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Volumn 1770, Issue 3, 2007, Pages 330-344

Cytochrome P450 systems-biological variations of electron transport chains

Author keywords

Cytochrome P450; Electron transfer; Heme thiolate protein; Monooxygenase; P450 system; Redox partner

Indexed keywords

ALKANE; AROMATIC COMPOUND; BILE ACID; CARCINOGEN; CYTOCHROME P450; FATTY ACID; HERBICIDE; ICOSANOID; INSECTICIDE; MULTIENZYME COMPLEX; OXYGEN; STEROID; TERPENE; UNSPECIFIC MONOOXYGENASE; VITAMIN; XENOBIOTIC AGENT;

EID: 33846473252     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2006.07.017     Document Type: Review
Times cited : (643)

References (179)
  • 1
    • 0027443640 scopus 로고
    • Molecular evolution of P450 superfamily and P450-containing monooxygenase systems
    • Degtyarenko K.N., and Archakov A.I. Molecular evolution of P450 superfamily and P450-containing monooxygenase systems. FEBS Lett. 332 (1993) 1-8
    • (1993) FEBS Lett. , vol.332 , pp. 1-8
    • Degtyarenko, K.N.1    Archakov, A.I.2
  • 2
    • 50449100139 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties
    • Omura T., and Sato R. The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties. J. Biol. Chem. 239 (1964) 2379-2385
    • (1964) J. Biol. Chem. , vol.239 , pp. 2379-2385
    • Omura, T.1    Sato, R.2
  • 3
    • 0014196737 scopus 로고
    • Reconversion of detergent- and sulfhydryl reagent-produced P-420 to P-450 by polyols and glutathione
    • Ichikawa Y., and Yamano T. Reconversion of detergent- and sulfhydryl reagent-produced P-420 to P-450 by polyols and glutathione. Biochim. Biophys. Acta 131 (1967) 490-497
    • (1967) Biochim. Biophys. Acta , vol.131 , pp. 490-497
    • Ichikawa, Y.1    Yamano, T.2
  • 4
    • 0014216316 scopus 로고
    • An electron spin resonance study of microsomal fex
    • Murakami K., and Mason H.S. An electron spin resonance study of microsomal fex. J. Biol. Chem. 242 (1967) 1102-1110
    • (1967) J. Biol. Chem. , vol.242 , pp. 1102-1110
    • Murakami, K.1    Mason, H.S.2
  • 5
    • 0025776149 scopus 로고
    • Nomenclature Committee of the International Union of Biochemistry (NC-IUB). Nomenclature of electron-transfer proteins. Recommendations 1989
    • NC-IUB. Nomenclature Committee of the International Union of Biochemistry (NC-IUB). Nomenclature of electron-transfer proteins. Recommendations 1989. Eur. J. Biochem. 200 (1991) 599-611
    • (1991) Eur. J. Biochem. , vol.200 , pp. 599-611
    • NC-IUB1
  • 6
    • 0343537840 scopus 로고
    • Regulation mechanism of the activity of the hepatic endosplasmic cytochrome P-450
    • Ruckpaul K., and Rein H. (Eds), Akademie-Verlag, Berlin
    • Ruckpaul K., Rein H., and Blanck J. Regulation mechanism of the activity of the hepatic endosplasmic cytochrome P-450. In: Ruckpaul K., and Rein H. (Eds). Basis and Mechanism of Regulation of Cytochrome P450 (1989), Akademie-Verlag, Berlin 1-55
    • (1989) Basis and Mechanism of Regulation of Cytochrome P450 , pp. 1-55
    • Ruckpaul, K.1    Rein, H.2    Blanck, J.3
  • 8
    • 0034572736 scopus 로고    scopus 로고
    • Cytochromes P450: a success story
    • (REVIEWS3003)
    • Werck-Reichhart D., and Feyereisen R. Cytochromes P450: a success story. Genome Biol. 1 (2000) (REVIEWS3003)
    • (2000) Genome Biol. , vol.1
    • Werck-Reichhart, D.1    Feyereisen, R.2
  • 10
    • 0034973773 scopus 로고    scopus 로고
    • Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity
    • Guengerich F.P. Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity. Chem. Res. Toxicol. 14 (2001) 611-650
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 611-650
    • Guengerich, F.P.1
  • 11
    • 33744520321 scopus 로고    scopus 로고
    • Cytochromes P450 as versatile biocatalysts
    • Bernhardt R. Cytochromes P450 as versatile biocatalysts. J. Biotechnol. 124 (2006) 128-145
    • (2006) J. Biotechnol. , vol.124 , pp. 128-145
    • Bernhardt, R.1
  • 14
    • 0026542989 scopus 로고
    • Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences
    • Gotoh O. Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences. J. Biol. Chem. 267 (1992) 83-90
    • (1992) J. Biol. Chem. , vol.267 , pp. 83-90
    • Gotoh, O.1
  • 15
    • 0034951704 scopus 로고    scopus 로고
    • Evolution of bioinorganic motifs in P450-containing systems
    • Degtyarenko K.N., and Kulikova T.A. Evolution of bioinorganic motifs in P450-containing systems. Biochem. Soc. Trans. 29 (2001) 139-147
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 139-147
    • Degtyarenko, K.N.1    Kulikova, T.A.2
  • 16
    • 0025784027 scopus 로고
    • Cytochrome P-450. Multiplicity of isoforms, substrates, and catalytic and regulatory mechanisms
    • Porter T.D., and Coon M.J. Cytochrome P-450. Multiplicity of isoforms, substrates, and catalytic and regulatory mechanisms. J. Biol. Chem. 266 (1991) 13469-13472
    • (1991) J. Biol. Chem. , vol.266 , pp. 13469-13472
    • Porter, T.D.1    Coon, M.J.2
  • 18
    • 0001507078 scopus 로고
    • Isolation from adrenal cortex of a nonheme iron protein and a flavoprotein functional as a reduced triphosphopyridine nucleotide-cytochrome P-450 reductase
    • Omura T., Sanders E., Estabrook R.W., Cooper D.Y., and Rosenthal O. Isolation from adrenal cortex of a nonheme iron protein and a flavoprotein functional as a reduced triphosphopyridine nucleotide-cytochrome P-450 reductase. Arch. Biochem. Biophys. 117 (1966) 660-673
    • (1966) Arch. Biochem. Biophys. , vol.117 , pp. 660-673
    • Omura, T.1    Sanders, E.2    Estabrook, R.W.3    Cooper, D.Y.4    Rosenthal, O.5
  • 19
    • 0014429295 scopus 로고
    • Role of hemoprotein P-450 in fatty acid omega-hydroxylation in a soluble enzyme system from liver microsomes
    • Lu A.Y., and Coon M.J. Role of hemoprotein P-450 in fatty acid omega-hydroxylation in a soluble enzyme system from liver microsomes. J. Biol. Chem. 243 (1968) 1331-1332
    • (1968) J. Biol. Chem. , vol.243 , pp. 1331-1332
    • Lu, A.Y.1    Coon, M.J.2
  • 20
    • 0014670327 scopus 로고
    • Resolution of the cytochrome P-450-containing omega-hydroxylation system of liver microsomes into three components
    • Lu A.Y., Junk K.W., and Coon M.J. Resolution of the cytochrome P-450-containing omega-hydroxylation system of liver microsomes into three components. J. Biol. Chem. 244 (1969) 3714-3721
    • (1969) J. Biol. Chem. , vol.244 , pp. 3714-3721
    • Lu, A.Y.1    Junk, K.W.2    Coon, M.J.3
  • 21
    • 0014357086 scopus 로고
    • A soluble methylene hydroxylase system: Structure and role of cytochrome P-450 and iron-sulfur protein components
    • Gunsalus I.C. A soluble methylene hydroxylase system: Structure and role of cytochrome P-450 and iron-sulfur protein components. Hoppe Seylers Z. Physiol. Chem. 349 (1968) 1610-1613
    • (1968) Hoppe Seylers Z. Physiol. Chem. , vol.349 , pp. 1610-1613
    • Gunsalus, I.C.1
  • 22
    • 0014429758 scopus 로고
    • A soluble cytochrome P-450 functional in methylene hydroxylation
    • Katagiri M., Ganguli B.N., and Gunsalus I.C. A soluble cytochrome P-450 functional in methylene hydroxylation. J. Biol. Chem. 243 (1968) 3543-3546
    • (1968) J. Biol. Chem. , vol.243 , pp. 3543-3546
    • Katagiri, M.1    Ganguli, B.N.2    Gunsalus, I.C.3
  • 23
    • 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. Characterization of a catalytically self-sufficient 119,000-dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium. J. Biol. Chem. 261 (1986) 7160-7169
    • (1986) J. Biol. Chem. , vol.261 , pp. 7160-7169
    • Narhi, L.O.1    Fulco, A.J.2
  • 24
    • 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
    • Narhi L.O., and Fulco A.J. 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 (1987) 6683-6690
    • (1987) J. Biol. Chem. , vol.262 , pp. 6683-6690
    • Narhi, L.O.1    Fulco, A.J.2
  • 25
    • 0028794689 scopus 로고    scopus 로고
    • Cytochrome P450: Structure, function, and generation of reactive oxygen species
    • Bernhardt R. Cytochrome P450: Structure, function, and generation of reactive oxygen species. Rev. Physiol., Biochem. Pharmacol. 127 (1996) 137-221
    • (1996) Rev. Physiol., Biochem. Pharmacol. , vol.127 , pp. 137-221
    • Bernhardt, R.1
  • 27
    • 0002108871 scopus 로고
    • Enzymology of mitochondrial side-chain cleavage by cytochrome P-450scc
    • Lambeth J.D. Enzymology of mitochondrial side-chain cleavage by cytochrome P-450scc. Frontiers in Biotransformation (1991) 58-100
    • (1991) Frontiers in Biotransformation , pp. 58-100
    • Lambeth, J.D.1
  • 28
    • 0345257882 scopus 로고    scopus 로고
    • Bacterial (CYP101) and mitochondrial P450 systems-how comparable are they?
