메뉴 건너뛰기




Volumn 78, Issue 8-9, 1996, Pages 744-751

Domain-domain interaction in cytochrome P450BM-3

Author keywords

Flavoproteins; Ionic strength; NADPH P450 reductase; Protein protein interaction

Indexed keywords

CYTOCHROME P450 ISOENZYME; FLAVINE MONONUCLEOTIDE; HEME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0030459246     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(97)82532-1     Document Type: Article
Times cited : (12)

References (62)
  • 1
    • 0022878676 scopus 로고
    • Characterization of a catalytically self-sufficient 119 000-dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium
    • 1 Narhi LO, Fulco AJ (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
  • 2
    • 0023654954 scopus 로고
    • Identification and characterization of two functional domains in cytochrome P-450BM-3, a catalytically self-sufficient monooxygenase induced by barbiturates in Bacillus megaterium
    • 2 Narhi LO, Fulco AJ (1987) Identification and characterization of two functional domains in cytochrome P-450BM-3, a catalytically self-sufficient monooxygenase induced by barbiturates in Bacillus megaterium. J Biol Chem 262, 6683-6690
    • (1987) J Biol Chem , vol.262 , pp. 6683-6690
    • Narhi, L.O.1    Fulco, A.J.2
  • 3
    • 0023654743 scopus 로고
    • Cloning of the gene encoding a catalytically self-sufficient cytochrome P-450 fatty acid monooxygenase induced by barbiturates in Bacillus megaterium and its functional expression and regulation in heterologous (Escherichia coli) and homologous (Bacillusn megaterium) hosts
    • 3 Wen LP, Fulco AJ (1987) Cloning of the gene encoding a catalytically self-sufficient cytochrome P-450 fatty acid monooxygenase induced by barbiturates in Bacillus megaterium and its functional expression and regulation in heterologous (Escherichia coli) and homologous (Bacillusn megaterium) hosts. J Biol Chem 262, 6676-6682
    • (1987) J Biol Chem , vol.262 , pp. 6676-6682
    • Wen, L.P.1    Fulco, A.J.2
  • 4
    • 0024410210 scopus 로고
    • Coding nucleotide, 5′ regulatory, and deduced amino acid sequences of P-450BM-3, a single peptide cytochrome P-450:NADPH-P-450 reductase from Bacillus megaterium
    • 4 Ruettinger RT, Wen LP, Fulco AJ (1989) Coding nucleotide, 5′ regulatory, and deduced amino acid sequences of P-450BM-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
  • 5
    • 0025976756 scopus 로고
    • An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals
    • 5 Porter TD (1991) An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals [review]. Trends Biochem Sci 16, 154-158
    • (1991) Trends Biochem Sci , vol.16 , pp. 154-158
    • Porter, T.D.1
  • 6
    • 0023044638 scopus 로고
    • NADPH-cytochrome P-450 oxidoreductase: Flavin mononucleotide and flavin adenine dinucleotide domains evolved from different flavoproteins
    • 6 Porter TD, Kasper CB (1986) NADPH-cytochrome P-450 oxidoreductase: flavin mononucleotide and flavin adenine dinucleotide domains evolved from different flavoproteins. Biochemistry 25, 1682-1687
    • (1986) Biochemistry , vol.25 , pp. 1682-1687
    • Porter, T.D.1    Kasper, C.B.2
  • 7
    • 0013569329 scopus 로고
    • Coding nucleotide sequence of rat NADPH-cytochrome P-450 oxidoreductase cDNA and identification of flavin-binding domains
    • 7 Porter TD, Kasper CB (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
  • 8
    • 0025315625 scopus 로고
