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Volumn 579, Issue 10, 2005, Pages 2215-2220

Analysis of the domain properties of the novel cytochrome P450 RhF

Author keywords

2Fe 2S; Cytochrome P450; Flavin; Monooxygenase; Reduction potential; Rhodococcus

Indexed keywords

CYTOCHROME P450; CYTOCHROME P450 RHF; FERREDOXIN; FLAVINE MONONUCLEOTIDE; HEME; IMIDAZOLE; UNCLASSIFIED DRUG;

EID: 16344368644     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.03.016     Document Type: Article
Times cited : (52)

References (22)
  • 1
    • 0023061373 scopus 로고
    • P450 genes: Structure, evolution and regulation
    • D.W. Nebert, and F.J. Gonzalez P450 genes: structure, evolution and regulation Ann. Rev. Biochem. 56 1987 945 993
    • (1987) Ann. Rev. Biochem. , vol.56 , pp. 945-993
    • Nebert, D.W.1    Gonzalez, F.J.2
  • 2
    • 0022878676 scopus 로고
    • Characterization of a catalytically self-sufficient 119 000-Da cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium
    • L.O. Narhi, and A.J. Fulco Characterization of a catalytically self-sufficient 119 000-Da 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
  • 5
    • 0036844477 scopus 로고    scopus 로고
    • A novel class of self-sufficient cytochrome P450 monooxygenases in prokaryotes
    • R. De Mot, and A.H.A. Parret 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.A.2
  • 7
    • 0034671918 scopus 로고    scopus 로고
    • Fusarium oxysporum fatty-acid subterminal hydroxylase (CYP505) is a membrane-bound eukaryotic counterpart of Bacillus megaterium cytochrome P450BM3
    • T. Kitazume, N. Takaya, N. Nakayama, and H. Shoun 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
  • 8
    • 0035573747 scopus 로고    scopus 로고
    • Characterization of four clustered and coregulated genes associated with fumonisin biosynthesis in Fusarium verticillioides
    • J.-A. Seo, R.H. Proctor, and R.D. Plattner 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
  • 9
    • 0037032543 scopus 로고    scopus 로고
    • A novel sterol 14α-demethylase/ferredoxin fusion protein (MCCYP51FX) from Methylococcus capsulatus represents a new class of the cytochrome P450 superfamily
    • C.J. Jackson, D.C. Lamb, T.H. Marczylo, A.G.S. Warrilow, N.J. Manning, D.J Lowe, D.E. Kelly, and S.L. Kelly A novel sterol 14α-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.S.4    Manning, N.J.5    Lowe, D.J.6    Kelly, D.E.7    Kelly, S.L.8
  • 10
    • 0036795043 scopus 로고    scopus 로고
    • Cloning, sequencing, and characterisation of the hexahydro-1,3,5- trinitro-1,3,5-triazine degradation gene cluster from Rhodococcus rhodocrous
    • H.M.B. Seth-Smith, S.J. Rosser, A. Basran, E.R. Travis, E.R. Dabbs, S. Nicklin, and N.C. Bruce Cloning, sequencing, and characterisation of the hexahydro-1,3,5-trinitro-1,3,5-triazine degradation gene cluster from Rhodococcus rhodocrous Appl. Environ. Microbiol. 68 2002 4764 4771
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 4764-4771
    • Seth-Smith, H.M.B.1    Rosser, S.J.2    Basran, A.3    Travis, E.R.4    Dabbs, E.R.5    Nicklin, S.6    Bruce, N.C.7
  • 11
    • 0036299635 scopus 로고    scopus 로고
    • Identification of a new class of cytochrome P450 from a Rhodococcus sp.
    • G.A. Roberts, G. Grogan, A. Greter, S.L. Flitsch, and N.J. Turner 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
  • 12
    • 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
    • G.A. Roberts, A. Celik, D.J.B. Hunter, T.W.B. Ost, J.W. White, S.K. Chapman, N.J. Turner, and S.L. Flitsch 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.B.3    Ost, T.W.B.4    White, J.W.5    Chapman, S.K.6    Turner, N.J.7    Flitsch, S.L.8
  • 13
    • 0028950304 scopus 로고
    • Degradation of the thiocarbamate herbicide EPTC (S-ethyl dipropylcarbamothioate) and biosafening by Rhodococcus sp. strain NI86/21 involve an inducible cytochrome P-450 system and aldehyde dehydrogenase