    • Schiffler B., and Bernhardt R. Bacterial (CYP101) and mitochondrial P450 systems-how comparable are they?. Biochem. Biophys. Res. Commun. 312 (2003) 223-228
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , pp. 223-228
    • Schiffler, B.1    Bernhardt, R.2
  • 29
    • 0033527407 scopus 로고    scopus 로고
    • Cytochrome P450105D1 (CYP105D1) from Streptomyces griseus: Heterologous expression, activity, and activation effects of multiple xenobiotics
    • Taylor M., Lamb D.C., Cannell R., Dawson M., and Kelly S.L. Cytochrome P450105D1 (CYP105D1) from Streptomyces griseus: Heterologous expression, activity, and activation effects of multiple xenobiotics. Biochem. Biophys. Res. Commun. 263 (1999) 838-842
    • (1999) Biochem. Biophys. Res. Commun. , vol.263 , pp. 838-842
    • Taylor, M.1    Lamb, D.C.2    Cannell, R.3    Dawson, M.4    Kelly, S.L.5
  • 30
    • 4744337841 scopus 로고    scopus 로고
    • Expression and characterization of the two flavodoxin proteins of Bacillus subtilis, YkuN and YkuP: biophysical properties and interactions with cytochrome P450 BioI
    • Lawson R.J., von Wachenfeldt C., Haq I., Perkins J., and Munro A.W. Expression and characterization of the two flavodoxin proteins of Bacillus subtilis, YkuN and YkuP: biophysical properties and interactions with cytochrome P450 BioI. Biochemistry 43 (2004) 12390-12409
    • (2004) Biochemistry , vol.43 , pp. 12390-12409
    • Lawson, R.J.1    von Wachenfeldt, C.2    Haq, I.3    Perkins, J.4    Munro, A.W.5
  • 31
    • 21344469236 scopus 로고    scopus 로고
    • Biosynthesis of the polyene macrolide antibiotic nystatin in Streptomyces noursei
    • Fjaervik E., and Zotchev S.B. Biosynthesis of the polyene macrolide antibiotic nystatin in Streptomyces noursei. Appl. Microbiol. Biotechnol. 67 (2005) 436-443
    • (2005) Appl. Microbiol. Biotechnol. , vol.67 , pp. 436-443
    • Fjaervik, E.1    Zotchev, S.B.2
  • 32
    • 14244251991 scopus 로고    scopus 로고
    • Characterization of the polyene macrolide P450 epoxidase from Streptomyces natalensis that converts de-epoxypimaricin into pimaricin
    • Mendes M.V., Anton N., Martin J.F., and Aparicio J.F. Characterization of the polyene macrolide P450 epoxidase from Streptomyces natalensis that converts de-epoxypimaricin into pimaricin. Biochem. J. 386 (2005) 57-62
    • (2005) Biochem. J. , vol.386 , pp. 57-62
    • Mendes, M.V.1    Anton, N.2    Martin, J.F.3    Aparicio, J.F.4
  • 33
    • 3943081412 scopus 로고    scopus 로고
    • Structural aspects of ligand binding to and electron transfer in bacterial and fungal P450s
    • Pylypenko O., and Schlichting I. Structural aspects of ligand binding to and electron transfer in bacterial and fungal P450s. Annu. Rev. Biochem. 73 (2004) 991-1018
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 991-1018
    • Pylypenko, O.1    Schlichting, I.2
  • 34
    • 17444405636 scopus 로고    scopus 로고
    • Biocatalytic production of perillyl alcohol from limonene by using a novel Mycobacterium sp. cytochrome P450 alkane hydroxylase expressed in Pseudomonas putida
    • van Beilen J.B., Holtackers R., Luscher D., Bauer U., Witholt B., and Duetz W.A. Biocatalytic production of perillyl alcohol from limonene by using a novel Mycobacterium sp. cytochrome P450 alkane hydroxylase expressed in Pseudomonas putida. Appl. Environ. Microbiol. 71 (2005) 1737-1744
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 1737-1744
    • van Beilen, J.B.1    Holtackers, R.2    Luscher, D.3    Bauer, U.4    Witholt, B.5    Duetz, W.A.6
  • 35
    • 0025840524 scopus 로고
    • Purification and characterization of a soybean flour-inducible ferredoxin reductase of Streptomyces griseus
    • Ramachandra M., Seetharam R., Emptage M.H., and Sariaslani F.S. Purification and characterization of a soybean flour-inducible ferredoxin reductase of Streptomyces griseus. J. Bacteriol. 173 (1991) 7106-7112
    • (1991) J. Bacteriol. , vol.173 , pp. 7106-7112
    • Ramachandra, M.1    Seetharam, R.2    Emptage, M.H.3    Sariaslani, F.S.4
  • 36
    • 0025159431 scopus 로고
    • Purification and characterization of a 7Fe ferredoxin from Streptomyces griseus
    • Trower M.K., Emptage M.H., and Sariaslani F.S. Purification and characterization of a 7Fe ferredoxin from Streptomyces griseus. Biochim. Biophys. Acta 1037 (1990) 281-289
    • (1990) Biochim. Biophys. Acta , vol.1037 , pp. 281-289
    • Trower, M.K.1    Emptage, M.H.2    Sariaslani, F.S.3
  • 37
    • 0026726458 scopus 로고
    • Cloning, nucleotide sequence determination and expression of the genes encoding cytochrome P-450soy (soyC) and ferredoxinsoy (soyB) from Streptomyces griseus
    • Trower M.K., Lenstra R., Omer C., Buchholz S.E., and Sariaslani F.S. Cloning, nucleotide sequence determination and expression of the genes encoding cytochrome P-450soy (soyC) and ferredoxinsoy (soyB) from Streptomyces griseus. Mol. Microbiol. 6 (1992) 2125-2134
    • (1992) Mol. Microbiol. , vol.6 , pp. 2125-2134
    • Trower, M.K.1    Lenstra, R.2    Omer, C.3    Buchholz, S.E.4    Sariaslani, F.S.5
  • 38
    • 0037245378 scopus 로고    scopus 로고
    • Expression, purification and characterisation of a Bacillus subtilis ferredoxin: A potential electron transfer donor to cytochrome P450 BioI
    • Green A.J., Munro A.W., Cheesman M.R., Reid G.A., von Wachenfeldt C., and Chapman S.K. Expression, purification and characterisation of a Bacillus subtilis ferredoxin: A potential electron transfer donor to cytochrome P450 BioI. J. Inorg. Biochem. 93 (2003) 92-99
    • (2003) J. Inorg. Biochem. , vol.93 , pp. 92-99
    • Green, A.J.1    Munro, A.W.2    Cheesman, M.R.3    Reid, G.A.4    von Wachenfeldt, C.5    Chapman, S.K.6
  • 40
    • 0025257597 scopus 로고
    • Putidaredoxin reductase and putidaredoxin. Cloning, sequence determination, and heterologous expression of the proteins
    • Peterson J.A., Lorence M.C., and Amarneh B. Putidaredoxin reductase and putidaredoxin. Cloning, sequence determination, and heterologous expression of the proteins. J. Biol. Chem. 265 (1990) 6066-6073
    • (1990) J. Biol. Chem. , vol.265 , pp. 6066-6073
    • Peterson, J.A.1    Lorence, M.C.2    Amarneh, B.3
  • 42
    • 0141869098 scopus 로고    scopus 로고
    • Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida
    • Sevrioukova I.F., Garcia C., Li H., Bhaskar B., and Poulos T.L. Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida. J. Mol. Biol. 333 (2003) 377-392
    • (2003) J. Mol. Biol. , vol.333 , pp. 377-392
    • Sevrioukova, I.F.1    Garcia, C.2    Li, H.3    Bhaskar, B.4    Poulos, T.L.5
  • 43
    • 1042264042 scopus 로고    scopus 로고
    • Crystal structure of putidaredoxin reductase from Pseudomonas putida, the final structural component of the cytochrome P450cam monooxygenase
    • Sevrioukova I.F., Li H., and Poulos T.L. Crystal structure of putidaredoxin reductase from Pseudomonas putida, the final structural component of the cytochrome P450cam monooxygenase. J. Mol. Biol. 336 (2004) 889-902
    • (2004) J. Mol. Biol. , vol.336 , pp. 889-902
    • Sevrioukova, I.F.1    Li, H.2    Poulos, T.L.3
  • 44
    • 0035965284 scopus 로고    scopus 로고
    • The interaction of bovine adrenodoxin with CYP11A1 (cytochrome P450scc) and CYP11B1 (cytochrome P45011beta). Acceleration of reduction and substrate conversion by site-directed mutagenesis of adrenodoxin
    • Schiffler B., Kiefer M., Wilken A., Hannemann F., Adolph H.W., and Bernhardt R. The interaction of bovine adrenodoxin with CYP11A1 (cytochrome P450scc) and CYP11B1 (cytochrome P45011beta). Acceleration of reduction and substrate conversion by site-directed mutagenesis of adrenodoxin. J. Biol. Chem. 276 (2001) 36225-36232
    • (2001) J. Biol. Chem. , vol.276 , pp. 36225-36232
    • Schiffler, B.1    Kiefer, M.2    Wilken, A.3    Hannemann, F.4    Adolph, H.W.5    Bernhardt, R.6
  • 45
    • 0034641677 scopus 로고    scopus 로고
    • Crystal structures of adrenodoxin reductase in complex with NADP+ and NADPH suggesting a mechanism for the electron transfer of an enzyme family
    • Ziegler G.A., and Schulz G.E. Crystal structures of adrenodoxin reductase in complex with NADP+ and NADPH suggesting a mechanism for the electron transfer of an enzyme family. Biochemistry 39 (2000) 10986-10995
    • (2000) Biochemistry , vol.39 , pp. 10986-10995
    • Ziegler, G.A.1    Schulz, G.E.2
  • 46
    • 0033057396 scopus 로고    scopus 로고