    • Comparison of the kinetics of reduction and intramolecular electron transfer in electrostatic and covalent complexes of ferredoxin-NADP+ reductase and flavodoxin from Anabaena PCC 7119
    • 8 Walker MC, Pueyo JJ, Gomez-Moreno C, Tollin G (1990) Comparison of the kinetics of reduction and intramolecular electron transfer in electrostatic and covalent complexes of ferredoxin-NADP+ reductase and flavodoxin from Anabaena PCC 7119. Arch Biochem Biophys 281, 76-83
    • (1990) Arch Biochem Biophys , vol.281 , pp. 76-83
    • Walker, M.C.1    Pueyo, J.J.2    Gomez-Moreno, C.3    Tollin, G.4
  • 10
    • 0026588925 scopus 로고
    • Identification of specific carboxyl groups on Anabaena PCC 7119 flavodoxin which are involved in the interaction with ferredoxin-NADP+ reductase
    • 10 Medina M, Peleato ML, Mendez E, Gomez-Moreno C (1992) Identification of specific carboxyl groups on Anabaena PCC 7119 flavodoxin which are involved in the interaction with ferredoxin-NADP+ reductase. Eur J Biochem 203, 373-379
    • (1992) Eur J Biochem , vol.203 , pp. 373-379
    • Medina, M.1    Peleato, M.L.2    Mendez, E.3    Gomez-Moreno, C.4
  • 11
    • 0028106174 scopus 로고
    • Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains
    • 11 Smith GCM, Tew DG, Wolf CR (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.M.1    Tew, D.G.2    Wolf, C.R.3
  • 12
    • 0030025558 scopus 로고    scopus 로고
    • Characterization of the FAD binding domain of cytochrome P450 reductase
    • 12 Hodgson AV, Strobel HW (1996) Characterization of the FAD binding domain of cytochrome P450 reductase. Arch Biochem Biophys 325, 99-106
    • (1996) Arch Biochem Biophys , vol.325 , pp. 99-106
    • Hodgson, A.V.1    Strobel, H.W.2
  • 13
    • 0030014679 scopus 로고    scopus 로고
    • The flavoprotein domain of P450BM-3: Expression, purification, and properties of the FAD-and FMN-binding sub-domains
    • 13 Sevrioukova IF, Truan G, Peterson JA (1996) The flavoprotein domain of P450BM-3: Expression, purification, and properties of the FAD-and FMN-binding sub-domains. Biochemistry 35, 7528-7535
    • (1996) Biochemistry , vol.35 , pp. 7528-7535
    • Sevrioukova, I.F.1    Truan, G.2    Peterson, J.A.3
  • 14
    • 0023184975 scopus 로고
    • A genetically engineered P450 monooxygenase: Construction of the functional fused enzyme between rat cytochrome P450c and NADPH-cytochrome P450 reductase
    • 14 Murakami H, Yabusaki Y, Sakaki T, Shibata M, Ohkawa H (1987) A genetically engineered P450 monooxygenase: construction of the functional fused enzyme between rat cytochrome P450c and NADPH-cytochrome P450 reductase. DNA 6, 189-197
    • (1987) DNA , vol.6 , pp. 189-197
    • Murakami, H.1    Yabusaki, Y.2    Sakaki, T.3    Shibata, M.4    Ohkawa, H.5
  • 15
    • 0025344142 scopus 로고
    • Genetically engineered P450 monooxygenases: Construction of bovine P450c17/yeast reductase fused enzymes
    • 15 Shibata M, Sakaki T, Yabusaki Y, Murakami H, Ohkawa H (1990) Genetically engineered P450 monooxygenases: construction of bovine P450c17/yeast reductase fused enzymes. DNA Cell Biol 9, 27-36
    • (1990) DNA Cell Biol , vol.9 , pp. 27-36
    • Shibata, M.1    Sakaki, T.2    Yabusaki, Y.3    Murakami, H.4    Ohkawa, H.5
  • 16
    • 0026485793 scopus 로고
    • High-level expression in Escherichia coli of enzymatically active fusion proteins containing the domains of mammalian cytochromes P450 and NADPH-P450 reductase flavoprotein