    • I. Nagy, G. Schoofs, F. Compernolle, P. Proost, J. Vanderleyden, and R. De Mot Degradation of the thiocarbamate herbicide EPTC (S-ethyl dipropylcarbamothioate) and biosafening by Rhodococcus sp. strain NI86/21 involve an inducible cytochrome P-450 system and aldehyde dehydrogenase J. Bacteriol. 177 1995 676 687
    • (1995) J. Bacteriol. , vol.177 , pp. 676-687
    • Nagy, I.1    Schoofs, G.2    Compernolle, F.3    Proost, P.4    Vanderleyden, J.5    De Mot, R.6
  • 14
    • 33750622183 scopus 로고
    • Cytochromes: Bacterial
    • R.G. Bartsch Cytochromes: bacterial Methods Enzymol. 23 1971 344 347
    • (1971) Methods Enzymol. , vol.23 , pp. 344-347
    • Bartsch, R.G.1
  • 15
    • 0032619605 scopus 로고    scopus 로고
    • UV-vis spectroscopy as a tool to study flavoproteins
    • Methods in Molecular Biology S.K. Chapman G.R. Reid Humana Press Totowa, NJ
    • P. Macheroux UV-vis spectroscopy as a tool to study flavoproteins Methods in Molecular Biology S.K. Chapman G.R. Reid Flavoprotein Protocols 131 1999 Humana Press Totowa, NJ 1 7
    • (1999) Flavoprotein Protocols , vol.131 , pp. 1-7
    • MacHeroux, P.1
  • 16
    • 0035957239 scopus 로고    scopus 로고
    • Activation of class III ribonucleotide reductase by flavodoxin: A protein radical-driven electron transfer to the iron-sulfur center
    • E. Mulliez, D. Padovani, M. Atta, C. Alcouffe, and M. Fontecave Activation of class III ribonucleotide reductase by flavodoxin: a protein radical-driven electron transfer to the iron-sulfur center Biochemistry 40 2001 3730 3736
    • (2001) Biochemistry , vol.40 , pp. 3730-3736
    • Mulliez, E.1    Padovani, D.2    Atta, M.3    Alcouffe, C.4    Fontecave, M.5
  • 17
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • P. Schuck Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling Biophys. J. 78 2000 1606 1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 18
    • 0034654352 scopus 로고    scopus 로고
    • A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions
    • J.S. Philo A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions Anal. Biochem. 279 2000 151 163
    • (2000) Anal. Biochem. , vol.279 , pp. 151-163
    • Philo, J.S.1
  • 20
    • 0028792364 scopus 로고
    • Structure and mechanism of the iron-sulfur flavoprotein phthalate dioxygenase reductase
    • G.T. Gassner, M.L. Ludwig, D.L. Gatti, C.C. Correll, and D.P. Ballou Structure and mechanism of the iron-sulfur flavoprotein phthalate dioxygenase reductase FASEB J. 9 1995 1411 1418
    • (1995) FASEB J. , vol.9 , pp. 1411-1418
    • Gassner, G.T.1    Ludwig, M.L.2    Gatti, D.L.3    Correll, C.C.4    Ballou, D.P.5
  • 21
    • 0028874558 scopus 로고
    • Preparation and characterization of a truncated form of phthalate dioxygenase reductase that lacks an iron-sulfur domain
    • G.T. Gassner, and D.P. Ballou Preparation and characterization of a truncated form of phthalate dioxygenase reductase that lacks an iron-sulfur domain Biochemistry 34 1995 13460 13471
    • (1995) Biochemistry , vol.34 , pp. 13460-13471
    • Gassner, G.T.1    Ballou, D.P.2
  • 22
    • 0142063412 scopus 로고    scopus 로고
    • Reduction potentials of Rieske clusters: Importance of the coupling between oxidation state and histidine protonation state
    • Y. Zu, M.M.-J. Couture, D.R.J Kolling, A.R. Crofts, L.D. Eltis, J.A. Fee, and J. Hirst Reduction potentials of Rieske clusters: importance of the coupling between oxidation state and histidine protonation state Biochemistry 42 2003 12400 12408
    • (2003) Biochemistry , vol.42 , pp. 12400-12408
    • Zu, Y.1    Couture, M.M.-J.2    Kolling, R.J.3    Crofts, A.R.4    Eltis, L.D.5    Fee, J.A.6    Hirst, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.