    • The structure of adrenodoxin reductase of mitochondrial P450 systems: Electron transfer for steroid biosynthesis
    • Ziegler G.A., Vonrhein C., Hanukoglu I., and Schulz G.E. The structure of adrenodoxin reductase of mitochondrial P450 systems: Electron transfer for steroid biosynthesis. J. Mol. Biol. 289 (1999) 981-990
    • (1999) J. Mol. Biol. , vol.289 , pp. 981-990
    • Ziegler, G.A.1    Vonrhein, C.2    Hanukoglu, I.3    Schulz, G.E.4
  • 47
    • 0037172776 scopus 로고    scopus 로고
    • A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin
    • Beilke D., Weiss R., Lohr F., Pristovsek P., Hannemann F., Bernhardt R., and Ruterjans H. A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin. Biochemistry 41 (2002) 7969-7978
    • (2002) Biochemistry , vol.41 , pp. 7969-7978
    • Beilke, D.1    Weiss, R.2    Lohr, F.3    Pristovsek, P.4    Hannemann, F.5    Bernhardt, R.6    Ruterjans, H.7
  • 48
    • 0032618110 scopus 로고    scopus 로고
    • Purified fusion enzyme between rat cytochrome P4501A1 and yeast NADPH-cytochrome P450 oxidoreductase
    • Hara M., Miyake J., Asada Y., and Ohkawa H. Purified fusion enzyme between rat cytochrome P4501A1 and yeast NADPH-cytochrome P450 oxidoreductase. Biosci. Biotechnol. Biochem. 63 (1999) 21-28
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 21-28
    • Hara, M.1    Miyake, J.2    Asada, Y.3    Ohkawa, H.4
  • 49
    • 0018563695 scopus 로고
    • The formation of binary and ternary complexes of cytochrome P-450scc with adrenodoxin and adrenodoxin reductase.adrenodoxin complex. The implication in ACTH function
    • Kido T., and Kimura T. The formation of binary and ternary complexes of cytochrome P-450scc with adrenodoxin and adrenodoxin reductase.adrenodoxin complex. The implication in ACTH function. J. Biol. Chem. 254 (1979) 11806-11815
    • (1979) J. Biol. Chem. , vol.254 , pp. 11806-11815
    • Kido, T.1    Kimura, T.2
  • 50
    • 0018291970 scopus 로고
    • Ionic effects on adrenal steroidogenic electron transport. The role of adrenodoxin as an electron shuttle
    • Lambeth J.D., Seybert D.W., and Kamin H. Ionic effects on adrenal steroidogenic electron transport. The role of adrenodoxin as an electron shuttle. J. Biol. Chem. 254 (1979) 7255-7264
    • (1979) J. Biol. Chem. , vol.254 , pp. 7255-7264
    • Lambeth, J.D.1    Seybert, D.W.2    Kamin, H.3
  • 51
    • 0018215190 scopus 로고
    • The participation of a second molecule of adrenodoxin in cytochrome P-450-catalyzed 11beta hydroxylation
    • Seybert D.W., Lambeth J.D., and Kamin H. The participation of a second molecule of adrenodoxin in cytochrome P-450-catalyzed 11beta hydroxylation. J. Biol. Chem. 253 (1978) 8355-8358
    • (1978) J. Biol. Chem. , vol.253 , pp. 8355-8358
    • Seybert, D.W.1    Lambeth, J.D.2    Kamin, H.3
  • 52
    • 0003357909 scopus 로고    scopus 로고
    • B.S. Werck-Reichhart D, Paquette S, Cytochrome P450, in: C.R. Somerville, Meyerowitz, E.M. (Eds.), The Arabidopsis Book, American Society of Plant Biologists, Rockville, MD, 2002, pp. doi:10.1199/tab.0028, www.aspb.org/publications/arabidopsis/.
  • 54
    • 77957192530 scopus 로고    scopus 로고
    • Function and evolution of plant cytochrome P450
    • Kahn R., and Durst F. Function and evolution of plant cytochrome P450. Recent Adv. Phytochem. 34 (2000) 151-189
    • (2000) Recent Adv. Phytochem. , vol.34 , pp. 151-189
    • Kahn, R.1    Durst, F.2
  • 55
    • 0003002061 scopus 로고    scopus 로고
    • Electron transfer proteins of cytochrome P450 systems
    • Hanukoglu I. Electron transfer proteins of cytochrome P450 systems. Adv. Mol. Cell. Biol. 14 (1996) 29-56
    • (1996) Adv. Mol. Cell. Biol. , vol.14 , pp. 29-56
    • Hanukoglu, I.1
  • 56
    • 0023044638 scopus 로고
    • NADPH-cytochrome P-450 oxidoreductase: Flavin mononucleotide and flavin adenine dinucleotide domains evolved from different flavoproteins
    • Porter T.D., and Kasper C.B. NADPH-cytochrome P-450 oxidoreductase: Flavin mononucleotide and flavin adenine dinucleotide domains evolved from different flavoproteins. Biochemistry 25 (1986) 1682-1687
    • (1986) Biochemistry , vol.25 , pp. 1682-1687
    • Porter, T.D.1    Kasper, C.B.2
  • 57
    • 0028106174 scopus 로고
    • Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains
    • Smith G.C., Tew D.G., and Wolf C.R. Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 8710-8714
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 8710-8714
    • Smith, G.C.1    Tew, D.G.2    Wolf, C.R.3
  • 58
    • 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. Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 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
  • 59
    • 12944300317 scopus 로고
    • Binding of nucleotides by proteins
    • Schulz G.E. Binding of nucleotides by proteins. Curr. Opin. Struct. Biol. 2 (1992) 61-67
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 61-67
    • Schulz, G.E.1
  • 60
    • 0036947946 scopus 로고    scopus 로고
    • The roles of cytochrome b5 in cytochrome P450 reactions
    • Porter T.D. The roles of cytochrome b5 in cytochrome P450 reactions. J. Biochem. Mol. Toxicol. 16 (2002) 311-316
    • (2002) J. Biochem. Mol. Toxicol. , vol.16 , pp. 311-316
    • Porter, T.D.1
  • 61
    • 0021383308 scopus 로고
    • On the function of cytochrome b5 in the cytochrome P-450-dependent oxygenase system
    • Hlavica P. On the function of cytochrome b5 in the cytochrome P-450-dependent oxygenase system. Arch. Biochem. Biophys. 228 (1984) 600-608
    • (1984) Arch. Biochem. Biophys. , vol.228 , pp. 600-608
    • Hlavica, P.1
  • 62
    • 85025548989 scopus 로고
    • Cytochrome b5 as electron donor to rabbit liver cytochrome P-450LM2 in reconstituted phospholipid vesicles
    • Ingelman-Sundberg M., and Johansson I. Cytochrome b5 as electron donor to rabbit liver cytochrome P-450LM2 in reconstituted phospholipid vesicles. Biochem. Biophys. Res. Commun. 97 (1980) 582-586
    • (1980) Biochem. Biophys. Res. Commun. , vol.97 , pp. 582-586
    • Ingelman-Sundberg, M.1    Johansson, I.2
  • 64
    • 0028970539 scopus 로고
    • Cytochrome b5, its functions, structure and membrane topology
    • Vergeres G., and Waskell L. Cytochrome b5, its functions, structure and membrane topology. Biochimie 77 (1995) 604-620
    • (1995) Biochimie , vol.77 , pp. 604-620
    • Vergeres, G.1    Waskell, L.2
  • 65
    • 0025767694 scopus 로고
    • A two component-type cytochrome P-450 monooxygenase system in a prokaryote that catalyzes hydroxylation of ML-236B to pravastatin, a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Serizawa N., and Matsuoka T. A two component-type cytochrome P-450 monooxygenase system in a prokaryote that catalyzes hydroxylation of ML-236B to pravastatin, a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Biochim. Biophys. Acta 1084 (1991) 35-40
    • (1991) Biochim. Biophys. Acta , vol.1084 , pp. 35-40
    • Serizawa, N.1    Matsuoka, T.2
  • 67
    • 3242730249 scopus 로고    scopus 로고
    • Crystal structure of P450cin in a complex with its substrate, 1,8-cineole, a close structural homologue to d-camphor, the substrate for P450cam
    • Meharenna Y.T., Li H., Hawkes D.B., Pearson A.G., De Voss J., and Poulos T.L. Crystal structure of P450cin in a complex with its substrate, 1,8-cineole, a close structural homologue to d-camphor, the substrate for P450cam. Biochemistry 43 (2004) 9487-9494
    • (2004) Biochemistry , vol.43 , pp. 9487-9494
    • Meharenna, Y.T.1    Li, H.2    Hawkes, D.B.3    Pearson, A.G.4    De Voss, J.5    Poulos, T.L.6
  • 68
    • 0025994649 scopus 로고
    • Expression and enzymatic activity of recombinant cytochrome P450 17 alpha-hydroxylase in Escherichia coli
    • Barnes H.J., Arlotto M.P., and Waterman M.R. Expression and enzymatic activity of recombinant cytochrome P450 17 alpha-hydroxylase in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 5597-5601
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 5597-5601
    • Barnes, H.J.1    Arlotto, M.P.2    Waterman, M.R.3
  • 69
    • 0028104977 scopus 로고
    • Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities
    • Jenkins C.M., and Waterman M.R. Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities. J. Biol. Chem. 269 (1994) 27401-27408
    • (1994) J. Biol. Chem. , vol.269 , pp. 27401-27408
    • Jenkins, C.M.1    Waterman, M.R.2
  • 71
    • 0034671777 scopus 로고    scopus 로고