    • 16 Fisher CW, Shet MS, Caudle DL, Martin-Wixtrom CA, Estabrook RW (1992) High-level expression in Escherichia coli of enzymatically active fusion proteins containing the domains of mammalian cytochromes P450 and NADPH-P450 reductase flavoprotein. Proc Natl Acad Sci USA 89, 10817-10821
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10817-10821
    • Fisher, C.W.1    Shet, M.S.2    Caudle, D.L.3    Martin-Wixtrom, C.A.4    Estabrook, R.W.5
  • 17
    • 0027146638 scopus 로고
    • Human cytochrome P450 3A4: Enzymatic properties of a purified recombinant fusion protein containing NADPH-P450 reductase
    • 17 Shet MS, Fisher CW, Holmans PL, Estabrook RW (1993) Human cytochrome P450 3A4: enzymatic properties of a purified recombinant fusion protein containing NADPH-P450 reductase. Proc Natl Acad Sci USA 90, 11748-11752
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11748-11752
    • Shet, M.S.1    Fisher, C.W.2    Holmans, P.L.3    Estabrook, R.W.4
  • 18
    • 0030021980 scopus 로고    scopus 로고
    • Mutagenesis study of ASP-290 in cytochrome P450 2B11 using a fusion protein with rat NADPH-cytochrome P450 reductase
    • 18 Harlow GR, Halpert JR (1996) Mutagenesis study of ASP-290 in cytochrome P450 2B11 using a fusion protein with rat NADPH-cytochrome P450 reductase. Arch Biochem Biophys 326, 85-92
    • (1996) Arch Biochem Biophys , vol.326 , pp. 85-92
    • Harlow, G.R.1    Halpert, J.R.2
  • 19
    • 0028839201 scopus 로고
    • NADPH-P450 reductase - Structural and functional comparisons of the eukaryotic and prokaryotic isoforms
    • 19 Sevrioukova IF, Peterson JA (1995) NADPH-P450 reductase - Structural and functional comparisons of the eukaryotic and prokaryotic isoforms. Biochimie 77, 562-572
    • (1995) Biochimie , vol.77 , pp. 562-572
    • Sevrioukova, I.F.1    Peterson, J.A.2
  • 20
    • 0029982439 scopus 로고    scopus 로고
    • Equilibrium and transient state spectrophotometric studies of the mechanism of reduction of the flavoprotein domain of P450BM-3
    • 20 Sevrioukova IF, Shaffer C, Ballou DP, Peterson JA (1996) Equilibrium and transient state spectrophotometric studies of the mechanism of reduction of the flavoprotein domain of P450BM-3. Biochemistry 35, 7058-7068
    • (1996) Biochemistry , vol.35 , pp. 7058-7068
    • Sevrioukova, I.F.1    Shaffer, C.2    Ballou, D.P.3    Peterson, J.A.4
  • 21
    • 0019876543 scopus 로고
    • Separate roles for FMN and FAD in catalysis by liver microsomal NADPH-cytochrome P-450 reductase
    • 21 Vermilion JL, Ballou DP, Massey V, Coon MJ (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
  • 22
    • 0023928296 scopus 로고
    • The effect of NADPH concentration on the reduction of cytochrome P-450 LM2
    • 22 Backes WL, Reker-Backes CE (1988) The effect of NADPH concentration on the reduction of cytochrome P-450 LM2. J Biol Chem 263, 247-253
    • (1988) J Biol Chem , vol.263 , pp. 247-253
    • Backes, W.L.1    Reker-Backes, C.E.2
  • 24
    • 0025718934 scopus 로고
    • Expression, purification, and properties of the flavoprotein domain of cytochrome P-450BM-3. Evidence for the importance of the amino-terminal region for FMN binding
    • 24 Oster T, Boddupalli SS, Peterson JA (1991) Expression, purification, and properties of the flavoprotein domain of cytochrome P-450BM-3. Evidence for the importance of the amino-terminal region for FMN binding. J Biol Chem 266, 22718-22725
    • (1991) J Biol Chem , vol.266 , pp. 22718-22725
    • Oster, T.1    Boddupalli, S.S.2    Peterson, J.A.3
  • 25
    • 0026745050 scopus 로고
