADP+ as studied by pulse radiolysis, Biochemistry 34, 12932-12936.
    • (1995) Biochemistry , vol.34 , pp. 12932-12936
    • Kobayashi, K.1    Miura, S.2    Miki, M.3    Ichikawa, Y.4    Tagawa, S.5
  • 65
    • 0023002182 scopus 로고
    • Association of ferredoxin-NADP+ reductase with NADP(H) specificity and oxidation-reduction properties
    • Batie, C. J. & Kamin, H. (1986) Association of ferredoxin-NADP+ reductase with NADP(H) specificity and oxidation-reduction properties, J. Biol. Chem. 261, 11214-11223.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11214-11223
    • Batie, C.J.1    Kamin, H.2
  • 66
    • 0031452439 scopus 로고    scopus 로고
    • Protein disulfide isomerase as a regulator of chloroplast translational activation
    • Kim, J. & Mayfield, S. P. (1997) Protein disulfide isomerase as a regulator of chloroplast translational activation, Science 278, 1954-1957.
    • (1997) Science , vol.278 , pp. 1954-1957
    • Kim, J.1    Mayfield, S.P.2
  • 67
    • 0028587976 scopus 로고
    • Light-regulated translation of chloroplast messenger RNAs through redox potential
    • Danon, A. & Mayfield, S. P. (1994) Light-regulated translation of chloroplast messenger RNAs through redox potential. Science 266, 1717-1719.
    • (1994) Science , vol.266 , pp. 1717-1719
    • Danon, A.1    Mayfield, S.P.2
  • 68
    • 0017578840 scopus 로고
    • Studies on the microsomal electron-transport system of anaerobically grown yeast. V. Purification and characterization of NADPH-cytochrome c reductase
    • Kubota, S., Yoshida, Y., Kumaoka, H. & Furumichi, A. (1977) Studies on the microsomal electron-transport system of anaerobically grown yeast. V. Purification and characterization of NADPH-cytochrome c reductase, J. Biochem. (Tokyo) 81, 197-205.
    • (1977) J. Biochem. (Tokyo) , vol.81 , pp. 197-205
    • Kubota, S.1    Yoshida, Y.2    Kumaoka, H.3    Furumichi, A.4
  • 69
    • 0017330064 scopus 로고
    • Purification and characterization of NADPH-cytochrome c (P450) reductase from the house fly, Musca domestica
    • Mayer, R. T. & Prough, R. A. (1977) Purification and characterization of NADPH-cytochrome c (P450) reductase from the house fly, Musca domestica, Comp. Biochem. Physiol. B 57, 81-87.
    • (1977) Comp. Biochem. Physiol. B , vol.57 , pp. 81-87
    • Mayer, R.T.1    Prough, R.A.2
  • 70
    • 0021293765 scopus 로고
    • Kinetic properties of guinea pig liver microsomal NADPH-cytochrome P-450 reductase
    • Kobayashi, S. & Rikans, L. E. (1984) Kinetic properties of guinea pig liver microsomal NADPH-cytochrome P-450 reductase, Comp. Biochem. Physiol. B 77, 313-318.
    • (1984) Comp. Biochem. Physiol. B , vol.77 , pp. 313-318
    • Kobayashi, S.1    Rikans, L.E.2
  • 71
    • 0021895443 scopus 로고
    • The interaction of cytochrome b5 with four cytochrome P-450 enzymes from the untreated rat
    • Jansson, I., Tamburini, P. P., Favreau, L. V, & Shenkman, J. B. (1985) The interaction of cytochrome b5 with four cytochrome P-450 enzymes from the untreated rat, Drug. Metab. Dispos. 13, 453-458.
    • (1985) Drug. Metab. Dispos. , vol.13 , pp. 453-458
    • Jansson, I.1    Tamburini, P.P.2    Favreau, L.V.3    Shenkman, J.B.4


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