    • Expression, purification, and characterization of BioI: A carbon-carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis
    • Stok J.E., and De Voss J. Expression, purification, and characterization of BioI: A carbon-carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis. Arch. Biochem. Biophys. 384 (2000) 351-360
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 351-360
    • Stok, J.E.1    De Voss, J.2
  • 72
    • 0029915099 scopus 로고    scopus 로고
    • Cloning of a potential cytochrome P450 from the archaeon Sulfolobus solfataricus
    • Wright R.L., Harris K., Solow B., White R.H., and Kennelly P.J. Cloning of a potential cytochrome P450 from the archaeon Sulfolobus solfataricus. FEBS Lett. 384 (1996) 235-239
    • (1996) FEBS Lett. , vol.384 , pp. 235-239
    • Wright, R.L.1    Harris, K.2    Solow, B.3    White, R.H.4    Kennelly, P.J.5
  • 75
    • 0032501058 scopus 로고    scopus 로고
    • Characterization of a cytochrome P450 from the acidothermophilic archaea Sulfolobus solfataricus
    • McLean M.A., Maves S.A., Weiss K.E., Krepich S., and Sligar S.G. Characterization of a cytochrome P450 from the acidothermophilic archaea Sulfolobus solfataricus. Biochem. Biophys. Res. Commun. 252 (1998) 166-172
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 166-172
    • McLean, M.A.1    Maves, S.A.2    Weiss, K.E.3    Krepich, S.4    Sligar, S.G.5
  • 76
    • 0034646311 scopus 로고    scopus 로고
    • Homology modeling, molecular dynamics simulations, and analysis of CYP119, a P450 enzyme from extreme acidothermophilic archaeon Sulfolobus solfataricus
    • Chang Y.T., and Loew G. Homology modeling, molecular dynamics simulations, and analysis of CYP119, a P450 enzyme from extreme acidothermophilic archaeon Sulfolobus solfataricus. Biochemistry 39 (2000) 2484-2498
    • (2000) Biochemistry , vol.39 , pp. 2484-2498
    • Chang, Y.T.1    Loew, G.2
  • 77
    • 0037145075 scopus 로고    scopus 로고
    • Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: high resolution structure and functional properties
    • Park S.Y., Yamane K., Adachi S., Shiro Y., Weiss K.E., Maves S.A., and Sligar S.G. Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: high resolution structure and functional properties. J. Inorg. Biochem. 91 (2002) 491-501
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 491-501
    • Park, S.Y.1    Yamane, K.2    Adachi, S.3    Shiro, Y.4    Weiss, K.E.5    Maves, S.A.6    Sligar, S.G.7
  • 78
    • 0034613190 scopus 로고    scopus 로고
    • Crystal structure of a thermophilic cytochrome P450 from the archaeon Sulfolobus solfataricus
    • Yano J.K., Koo L.S., Schuller D.J., Li H., Ortiz de Montellano P.R., and Poulos T.L. Crystal structure of a thermophilic cytochrome P450 from the archaeon Sulfolobus solfataricus. J. Biol. Chem. 275 (2000) 31086-31092
    • (2000) J. Biol. Chem. , vol.275 , pp. 31086-31092
    • Yano, J.K.1    Koo, L.S.2    Schuller, D.J.3    Li, H.4    Ortiz de Montellano, P.R.5    Poulos, T.L.6
  • 79
    • 0037223885 scopus 로고    scopus 로고
    • Aromatic stacking as a determinant of the thermal stability of CYP119 from Sulfolobus solfataricus
    • Puchkaev A.V., Koo L.S., and Ortiz de Montellano P.R. Aromatic stacking as a determinant of the thermal stability of CYP119 from Sulfolobus solfataricus. Arch. Biochem. Biophys. 409 (2003) 52-58
    • (2003) Arch. Biochem. Biophys. , vol.409 , pp. 52-58
    • Puchkaev, A.V.1    Koo, L.S.2    Ortiz de Montellano, P.R.3
  • 80
    • 0034823445 scopus 로고    scopus 로고
    • Reversible pressure deformation of a thermophilic cytochrome P450 enzyme (CYP119) and its active-site mutants
    • Tschirret-Guth R.A., Koo L.S., Hoa G.H., and Ortiz de Montellano P.R. Reversible pressure deformation of a thermophilic cytochrome P450 enzyme (CYP119) and its active-site mutants. J. Am. Chem. Soc. 123 (2001) 3412-3417
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3412-3417
    • Tschirret-Guth, R.A.1    Koo, L.S.2    Hoa, G.H.3    Ortiz de Montellano, P.R.4
  • 81
    • 0035721731 scopus 로고    scopus 로고
    • Role of a highly conserved YPITP motif in 2-oxoacid:ferredoxin oxidoreductase: Heterologous expression of the gene from Sulfolobus sp.strain 7, and characterization of the recombinant and variant enzymes
    • Fukuda E., Kino H., Matsuzawa H., and Wakagi T. Role of a highly conserved YPITP motif in 2-oxoacid:ferredoxin oxidoreductase: Heterologous expression of the gene from Sulfolobus sp.strain 7, and characterization of the recombinant and variant enzymes. Eur. J. Biochem. 268 (2001) 5639-5646
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5639-5646
    • Fukuda, E.1    Kino, H.2    Matsuzawa, H.3    Wakagi, T.4
  • 82
    • 0002012621 scopus 로고    scopus 로고
    • Zinc and an N-terminal extra stretch of the ferredoxin from a thermoacidophilic archaeon stabilize the molecule at high temperature
    • Kojoh K., Matsuzawa H., and Wakagi T. Zinc and an N-terminal extra stretch of the ferredoxin from a thermoacidophilic archaeon stabilize the molecule at high temperature. Eur. J. Biochem. 264 (1999) 85-91
    • (1999) Eur. J. Biochem. , vol.264 , pp. 85-91
    • Kojoh, K.1    Matsuzawa, H.2    Wakagi, T.3
  • 83
    • 11144270960 scopus 로고    scopus 로고
    • The Sulfolobus solfataricus electron donor partners of thermophilic CYP119: An unusual non-NAD(P)H-dependent cytochrome P450 system
    • Puchkaev A.V., and Ortiz de Montellano P.R. The Sulfolobus solfataricus electron donor partners of thermophilic CYP119: An unusual non-NAD(P)H-dependent cytochrome P450 system. Arch. Biochem. Biophys. 434 (2005) 169-177
    • (2005) Arch. Biochem. Biophys. , vol.434 , pp. 169-177
    • Puchkaev, A.V.1    Ortiz de Montellano, P.R.2
  • 84
    • 0037202185 scopus 로고    scopus 로고
    • CYP119 plus a Sulfolobus tokodaii strain 7 ferredoxin and 2-oxoacid:ferredoxin oxidoreductase constitute a high-temperature cytochrome P450 catalytic system
    • Puchkaev A.V., Wakagi T., and Ortiz de Montellano P.R. CYP119 plus a Sulfolobus tokodaii strain 7 ferredoxin and 2-oxoacid:ferredoxin oxidoreductase constitute a high-temperature cytochrome P450 catalytic system. J. Am. Chem. Soc. 124 (2002) 12682-12683
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 12682-12683
    • Puchkaev, A.V.1    Wakagi, T.2    Ortiz de Montellano, P.R.3
  • 85
    • 3042686713 scopus 로고    scopus 로고
    • Structure and direct electrochemistry of cytochrome P450 from the thermoacidophilic crenarchaeon, Sulfolobus tokodaii strain 7
    • Oku Y., Ohtaki A., Kamitori S., Nakamura N., Yohda M., Ohno H., and Kawarabayasi Y. Structure and direct electrochemistry of cytochrome P450 from the thermoacidophilic crenarchaeon, Sulfolobus tokodaii strain 7. J. Inorg. Biochem. 98 (2004) 1194-1199
    • (2004) J. Inorg. Biochem. , vol.98 , pp. 1194-1199
    • Oku, Y.1    Ohtaki, A.2    Kamitori, S.3    Nakamura, N.4    Yohda, M.5    Ohno, H.6    Kawarabayasi, Y.7
  • 86
    • 0347927627 scopus 로고    scopus 로고
    • Preliminary characterization and crystal structure of a thermostable cytochrome P450 from Thermus thermophilus
    • Yano J.K., Blasco F., Li H., Schmid R.D., Henne A., and Poulos T.L. Preliminary characterization and crystal structure of a thermostable cytochrome P450 from Thermus thermophilus. J. Biol. Chem. 278 (2003) 608-616
    • (2003) J. Biol. Chem. , vol.278 , pp. 608-616
    • Yano, J.K.1    Blasco, F.2    Li, H.3    Schmid, R.D.4    Henne, A.5    Poulos, T.L.6
  • 87
    • 3042607977 scopus 로고    scopus 로고
    • CYP175A1 from Thermus thermophilus HB27, the first beta-carotene hydroxylase of the P450 superfamily
    • Blasco F., Kauffmann I., and Schmid R.D. CYP175A1 from Thermus thermophilus HB27, the first beta-carotene hydroxylase of the P450 superfamily. Appl. Microbiol. Biotechnol. 64 (2004) 671-674
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 671-674
    • Blasco, F.1    Kauffmann, I.2    Schmid, R.D.3
  • 88
    • 0037032543 scopus 로고    scopus 로고
    • A novel sterol 14alpha-demethylase/ferredoxin fusion protein (MCCYP51FX) from Methylococcus capsulatus represents a new class of the cytochrome P450 superfamily
    • Jackson C.J., Lamb D.C., Marczylo T.H., Warrilow A.G., Manning N.J., Lowe D.J., Kelly D.E., and Kelly S.L. A novel sterol 14alpha-demethylase/ferredoxin fusion protein (MCCYP51FX) from Methylococcus capsulatus represents a new class of the cytochrome P450 superfamily. J. Biol. Chem. 277 (2002) 46959-46965