    • Reconstitution of the fatty acid hydroxylation function of cytochrome P-450BM-3 utilizing its individual recombinant hemo-and flavoprotein domains
    • 25 Boddupalli SS, Oster T, Estabrook RW, Peterson JA (1992) Reconstitution of the fatty acid hydroxylation function of cytochrome P-450BM-3 utilizing its individual recombinant hemo-and flavoprotein domains. J Biol Chem 267, 10375-10380
    • (1992) J Biol Chem , vol.267 , pp. 10375-10380
    • Boddupalli, S.S.1    Oster, T.2    Estabrook, R.W.3    Peterson, J.A.4
  • 26
  • 27
    • 0018354912 scopus 로고
    • Properties of NADPH-cytochrome P-450 reductase purified from rabbit liver microsomes
    • 27 French JS, Coon MJ (1979) Properties of NADPH-cytochrome P-450 reductase purified from rabbit liver microsomes. Arch Biochem Biophys 195, 565-577
    • (1979) Arch Biochem Biophys , vol.195 , pp. 565-577
    • French, J.S.1    Coon, M.J.2
  • 28
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes: I. Evidence for its hemoprotein nature
    • 28 Omura T. Sato R (1964) The carbon monoxide-binding pigment of liver microsomes: I. Evidence for its hemoprotein nature. J Biol Chem 239, 2370-2378
    • (1964) J Biol Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 29
    • 0019769046 scopus 로고
    • Purification and properties of protocatechuate 3,4-dioxygenase from Pseudomonas putida. A new iron to subunit stoichiometry
    • 29 Bull C, Ballou DP (1981) Purification and properties of protocatechuate 3,4-dioxygenase from Pseudomonas putida. A new iron to subunit stoichiometry. J Biol Chem 256, 12673-12680
    • (1981) J Biol Chem , vol.256 , pp. 12673-12680
    • Bull, C.1    Ballou, D.P.2
  • 30
    • 49749184695 scopus 로고
    • The microestimation of succinate and the extinction coefficient of cytochrome c
    • 30 Massey V (1959) The microestimation of succinate and the extinction coefficient of cytochrome c. Biochim Biophys Acta 34, 255-256
    • (1959) Biochim Biophys Acta , vol.34 , pp. 255-256
    • Massey, V.1
  • 32
    • 0019888048 scopus 로고
    • Electrostatic interaction of cytochrome c with cytochrome c1 and cytochrome oxidase
    • 32 Smith HT, Ahmed AJ, Millett F (1981) Electrostatic interaction of cytochrome c with cytochrome c1 and cytochrome oxidase. J Biol Chem 256, 4984-4990
    • (1981) J Biol Chem , vol.256 , pp. 4984-4990
    • Smith, H.T.1    Ahmed, A.J.2    Millett, F.3
  • 33
    • 0019877180 scopus 로고
    • The relation of pH and oxidation-reduction potential to the association state of the ferredoxin, ferredoxin:NADP+ reductase complex
    • 33 Batie CJ, Kamin H (1981) The relation of pH and oxidation-reduction potential to the association state of the ferredoxin, ferredoxin:NADP+ reductase complex. J Biol Chem 256, 7756-7763
    • (1981) J Biol Chem , vol.256 , pp. 7756-7763
    • Batie, C.J.1    Kamin, H.2
  • 34
    • 0020490571 scopus 로고
    • The asymmetric distribution of charges on the surface of horse cytochrome c. Functional implications
    • 34 Koppenol WH, Margoliash E (1982) The asymmetric distribution of charges on the surface of horse cytochrome c. Functional implications. J Biol Chem 257, 4426-4437
    • (1982) J Biol Chem , vol.257 , pp. 4426-4437
    • Koppenol, W.H.1    Margoliash, E.2
  • 35
    • 0020477023 scopus 로고
    • Transient kinetics of electron transfer reactions of flavodoxin: Ionic strength dependence of semiquinone oxidation by cytochrome c, ferricyanide, and ferric ethylenediaminetetraacetic acid and computer modeling of reaction complexes
    • 35 Simondsen RP, Weber PC, Salemme FR, Tollin G (1982) Transient kinetics of electron transfer reactions of flavodoxin: ionic strength dependence of semiquinone oxidation by cytochrome c, ferricyanide, and ferric ethylenediaminetetraacetic acid and computer modeling of reaction complexes. Biochemistry 21, 6366-6375
    • (1982) Biochemistry , vol.21 , pp. 6366-6375
    • Simondsen, R.P.1    Weber, P.C.2    Salemme, F.R.3    Tollin, G.4
  • 36
    • 0017088267 scopus 로고
    • Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography
    • 36 Yasukochi Y, Masters BS (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.2
  • 37
    • 0001219461 scopus 로고
    • Charge transfer complexes of lipoyl dehydrogenase and free flavins
    • 37 Massey V, Palmer G (1962) Charge transfer complexes of lipoyl dehydrogenase and free flavins. J Biol Chem 237, 2347-2358
    • (1962) J Biol Chem , vol.237 , pp. 2347-2358
    • Massey, V.1    Palmer, G.2
  • 38
    • 0014014275 scopus 로고
    • Charge-transfer complexes of nicotinamide adenine dinucleotide analogues and flavin mononucleotide
    • 38 Sakurai T, Hosoya H (1966) Charge-transfer complexes of nicotinamide adenine dinucleotide analogues and flavin mononucleotide. Biochim Biophys Acta 112, 459-465
    • (1966) Biochim Biophys Acta , vol.112 , pp. 459-465
    • Sakurai, T.1    Hosoya, H.2
  • 39
    • 0001409925 scopus 로고
    • Role of charge-transfer interactions in flavoprotein catalysis
    • 39 Massey V, Ghisla S (1974) Role of charge-transfer interactions in flavoprotein catalysis. Ann NY Acad Sci 227, 446-465
    • (1974) Ann NY Acad Sci , vol.227 , pp. 446-465
    • Massey, V.1    Ghisla, S.2
  • 40
    • 0026023225 scopus 로고
    • Atomic structure of ferredoxin-NADP+ reductase: Prototype for a structurally novel flavoenzyme family
    • 40 Karplus PA, Daniels MJ, Herriott JR (1991) Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family. Science 251, 60-66
    • (1991) Science , vol.251 , pp. 60-66
    • Karplus, P.A.1    Daniels, M.J.2    Herriott, J.R.3
  • 41
    • 0027130428 scopus 로고
    • Interaction with arginine 597 of NADPH-cytochrome P-450 oxidoreductase is a primary source of the uniform binding energy used to discriminate between NADPH and NADH
    • 41 Sem DS, Kasper CB (1993) Interaction with arginine 597 of NADPH-cytochrome P-450 oxidoreductase is a primary source of the uniform binding energy used to discriminate between NADPH and NADH. Biochemistry 32, 11548-11558
    • (1993) Biochemistry , vol.32 , pp. 11548-11558
    • Sem, D.S.1    Kasper, C.B.2
  • 42
    • 0023695280 scopus 로고
    • Electrostatic interactions between cytochrome P-450 LM2 and NADPH-cytochrome P-450 reductase
    • 42 Bernhardt R, Kraft R, Otto A, Ruckpaul K (1988) Electrostatic interactions between cytochrome P-450 LM2 and NADPH-cytochrome P-450 reductase. Biomed Biochim Acta 47, 581-592
    • (1988) Biomed Biochim Acta , vol.47 , pp. 581-592
    • Bernhardt, R.1    Kraft, R.2    Otto, A.3    Ruckpaul, K.4
  • 43
    • 0023972392 scopus 로고
    • Role of electrostatic interactions in the reaction of NADPH-cytochrome P-450 reductase with cytochromes P-450
    • 43 Nadler SG, Strobel HW (1988) Role of electrostatic interactions in the reaction of NADPH-cytochrome P-450 reductase with cytochromes P-450. Arch Biochem Biophys 261, 418-429
    • (1988) Arch Biochem Biophys , vol.261 , pp. 418-429
    • Nadler, S.G.1    Strobel, H.W.2
  • 44