    • (2002) J. Biol. Chem. , vol.277 , pp. 46959-46965
    • Jackson, C.J.1    Lamb, D.C.2    Marczylo, T.H.3    Warrilow, A.G.4    Manning, N.J.5    Lowe, D.J.6    Kelly, D.E.7    Kelly, S.L.8
  • 89
    • 0033529797 scopus 로고    scopus 로고
    • Characterization and catalytic properties of the sterol 14alpha-demethylase from Mycobacterium tuberculosis
    • Bellamine A., Mangla A.T., Nes W.D., and Waterman M.R. Characterization and catalytic properties of the sterol 14alpha-demethylase from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 8937-8942
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 8937-8942
    • Bellamine, A.1    Mangla, A.T.2    Nes, W.D.3    Waterman, M.R.4
  • 90
    • 18044393406 scopus 로고    scopus 로고
    • MT FdR: A ferredoxin reductase from M. tuberculosis that couples to MT CYP51
    • Zanno A., Kwiatkowski N., Vaz A.D., and Guardiola-Diaz H.M. MT FdR: A ferredoxin reductase from M. tuberculosis that couples to MT CYP51. Biochim. Biophys. Acta 1707 (2005) 157-169
    • (2005) Biochim. Biophys. Acta , vol.1707 , pp. 157-169
    • Zanno, A.1    Kwiatkowski, N.2    Vaz, A.D.3    Guardiola-Diaz, H.M.4
  • 92
    • 0036795043 scopus 로고    scopus 로고
    • Cloning, sequencing, and characterization of the hexahydro-1,3,5-Trinitro-1,3,5-triazine degradation gene cluster from Rhodococcus rhodochrous
    • Seth-Smith H.M., Rosser S.J., Basran A., Travis E.R., Dabbs E.R., Nicklin S., and Bruce N.C. Cloning, sequencing, and characterization of the hexahydro-1,3,5-Trinitro-1,3,5-triazine degradation gene cluster from Rhodococcus rhodochrous. Appl. Environ. Microbiol. 68 (2002) 4764-4771
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 4764-4771
    • Seth-Smith, H.M.1    Rosser, S.J.2    Basran, A.3    Travis, E.R.4    Dabbs, E.R.5    Nicklin, S.6    Bruce, N.C.7
  • 93
    • 0036299635 scopus 로고    scopus 로고
    • Identification of a new class of cytochrome P450 from a Rhodococcus sp
    • Roberts G.A., Grogan G., Greter A., Flitsch S.L., and Turner N.J. Identification of a new class of cytochrome P450 from a Rhodococcus sp. J. Bacteriol. 184 (2002) 3898-3908
    • (2002) J. Bacteriol. , vol.184 , pp. 3898-3908
    • Roberts, G.A.1    Grogan, G.2    Greter, A.3    Flitsch, S.L.4    Turner, N.J.5
  • 95
    • 1542571790 scopus 로고    scopus 로고
    • A self-sufficient cytochrome p450 with a primary structural organization that includes a flavin domain and a [2Fe-2S] redox center
    • Roberts G.A., Celik A., Hunter D.J., Ost T.W., White J.H., Chapman S.K., Turner N.J., and Flitsch S.L. A self-sufficient cytochrome p450 with a primary structural organization that includes a flavin domain and a [2Fe-2S] redox center. J. Biol. Chem. 278 (2003) 48914-48920
    • (2003) J. Biol. Chem. , vol.278 , pp. 48914-48920
    • Roberts, G.A.1    Celik, A.2    Hunter, D.J.3    Ost, T.W.4    White, J.H.5    Chapman, S.K.6    Turner, N.J.7    Flitsch, S.L.8
  • 96
    • 0036844477 scopus 로고    scopus 로고
    • A novel class of self-sufficient cytochrome P450 monooxygenases in prokaryotes
    • De Mot R., and Parret A.H. A novel class of self-sufficient cytochrome P450 monooxygenases in prokaryotes. Trends Microbiol. 10 (2002) 502-508
    • (2002) Trends Microbiol. , vol.10 , pp. 502-508
    • De Mot, R.1    Parret, A.H.2
  • 97
    • 33846554933 scopus 로고    scopus 로고
    • L. Liu, R.D. Schmid, V.B. Urlacher, Cloning, expression, and characterization of a self-sufficient cytochrome P450 monooxygenase from Rhodococcus ruber DSM 44319., Appl. Microbiol. Biotechnol. (in press).
  • 99
    • 0016373637 scopus 로고
    • (Omega-2) hydroxylation of fatty acids by a soluble system from Bacillus megaterium
    • Miura Y., and Fulco A.J. (Omega-2) hydroxylation of fatty acids by a soluble system from Bacillus megaterium. J. Biol. Chem. 249 (1974) 1880-1888
    • (1974) J. Biol. Chem. , vol.249 , pp. 1880-1888
    • Miura, Y.1    Fulco, A.J.2
  • 100
    • 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
    • Ruettinger R.T., Wen L.P., and Fulco A.J. 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 (1989) 10987-10995
    • (1989) J. Biol. Chem. , vol.264 , pp. 10987-10995
    • Ruettinger, R.T.1    Wen, L.P.2    Fulco, A.J.3
  • 102
    • 0025922972 scopus 로고
    • P450BM-3 and other inducible bacterial P450 cytochromes: Biochemistry and regulation
    • Fulco A.J. P450BM-3 and other inducible bacterial P450 cytochromes: Biochemistry and regulation. Annu. Rev. Pharmacol. Toxicol. 31 (1991) 177-203
    • (1991) Annu. Rev. Pharmacol. Toxicol. , vol.31 , pp. 177-203
    • Fulco, A.J.1
  • 103
    • 0030057886 scopus 로고    scopus 로고
    • Probing electron transfer in flavocytochrome P-450 BM3 and its component domains
    • Munro A.W., Daff S., Coggins J.R., Lindsay J.G., and Chapman S.K. Probing electron transfer in flavocytochrome P-450 BM3 and its component domains. Eur. J. Biochem. 239 (1996) 403-409
    • (1996) Eur. J. Biochem. , vol.239 , pp. 403-409
    • Munro, A.W.1    Daff, S.2    Coggins, J.R.3    Lindsay, J.G.4    Chapman, S.K.5
  • 108
    • 0035210014 scopus 로고    scopus 로고
    • Fatty-acid-displaced transcriptional repressor, a conserved regulator of cytochrome P450 102 transcription in Bacillus species
    • Gustafsson M.C., Palmer C.N., Wolf C.R., and von Wachenfeldt C. Fatty-acid-displaced transcriptional repressor, a conserved regulator of cytochrome P450 102 transcription in Bacillus species. Arch. Microbiol. 176 (2001) 459-464
    • (2001) Arch. Microbiol. , vol.176 , pp. 459-464
    • Gustafsson, M.C.1    Palmer, C.N.2    Wolf, C.R.3    von Wachenfeldt, C.4
  • 109
    • 0034763568 scopus 로고    scopus 로고
    • Transcriptional regulation of the Bacillus subtilis bscR-CYP102A3 operon by the BscR repressor and differential induction of cytochrome CYP102A3 expression by oleic acid and palmitate
    • Lee T.R., Hsu H.P., and Shaw G.C. Transcriptional regulation of the Bacillus subtilis bscR-CYP102A3 operon by the BscR repressor and differential induction of cytochrome CYP102A3 expression by oleic acid and palmitate. J. Biochem. (Tokyo) 130 (2001) 569-574
    • (2001) J. Biochem. (Tokyo) , vol.130 , pp. 569-574
    • Lee, T.R.1    Hsu, H.P.2    Shaw, G.C.3
  • 110
    • 11244302709 scopus 로고    scopus 로고
    • Cloning, expression and characterisation of CYP102A2, a self-sufficient P450 monooxygenase from Bacillus subtilis
    • Budde M., Maurer S.C., Schmid R.D., and Urlacher V.B. Cloning, expression and characterisation of CYP102A2, a self-sufficient P450 monooxygenase from Bacillus subtilis. Appl. Microbiol. Biotechnol. 66 (2004) 180-186
    • (2004) Appl. Microbiol. Biotechnol. , vol.66 , pp. 180-186
    • Budde, M.1    Maurer, S.C.2    Schmid, R.D.3    Urlacher, V.B.4
  • 111
    • 32344437281 scopus 로고    scopus 로고
    • Altering the regioselectivity of cytochrome P450 CYP102A3 of Bacillus subtilis by using a new versatile assay system
    • Lentz O., Feenstra A., Habicher T., Hauer B., Schmid R.D., and Urlacher V.B. Altering the regioselectivity of cytochrome P450 CYP102A3 of Bacillus subtilis by using a new versatile assay system. ChemBioChem 7 (2006) 345-350
    • (2006) ChemBioChem , vol.7 , pp. 345-350
    • Lentz, O.1    Feenstra, A.2    Habicher, T.3    Hauer, B.4    Schmid, R.D.5    Urlacher, V.B.6
  • 112
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 113
    • 0029004590 scopus 로고
    • Protein modeling by E-mail
    • Peitsch M.C. Protein modeling by E-mail. Bio/Technology 13 (1995) 658-660
    • (1995) Bio/Technology , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 114
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede T., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL: An automated protein homology-modeling server. Nucleic Acids Res. 31 (2003) 3381-3385
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 115
    • 0031013972 scopus 로고    scopus 로고
    • The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid
    • Li H., and Poulos T.L. The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid. Nat. Struct. Biol. 4 (1997) 140-146
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 140-146
    • Li, H.1    Poulos, T.L.2
  • 117
    • 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. Fusarium oxysporum fatty-acid subterminal hydroxylase (CYP505) is a membrane-bound eukaryotic counterpart of Bacillus megaterium cytochrome P450BM3. J. Biol. Chem. 275 (2000) 39734-39740
    • (2000) J. Biol. Chem. , vol.275 , pp. 39734-39740
    • Kitazume, T.1    Takaya, N.2    Nakayama, N.3    Shoun, H.4
  • 118
    • 0029892430 scopus 로고    scopus 로고
    • Cytochrome P450foxy, a catalytically self-sufficient fatty acid hydroxylase of the fungus Fusarium oxysporum
    • Nakayama N., Takemae A., and Shoun H. Cytochrome P450foxy, a catalytically self-sufficient fatty acid hydroxylase of the fungus Fusarium oxysporum. J. Biochem. (Tokyo) 119 (1996) 435-440
    • (1996) J. Biochem. (Tokyo) , vol.119 , pp. 435-440
    • Nakayama, N.1    Takemae, A.2    Shoun, H.3
  • 119
    • 0036236942 scopus 로고    scopus 로고
    • Kinetic analysis of hydroxylation of saturated fatty acids by recombinant P450foxy produced by an Escherichia coli expression system
    • Kitazume T., Tanaka A., Takaya N., Nakamura A., Matsuyama S., Suzuki T., and Shoun H. Kinetic analysis of hydroxylation of saturated fatty acids by recombinant P450foxy produced by an Escherichia coli expression system. Eur. J. Biochem. 269 (2002) 2075-2082
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2075-2082
    • Kitazume, T.1    Tanaka, A.2    Takaya, N.3    Nakamura, A.4    Matsuyama, S.5    Suzuki, T.6    Shoun, H.7
  • 120
    • 25444445534 scopus 로고    scopus 로고
    • Genome-wide structural and evolutionary analysis of the P450 monooxygenase genes (P450ome) in the white rot fungus Phanerochaete chrysosporium: evidence for gene duplications and extensive gene clustering
    • Doddapaneni H., Chakraborty R., and Yadav J.S. Genome-wide structural and evolutionary analysis of the P450 monooxygenase genes (P450ome) in the white rot fungus Phanerochaete chrysosporium: evidence for gene duplications and extensive gene clustering. Genomics 6 (2005) 92
    • (2005) Genomics , vol.6 , pp. 92
    • Doddapaneni, H.1    Chakraborty, R.2    Yadav, J.S.3
  • 121
    • 0035573747 scopus 로고    scopus 로고
    • Characterization of four clustered and coregulated genes associated with fumonisin biosynthesis in Fusarium verticillioides
    • Seo J.A., Proctor R.H., and Plattner R.D. Characterization of four clustered and coregulated genes associated with fumonisin biosynthesis in Fusarium verticillioides. Fungal. Genet. Biol. 34 (2001) 155-165
    • (2001) Fungal. Genet. Biol. , vol.34 , pp. 155-165
    • Seo, J.A.1    Proctor, R.H.2    Plattner, R.D.3
  • 122
    • 0037373801 scopus 로고    scopus 로고
    • Co-expression of 15 contiguous genes delineates a fumonisin biosynthetic gene cluster in Gibberella moniliformis
    • Proctor R.H., Brown D.W., Plattner R.D., and Desjardins A.E. Co-expression of 15 contiguous genes delineates a fumonisin biosynthetic gene cluster in Gibberella moniliformis. Fungal Genet. Biol. 38 (2003) 237-249
    • (2003) Fungal Genet. Biol. , vol.38 , pp. 237-249
    • Proctor, R.H.1    Brown, D.W.2    Plattner, R.D.3    Desjardins, A.E.4
  • 123
    • 0025871374 scopus 로고
    • Nucleotide sequence of the unique nitrate/nitrite-inducible cytochrome P-450 cDNA from Fusarium oxysporum
    • Kizawa H., Tomura D., Oda M., Fukamizu A., Hoshino T., Gotoh O., Yasui T., and Shoun H. Nucleotide sequence of the unique nitrate/nitrite-inducible cytochrome P-450 cDNA from Fusarium oxysporum. J. Biol. Chem. 266 (1991) 10632-10637
    • (1991) J. Biol. Chem. , vol.266 , pp. 10632-10637
    • Kizawa, H.1    Tomura, D.2    Oda, M.3    Fukamizu, A.4    Hoshino, T.5    Gotoh, O.6    Yasui, T.7    Shoun, H.8
  • 124
    • 0033572625 scopus 로고    scopus 로고
    • Cytochrome P450nor, a novel class of mitochondrial cytochrome P450 involved in nitrate respiration in the fungus Fusarium oxysporum
    • Takaya N., Suzuki S., Kuwazaki S., Shoun H., Maruo F., Yamaguchi M., and Takeo K. Cytochrome P450nor, a novel class of mitochondrial cytochrome P450 involved in nitrate respiration in the fungus Fusarium oxysporum. Arch. Biochem. Biophys. 372 (1999) 340-346
    • (1999) Arch. Biochem. Biophys. , vol.372 , pp. 340-346
    • Takaya, N.1    Suzuki, S.2    Kuwazaki, S.3    Shoun, H.4    Maruo, F.5    Yamaguchi, M.6    Takeo, K.7
  • 125
    • 10444284194 scopus 로고    scopus 로고
    • Nitric oxide reductase (P450nor) from Fusarium oxysporum
    • Daiber A., Shoun H., and Ullrich V. Nitric oxide reductase (P450nor) from Fusarium oxysporum. J. Inorg. Biochem. 99 (2005) 185-193
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 185-193
    • Daiber, A.1    Shoun, H.2    Ullrich, V.3
  • 126
    • 0027418338 scopus 로고
    • Cytochrome P-450 55A1 (P-450dNIR) acts as nitric oxide reductase employing NADH as the direct electron donor
    • Nakahara K., Tanimoto T., Hatano K., Usuda K., and Shoun H. Cytochrome P-450 55A1 (P-450dNIR) acts as nitric oxide reductase employing NADH as the direct electron donor. J. Biol. Chem. 268 (1993) 8350-8355
    • (1993) J. Biol. Chem. , vol.268 , pp. 8350-8355
    • Nakahara, K.1    Tanimoto, T.2    Hatano, K.3    Usuda, K.4    Shoun, H.5
  • 127
    • 0030458981 scopus 로고    scopus 로고
    • Two isozymes of P450nor of Cylindrocarpon tonkinense: molecular cloning of the cDNAs and genes, expressions in the yeast, and the putative NAD(P)H-binding site
    • Kudo T., Tomura D., Liu D.L., Dai X.Q., and Shoun H. Two isozymes of P450nor of Cylindrocarpon tonkinense: molecular cloning of the cDNAs and genes, expressions in the yeast, and the putative NAD(P)H-binding site. Biochimie 78 (1996) 792-799
    • (1996) Biochimie , vol.78 , pp. 792-799
    • Kudo, T.1    Tomura, D.2    Liu, D.L.3    Dai, X.Q.4    Shoun, H.5
  • 128
    • 0034852729 scopus 로고    scopus 로고
    • Purification and cDNA cloning of nitric oxide reductase cytochrome P450nor (CYP55A4) from Trichosporon cutaneum
    • Zhang L., Takaya N., Kitazume T., Kondo T., and Shoun H. Purification and cDNA cloning of nitric oxide reductase cytochrome P450nor (CYP55A4) from Trichosporon cutaneum. Eur. J. Biochem. 268 (2001) 3198-3204
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3198-3204
    • Zhang, L.1    Takaya, N.2    Kitazume, T.3    Kondo, T.4    Shoun, H.5
  • 129
    • 0035144016 scopus 로고    scopus 로고
    • Tomato allene oxide synthase and fatty acid hydroperoxide lyase, two cytochrome P450s involved in oxylipin metabolism, are targeted to different membranes of chloroplast envelope
    • Froehlich J.E., Itoh A., and Howe G.A. Tomato allene oxide synthase and fatty acid hydroperoxide lyase, two cytochrome P450s involved in oxylipin metabolism, are targeted to different membranes of chloroplast envelope. Plant Physiol. 125 (2001) 306-317
    • (2001) Plant Physiol. , vol.125 , pp. 306-317
    • Froehlich, J.E.1    Itoh, A.2    Howe, G.A.3
  • 130
    • 0035793589 scopus 로고    scopus 로고
    • Molecular cloning of a divinyl ether synthase. Identification as a CYP74 cytochrome P-450
    • Itoh A., and Howe G.A. Molecular cloning of a divinyl ether synthase. Identification as a CYP74 cytochrome P-450. J. Biol. Chem. 276 (2001) 3620-3627
    • (2001) J. Biol. Chem. , vol.276 , pp. 3620-3627
    • Itoh, A.1    Howe, G.A.2
  • 131
    • 0027462555 scopus 로고
    • Low carbon monoxide affinity allene oxide synthase is the predominant cytochrome P450 in many plant tissues
    • Lau S.M., Harder P.A., and O'Keefe D.P. Low carbon monoxide affinity allene oxide synthase is the predominant cytochrome P450 in many plant tissues. Biochemistry 32 (1993) 1945-1950
    • (1993) Biochemistry , vol.32 , pp. 1945-1950
    • Lau, S.M.1    Harder, P.A.2    O'Keefe, D.P.3
  • 133
    • 0002082336 scopus 로고    scopus 로고
    • Jasmonic acid signaled responses in plants
    • Agrawal A., Tuzun S., and Bent E. (Eds), American Phytopathological Society Press, Minnesota
    • Staswick P., and Lehman C.C. Jasmonic acid signaled responses in plants. In: Agrawal A., Tuzun S., and Bent E. (Eds). Induced Plant Defenses Against Pathogens and Herbivores (1999), American Phytopathological Society Press, Minnesota 117-136
    • (1999) Induced Plant Defenses Against Pathogens and Herbivores , pp. 117-136
    • Staswick, P.1    Lehman, C.C.2
  • 134
    • 0001401384 scopus 로고
    • Evidence for the involvement of jasmonates and their octadecanoid precursors in the tendril coiling response of Bryonia dioica
    • Weiler E.W., Albrecht T., Groth B., Xia Z.Q., Luxem M., Liss A.L., and Spengler P. Evidence for the involvement of jasmonates and their octadecanoid precursors in the tendril coiling response of Bryonia dioica. Phytochemistry 32 (1993) 591-600