    • 0025755694 scopus 로고
    • Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagenesis. Interaction with NADPH-cytochrome P450 reductase
    • 44 Shimizu T, Tateishi T, Hatano M, Fujii-Kuriyama Y (1991) Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagenesis. Interaction with NADPH-cytochrome P450 reductase. J Biol Chem 266, 3372-3375
    • (1991) J Biol Chem , vol.266 , pp. 3372-3375
    • Shimizu, T.1    Tateishi, T.2    Hatano, M.3    Fujii-Kuriyama, Y.4
  • 45
    • 0021866350 scopus 로고
    • Electrostatic interactions during electron transfer reactions between c-type cytochromes and flavodoxin
    • 45 Weber PC, Tollin G (1985) Electrostatic interactions during electron transfer reactions between c-type cytochromes and flavodoxin. J Biol Chem 260, 5568-5573
    • (1985) J Biol Chem , vol.260 , pp. 5568-5573
    • Weber, P.C.1    Tollin, G.2
  • 48
    • 0029115790 scopus 로고
    • Site-specific mutagenesis demonstrates that the structural requirements for efficient electron transfer in Anabaena ferredoxin and flavodoxin are highly dependent on the reaction partner: Kinetic studies with photosystem I, ferredoxin:NADP+ reductase, and cytochrome c
    • 48 Navarro JA, Hervas M, Genzor CG, Cheddar G, Fillat MF, de la Rosa MA, Gomez-Moreno C, Cheng H, Xia B, Chae YK et al (1995) Site-specific mutagenesis demonstrates that the structural requirements for efficient electron transfer in Anabaena ferredoxin and flavodoxin are highly dependent on the reaction partner: kinetic studies with photosystem I, ferredoxin:NADP+ reductase, and cytochrome c. Arch Biochem Biophys 321, 229-238
    • (1995) Arch Biochem Biophys , vol.321 , pp. 229-238
    • Navarro, J.A.1    Hervas, M.2    Genzor, C.G.3    Cheddar, G.4    Fillat, M.F.5    De La Rosa, M.A.6    Gomez-Moreno, C.7    Cheng, H.8    Xia, B.9    Chae, Y.K.10
  • 49
    • 0025945557 scopus 로고
    • Characterization of recombinant Bacillus megaterium cytochrome P-450 BM-3 and its two functional domains
    • 49 Li HY, Darwish K, Poulos TL (1991) Characterization of recombinant Bacillus megaterium cytochrome P-450 BM-3 and its two functional domains. J Biol Chem 266, 11909-11914
    • (1991) J Biol Chem , vol.266 , pp. 11909-11914
    • Li, H.Y.1    Darwish, K.2    Poulos, T.L.3
  • 50
    • 0027522735 scopus 로고
    • Critical residues involved in FMN binding and catalytic activity in cytochrome P450BM-3
    • 50 Klein ML, Fuko AJ (1993) Critical residues involved in FMN binding and catalytic activity in cytochrome P450BM-3. J Biol Chem 268, 7553-7561
    • (1993) J Biol Chem , vol.268 , pp. 7553-7561
    • Klein, M.L.1    Fuko, A.J.2
  • 52
    • 0018291970 scopus 로고
    • Ionic effects on adrenal steroidogenic electron transport. The role of adrenodoxin as an electron shuttle
    • 52 Lambeth JD, Seybert DW, Kamin H (1979) Ionic effects on adrenal steroidogenic electron transport. The role of adrenodoxin as an electron shuttle. J Biol Chem 254, 7255-7264
    • (1979) J Biol Chem , vol.254 , pp. 7255-7264
    • Lambeth, J.D.1    Seybert, D.W.2    Kamin, H.3
  • 53
    • 0017149484 scopus 로고
    • Studies on the binding of FMN by apoflavodoxin from Peptostreptococcus elsdenii, pH and NaCl concentration dependence
    • 53 Gast R, Valk BE, Muller F, Mayhew SG, Veeger C (1976) Studies on the binding of FMN by apoflavodoxin from Peptostreptococcus elsdenii, pH and NaCl concentration dependence. Biochim Biophys Acta 446, 463-471
    • (1976) Biochim Biophys Acta , vol.446 , pp. 463-471