    • (1993) Phytochemistry , vol.32 , pp. 591-600
    • Weiler, E.W.1    Albrecht, T.2    Groth, B.3    Xia, Z.Q.4    Luxem, M.5    Liss, A.L.6    Spengler, P.7
  • 135
    • 0001371163 scopus 로고    scopus 로고
    • The critical requirement for linolenic acid is pollen development, not photosynthesis, in an arabidopsis mutant
    • McConn M., and Browse J. The critical requirement for linolenic acid is pollen development, not photosynthesis, in an arabidopsis mutant. Plant Cell. 8 (1996) 403-416
    • (1996) Plant Cell. , vol.8 , pp. 403-416
    • McConn, M.1    Browse, J.2
  • 136
    • 27544510764 scopus 로고    scopus 로고
    • Cellular and molecular biology of prostacyclin synthase
    • Wu K.K., and Liou J.Y. Cellular and molecular biology of prostacyclin synthase. Biochem. Biophys. Res. Commun. 338 (2005) 45-52
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 45-52
    • Wu, K.K.1    Liou, J.Y.2
  • 137
    • 0024494718 scopus 로고
    • On the mechanism of prostacyclin and thromboxane A2 biosynthesis
    • Hecker M., and Ullrich V. On the mechanism of prostacyclin and thromboxane A2 biosynthesis. J. Biol. Chem. 264 (1989) 141-150
    • (1989) J. Biol. Chem. , vol.264 , pp. 141-150
    • Hecker, M.1    Ullrich, V.2
  • 138
    • 0019420183 scopus 로고
    • Bovine endothelial cells in culture produce thromboxane as well as prostacyclin
    • Ingerman-Wojenski C., Silver M.J., Smith J.B., and Macarak E. Bovine endothelial cells in culture produce thromboxane as well as prostacyclin. J. Clin. Invest. 67 (1981) 1292-1296
    • (1981) J. Clin. Invest. , vol.67 , pp. 1292-1296
    • Ingerman-Wojenski, C.1    Silver, M.J.2    Smith, J.B.3    Macarak, E.4
  • 139
    • 0017094798 scopus 로고
    • An enzyme isolated from arteries transforms prostaglandin endoperoxides to an unstable substance that inhibits platelet aggregation
    • Moncada S., Gryglewski R., Bunting S., and Vane J.R. An enzyme isolated from arteries transforms prostaglandin endoperoxides to an unstable substance that inhibits platelet aggregation. Nature 263 (1976) 663-665
    • (1976) Nature , vol.263 , pp. 663-665
    • Moncada, S.1    Gryglewski, R.2    Bunting, S.3    Vane, J.R.4
  • 140
    • 0017749182 scopus 로고
    • Differential formation of prostacyclin (PGX or PGI2) by layers of the arterial wall. An explanation for the anti-thrombotic properties of vascular endothelium
    • Moncada S., Herman A.G., Higgs E.A., and Vane J.R. Differential formation of prostacyclin (PGX or PGI2) by layers of the arterial wall. An explanation for the anti-thrombotic properties of vascular endothelium. Thromb. Res. 11 (1977) 323-344
    • (1977) Thromb. Res. , vol.11 , pp. 323-344
    • Moncada, S.1    Herman, A.G.2    Higgs, E.A.3    Vane, J.R.4
  • 141
    • 0034096393 scopus 로고    scopus 로고
    • Distribution and cellular localization of prostacyclin synthase in human brain
    • Siegle I., Klein T., Zou M.H., Fritz P., and Komhoff M. Distribution and cellular localization of prostacyclin synthase in human brain. J. Histochem. Cytochem. 48 (2000) 631-641
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 631-641
    • Siegle, I.1    Klein, T.2    Zou, M.H.3    Fritz, P.4    Komhoff, M.5
  • 142
    • 0023140204 scopus 로고
    • Overview of physiological and pathophysiological effects of thromboxane A2
    • Ogletree M.L. Overview of physiological and pathophysiological effects of thromboxane A2. Fed. Proc. 46 (1987) 133-138
    • (1987) Fed. Proc. , vol.46 , pp. 133-138
    • Ogletree, M.L.1
  • 144
    • 0035978365 scopus 로고    scopus 로고
    • New physiological and pathophysiological aspects on the thromboxane A(2)-prostacyclin regulatory system
    • Ullrich V., Zou M.H., and Bachschmid M. New physiological and pathophysiological aspects on the thromboxane A(2)-prostacyclin regulatory system. Biochim. Biophys. Acta 1532 (2001) 1-14
    • (2001) Biochim. Biophys. Acta , vol.1532 , pp. 1-14
    • Ullrich, V.1    Zou, M.H.2    Bachschmid, M.3
  • 145
    • 0037228761 scopus 로고    scopus 로고
    • Enhanced heterologous expression of two Streptomyces griseolus cytochrome P450s and Streptomyces coelicolor ferredoxin reductase as potentially efficient hydroxylation catalysts
    • Hussain H.A., and Ward J.M. Enhanced heterologous expression of two Streptomyces griseolus cytochrome P450s and Streptomyces coelicolor ferredoxin reductase as potentially efficient hydroxylation catalysts. Appl. Environ. Microbiol. 69 (2003) 373-382
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 373-382
    • Hussain, H.A.1    Ward, J.M.2
  • 146
    • 14644429097 scopus 로고    scopus 로고
    • Kinetic and binding studies with purified recombinant proteins ferredoxin reductase, ferredoxin and cytochrome P450 comprising the morpholine mono-oxygenase from Mycobacterium sp. strain HE5
    • Sielaff B., and Andreesen J.R. Kinetic and binding studies with purified recombinant proteins ferredoxin reductase, ferredoxin and cytochrome P450 comprising the morpholine mono-oxygenase from Mycobacterium sp. strain HE5. FEBS J. 272 (2005) 1148-1159
    • (2005) FEBS J. , vol.272 , pp. 1148-1159
    • Sielaff, B.1    Andreesen, J.R.2
  • 147
    • 0036036620 scopus 로고    scopus 로고
    • P450(camr), a cytochrome P450 catalysing the stereospecific 6-endo-hydroxylation of (1 R)-(+)-camphor
    • Grogan G., Roberts G.A., Parsons S., Turner N.J., and Flitsch S.L. P450(camr), a cytochrome P450 catalysing the stereospecific 6-endo-hydroxylation of (1 R)-(+)-camphor. Appl. Microbiol. Biotechnol. 59 (2002) 449-454
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 449-454
    • Grogan, G.1    Roberts, G.A.2    Parsons, S.3    Turner, N.J.4    Flitsch, S.L.5
  • 148
    • 28144461935 scopus 로고    scopus 로고
    • Reconstitution of beta-carotene hydroxylase activity of thermostable CYP175A1 monooxygenase
    • Momoi K., Hofmann U., Schmid R.D., and Urlacher V.B. Reconstitution of beta-carotene hydroxylase activity of thermostable CYP175A1 monooxygenase. Biochem. Biophys. Res. Commun. 339 (2006) 331-336
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 331-336
    • Momoi, K.1    Hofmann, U.2    Schmid, R.D.3    Urlacher, V.B.4
  • 150
    • 32644472828 scopus 로고    scopus 로고
    • Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris
    • Bell S.G., Hoskins N., Xu F., Caprotti D., Rao Z., and Wong L.L. Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris. Biochem. Biophys. Res. Commun. 342 (2006) 191-196
    • (2006) Biochem. Biophys. Res. Commun. , vol.342 , pp. 191-196
    • Bell, S.G.1    Hoskins, N.2    Xu, F.3    Caprotti, D.4    Rao, Z.5    Wong, L.L.6
  • 151
    • 0026760514 scopus 로고
    • Reconstitution of cytochrome P4502B4 (LM2) activity with camphor and linalool monooxygenase electron donors
    • Bernhardt R., and Gunsalus I.C. Reconstitution of cytochrome P4502B4 (LM2) activity with camphor and linalool monooxygenase electron donors. Biochem. Biophys. Res. Commun. 187 (1992) 310-317
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 310-317
    • Bernhardt, R.1    Gunsalus, I.C.2
  • 152
    • 8744241642 scopus 로고    scopus 로고
    • EpoK, a cytochrome P450 involved in biosynthesis of the anticancer agents epothilones A and B. Substrate-mediated rescue of a P450 enzyme
    • Ogura H., Nishida C.R., Hoch U.R., Perera R., Dawson J.H., and Ortiz de Montellano P.R. EpoK, a cytochrome P450 involved in biosynthesis of the anticancer agents epothilones A and B. Substrate-mediated rescue of a P450 enzyme. Biochemistry 43 (2004) 14712-14721
    • (2004) Biochemistry , vol.43 , pp. 14712-14721
    • Ogura, H.1    Nishida, C.R.2    Hoch, U.R.3    Perera, R.4    Dawson, J.H.5    Ortiz de Montellano, P.R.6
  • 154
    • 23844515682 scopus 로고    scopus 로고
    • Analysis of the nearly identical morpholine monooxygenase-encoding mor genes from different Mycobacterium strains and characterization of the specific NADH : ferredoxin oxidoreductase of this cytochrome P450 system
    • Sielaff B., and Andreesen J.R. Analysis of the nearly identical morpholine monooxygenase-encoding mor genes from different Mycobacterium strains and characterization of the specific NADH : ferredoxin oxidoreductase of this cytochrome P450 system. Microbiology 151 (2005) 2593-2603
    • (2005) Microbiology , vol.151 , pp. 2593-2603
    • Sielaff, B.1    Andreesen, J.R.2
  • 155
    • 0034892705 scopus 로고    scopus 로고
    • A cytochrome P450 and a ferredoxin isolated from Mycobacterium sp. strain HE5 after growth on morpholine
    • Sielaff B., Andreesen J.R., and Schrader T. A cytochrome P450 and a ferredoxin isolated from Mycobacterium sp. strain HE5 after growth on morpholine. Appl. Microbiol. Biotechnol. 56 (2001) 458-464
    • (2001) Appl. Microbiol. Biotechnol. , vol.56 , pp. 458-464
    • Sielaff, B.1    Andreesen, J.R.2    Schrader, T.3
  • 156
    • 33744821345 scopus 로고    scopus 로고
    • Design of an Escherichia coli system for whole cell mediated steroid synthesis and molecular evolution of steroid hydroxylases
    • Hannemann F., Virus C., and Bernhardt R. Design of an Escherichia coli system for whole cell mediated steroid synthesis and molecular evolution of steroid hydroxylases. J. Biotechnol. 124 (2006) 172-181
    • (2006) J. Biotechnol. , vol.124 , pp. 172-181
    • Hannemann, F.1    Virus, C.2    Bernhardt, R.3
  • 158
    • 0018801058 scopus 로고
    • Purification and characterization of cytochrome P-450meg
    • Berg A., Ingelman-Sundberg M., and Gustafsson J.A. Purification and characterization of cytochrome P-450meg. J. Biol. Chem. 254 (1979) 5264-5271
    • (1979) J. Biol. Chem. , vol.254 , pp. 5264-5271
    • Berg, A.1    Ingelman-Sundberg, M.2    Gustafsson, J.A.3
  • 159
    • 0017295461 scopus 로고
    • Autooxidation and hydroxylation reactions of oxygenated cytochrome P-450cam
    • Lipscomb J.D., Sligar S.G., Namtvedt M.J., and Gunsalus I.C. Autooxidation and hydroxylation reactions of oxygenated cytochrome P-450cam. J. Biol. Chem. 251 (1976) 1116-1124
    • (1976) J. Biol. Chem. , vol.251 , pp. 1116-1124
    • Lipscomb, J.D.1    Sligar, S.G.2    Namtvedt, M.J.3    Gunsalus, I.C.4
  • 160
    • 0037133263 scopus 로고    scopus 로고
    • Functional expression of human mitochondrial CYP11B2 in fission yeast and identification of a new internal electron transfer protein, etp1
    • Bureik M., Schiffler B., Hiraoka Y., Vogel F., and Bernhardt R. Functional expression of human mitochondrial CYP11B2 in fission yeast and identification of a new internal electron transfer protein, etp1. Biochemistry 41 (2002) 2311-2321
    • (2002) Biochemistry , vol.41 , pp. 2311-2321
    • Bureik, M.1    Schiffler, B.2    Hiraoka, Y.3    Vogel, F.4    Bernhardt, R.5
  • 162
    • 0037157130 scopus 로고    scopus 로고
    • Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119
    • Koo L.S., Immoos C.E., Cohen M.S., Farmer P.J., and Ortiz de Montellano P.R. Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119. J. Am. Chem. Soc. 124 (2002) 5684-5691
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5684-5691
    • Koo, L.S.1    Immoos, C.E.2    Cohen, M.S.3    Farmer, P.J.4    Ortiz de Montellano, P.R.5
  • 163
    • 15944383707 scopus 로고    scopus 로고
    • Coexpression in yeast of Taxus cytochrome P450 reductase with cytochrome P450 oxygenases involved in Taxol biosynthesis
    • Jennewein S., Park H., DeJong J.M., Long R.M., Bollon A.P., and Croteau R.B. Coexpression in yeast of Taxus cytochrome P450 reductase with cytochrome P450 oxygenases involved in Taxol biosynthesis. Biotechnol. Bioeng. 89 (2005) 588-598
    • (2005) Biotechnol. Bioeng. , vol.89 , pp. 588-598
    • Jennewein, S.1    Park, H.2    DeJong, J.M.3    Long, R.M.4    Bollon, A.P.5    Croteau, R.B.6
  • 164
    • 27244462209 scopus 로고    scopus 로고
    • Reconstitution of the enzymatic activities of cytochrome P450s using recombinant flavocytochromes containing rat cytochrome b(5) fused to NADPH-cytochrome P450 reductase with various membrane-binding segments
    • Gilep A.A., Guryev O.L., Usanov S.A., and Estabrook R.W. Reconstitution of the enzymatic activities of cytochrome P450s using recombinant flavocytochromes containing rat cytochrome b(5) fused to NADPH-cytochrome P450 reductase with various membrane-binding segments. Arch. Biochem. Biophys. 390 (2001) 215-221
    • (2001) Arch. Biochem. Biophys. , vol.390 , pp. 215-221
    • Gilep, A.A.1    Guryev, O.L.2    Usanov, S.A.3    Estabrook, R.W.4
  • 165
    • 0032813363 scopus 로고    scopus 로고
    • Engineering and biochemical characterization of the rat microsomal cytochrome P4501A1 fused to ferredoxin and ferredoxin-NADP(+) reductase from plant chloroplasts
    • Lacour T., and Ohkawa H. Engineering and biochemical characterization of the rat microsomal cytochrome P4501A1 fused to ferredoxin and ferredoxin-NADP(+) reductase from plant chloroplasts. Biochim. Biophys. Acta 1433 (1999) 87-102
    • (1999) Biochim. Biophys. Acta , vol.1433 , pp. 87-102
    • Lacour, T.1    Ohkawa, H.2
  • 166
    • 0027311918 scopus 로고
    • Construction and function of fusion enzymes of the human cytochrome P450scc system
    • Harikrishna J.A., Black S.M., Szklarz G.D., and Miller W.L. Construction and function of fusion enzymes of the human cytochrome P450scc system. DNA Cell Biol. 12 (1993) 371-379
    • (1993) DNA Cell Biol. , vol.12 , pp. 371-379
    • Harikrishna, J.A.1    Black, S.M.2    Szklarz, G.D.3    Miller, W.L.4
  • 167
    • 0343920070 scopus 로고    scopus 로고
    • Construction and characterization of a catalytic fusion protein system: P-450(11beta)-adrenodoxin reductase-adrenodoxin
    • Cao P.R., Bulow H., Dumas B., and Bernhardt R. Construction and characterization of a catalytic fusion protein system: P-450(11beta)-adrenodoxin reductase-adrenodoxin. Biochim. Biophys. Acta 1476 (2000) 253-264
    • (2000) Biochim. Biophys. Acta , vol.1476 , pp. 253-264
    • Cao, P.R.1    Bulow, H.2    Dumas, B.3    Bernhardt, R.4
  • 168
    • 32644461918 scopus 로고    scopus 로고
    • Functional expression system for cytochrome P450 genes using the reductase domain of self-sufficient P450RhF from Rhodococcus sp. NCIMB 9784
    • Nodate M., Kubota M., and Misawa N. Functional expression system for cytochrome P450 genes using the reductase domain of self-sufficient P450RhF from Rhodococcus sp. NCIMB 9784. Appl. Microbiol. Biotechnol. (2005) 1-8
    • (2005) Appl. Microbiol. Biotechnol. , pp. 1-8
    • Nodate, M.1    Kubota, M.2    Misawa, N.3
  • 172
    • 0034296561 scopus 로고    scopus 로고
    • Expression of human cytochromes P450 1A1 and P450 1A2 as fused enzymes with yeast NADPH-cytochrome P450 oxidoreductase in transgenic tobacco plants
    • Shiota N., Kodama S., Inui H., and Ohkawa H. Expression of human cytochromes P450 1A1 and P450 1A2 as fused enzymes with yeast NADPH-cytochrome P450 oxidoreductase in transgenic tobacco plants. Biosci. Biotechnol. Biochem. 64 (2000) 2025-2033
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 2025-2033
    • Shiota, N.1    Kodama, S.2    Inui, H.3    Ohkawa, H.4
  • 174
    • 0033072740 scopus 로고    scopus 로고
    • An introduction to the cytochrome P450s
    • Estabrook R. An introduction to the cytochrome P450s. Mol. Aspects Med. 20 (1999) 5-137
    • (1999) Mol. Aspects Med. , vol.20 , pp. 5-137
    • Estabrook, R.1
  • 175
    • 0037306331 scopus 로고    scopus 로고
    • The many roles of cytochrome b5
    • Schenkman J.B., and Jansson I. The many roles of cytochrome b5. Pharmacol. Ther. 97 (2003) 139-152
    • (2003) Pharmacol. Ther. , vol.97 , pp. 139-152
    • Schenkman, J.B.1    Jansson, I.2
  • 176
    • 0029784085 scopus 로고    scopus 로고
    • 2-oxoacid:ferredoxin oxidoreductase from the thermoacidophilic archaeon. Sulfolobus sp. strain 7
    • Zhang Q., Iwasaki T., Wakagi T., and Oshima T. 2-oxoacid:ferredoxin oxidoreductase from the thermoacidophilic archaeon. Sulfolobus sp. strain 7. J. Biochem. (Tokyo) 120 (1996) 587-599
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 587-599
    • Zhang, Q.1    Iwasaki, T.2    Wakagi, T.3    Oshima, T.4
  • 177
    • 0036669427 scopus 로고    scopus 로고
    • Thromboxane synthase: structure and function of protein and gene
    • Wang L.-H., and Kulmacz R.J. Thromboxane synthase: structure and function of protein and gene. Prostaglandins Other Lipid Mediat. 68-69 (2002) 409-422
    • (2002) Prostaglandins Other Lipid Mediat. , vol.68-69 , pp. 409-422
    • Wang, L.-H.1    Kulmacz, R.J.2
  • 178
    • 0036669428 scopus 로고    scopus 로고
    • Hydroperoxide lyase and divinyl ether synthase
    • Grechkin A.N. Hydroperoxide lyase and divinyl ether synthase. Prostaglandins Other Lipid Mediat. 68-69 (2002) 457-470
    • (2002) Prostaglandins Other Lipid Mediat. , vol.68-69 , pp. 457-470
    • Grechkin, A.N.1


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