    • Gast, R.1    Valk, B.E.2    Muller, F.3    Mayhew, S.G.4    Veeger, C.5
  • 54
    • 0028116510 scopus 로고
    • Evidence for conformational dynamics and molecular aggregation in cytochrome P450 102 (BM-3)
    • 54 Black SD, Martin ST (1994) Evidence for conformational dynamics and molecular aggregation in cytochrome P450 102 (BM-3). Biochemistry 33, 12056-12062
    • (1994) Biochemistry , vol.33 , pp. 12056-12062
    • Black, S.D.1    Martin, S.T.2
  • 55
    • 0027978480 scopus 로고
    • On the domain structure of cytochrome P450 102 (BM-3): Isolation and properties of a 45-kDa FAD/NADP domain
    • 55 Black SD (1994) On the domain structure of cytochrome P450 102 (BM-3): isolation and properties of a 45-kDa FAD/NADP domain. Biochem Biophys Res Commun 203, 162-168
    • (1994) Biochem Biophys Res Commun , vol.203 , pp. 162-168
    • Black, S.D.1
  • 56
    • 0018220868 scopus 로고
    • Identification of the high and low potential flavins of liver microsomal NADPH-cytochrome P-450 reductase
    • 56 Vermilion JL, Coon MJ (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
  • 57
    • 0015795938 scopus 로고
    • Some properties of hepatic reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase
    • 57 Iyanagi T, Mason HS (1973) Some properties of hepatic reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase. Biochemistry 12, 2297-2308
    • (1973) Biochemistry , vol.12 , pp. 2297-2308
    • Iyanagi, T.1    Mason, H.S.2
  • 58
    • 0016364533 scopus 로고
    • Redox properties of the reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 and reduced nicotinamide adenine dinucleotide-cytochrome b5 reductases
    • 58 Iyanagi T, Makino N, Mason HS (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
  • 59
    • 0017801794 scopus 로고
    • Purified liver microsomal NADPH-cytochrome P-450 reductase. Spectral characterization of oxidation-reduction states
    • 59 Vermilion JL, Coon MJ (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
  • 60
    • 0001204305 scopus 로고
    • Studies on the mechanism of microsomal triphosphopyridine nucleotide-cytochrome c reductase
    • 60 Masters BS, Kamin H, Gibson QH, Williams CH Jr (1965) Studies on the mechanism of microsomal triphosphopyridine nucleotide-cytochrome c reductase. J Biol Chem 240, 921-931
    • (1965) J Biol Chem , vol.240 , pp. 921-931
    • Masters, B.S.1    Kamin, H.2    Gibson, Q.H.3    Williams C.H., Jr.4
  • 61
    • 0024441603 scopus 로고
    • Time-resolved fluorescence spectroscopy of NADPH-cytochrome P-450 reductase: Demonstration of energy transfer between the two prosthetic groups
    • 61 Bastiaens PI, Bonants PJ, Muller F, Visser AJ (1989) Time-resolved fluorescence spectroscopy of NADPH-cytochrome P-450 reductase: demonstration of energy transfer between the two prosthetic groups. Biochemistry 28, 8416-8425
    • (1989) Biochemistry , vol.28 , pp. 8416-8425
    • Bastiaens, P.I.1    Bonants, P.J.2    Muller, F.3    Visser, A.J.4
  • 62
    • 0004156151 scopus 로고
    • (Nozaki M, Yamamoto S, Ishimura Y, Coon MJ, Ernster LM, Estabrook RW, eds) Academic Press, New York
    • 62 Blumberg WE, Nishimoto M, Mason HS (1982) In: Oxygenases and Oxygen Metabolism (Nozaki M, Yamamoto S, Ishimura Y, Coon MJ, Ernster LM, Estabrook RW, eds) Academic Press, New York, 333-343
    • (1982) Oxygenases and Oxygen Metabolism , pp. 333-343
    • Blumberg, W.E.1    Nishimoto, M.2    Mason, H.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.