메뉴 건너뛰기




Volumn 342, Issue 1, 2006, Pages 191-196

Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris

Author keywords

Electron transfer; Monooxygenases; P450 enzymes; Rhodopseudomonas palustris; Substrate specificity

Indexed keywords

4 HYDROXYBENZOIC ACID; BACTERIAL ENZYME; BENZALDEHYDE; BENZENE; BENZOIC ACID; CYTOCHROME P450; CYTOCHROME P450 153A5; CYTOCHROME P450 195A2; CYTOCHROME P450 203A1; CYTOCHROME P450 A99A2; FERREDOXIN; OXIDOREDUCTASE; PALUSTRISREDOXIN A ENZYME; PHENOL; PUTIDAREDOXIN; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

EID: 32644472828     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.01.133     Document Type: Article
Times cited : (66)

References (28)
  • 1
    • 0015190808 scopus 로고
    • Catabolism of aromatic compounds by microorganisms
    • S. Dagley Catabolism of aromatic compounds by microorganisms Adv. Microb. Physiol. 6 1971 1 46
    • (1971) Adv. Microb. Physiol. , vol.6 , pp. 1-46
    • Dagley, S.1
  • 2
    • 0023971827 scopus 로고
    • Anaerobic and aerobic metabolism of diverse aromatic compounds by the photosynthetic bacterium Rhodopseudomonas palustris
    • C.S. Harwood, and J. Gibson Anaerobic and aerobic metabolism of diverse aromatic compounds by the photosynthetic bacterium Rhodopseudomonas palustris Appl. Environ. Microbiol. 54 1988 712 717
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 712-717
    • Harwood, C.S.1    Gibson, J.2
  • 3
    • 0018896524 scopus 로고
    • Phototrophic growth on citrate and regulations of citrate lyase in three strains of Rhodopseudomonas palustris
    • F. Giffhorn, and A. Kuhn Phototrophic growth on citrate and regulations of citrate lyase in three strains of Rhodopseudomonas palustris FEMS Microbiol. Lett. 7 1980 225 228
    • (1980) FEMS Microbiol. Lett. , vol.7 , pp. 225-228
    • Giffhorn, F.1    Kuhn, A.2
  • 4
    • 2442480590 scopus 로고    scopus 로고
    • Degradation of aromatic substances by a marine photosynthetic bacterium Rhodopseudomonas palustris (KK1)
    • N. Elangovan, P.S.S. Gandhi, T. Kumaran, and P.T. Kalaichelvan Degradation of aromatic substances by a marine photosynthetic bacterium Rhodopseudomonas palustris (KK1) Ind. J. Environ. Protect. 20 2000 366 371
    • (2000) Ind. J. Environ. Protect. , vol.20 , pp. 366-371
    • Elangovan, N.1    Gandhi, P.S.S.2    Kumaran, T.3    Kalaichelvan, P.T.4
  • 6
    • 0033287587 scopus 로고    scopus 로고
    • Nature's universal oxygenases: The cytochromes P450
    • S.G. Sligar Nature's universal oxygenases: the cytochromes P450 Essays Biochem. 34 1999 71 83
    • (1999) Essays Biochem. , vol.34 , pp. 71-83
    • Sligar, S.G.1
  • 9
    • 0034973773 scopus 로고    scopus 로고
    • Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity
    • F.P. Guengerich 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
  • 10
    • 0041513426 scopus 로고    scopus 로고
    • Reactions catalyzed by bacterial cytochromes P 450
    • M.J. Cryle, J.E. Stok, and J.J. De Voss Reactions catalyzed by bacterial cytochromes P 450 Aust. J. Chem. 56 2003 749 762
    • (2003) Aust. J. Chem. , vol.56 , pp. 749-762
    • Cryle, M.J.1    Stok, J.E.2    De Voss, J.J.3
  • 11
    • 20544472150 scopus 로고    scopus 로고
    • Tributyl phosphate degradation by Rhodopseudomonas palustris and other photosynthetic bacteria
    • C. Berne, B. Allainmat, and D. Garcia Tributyl phosphate degradation by Rhodopseudomonas palustris and other photosynthetic bacteria Biotechnol. Lett. 27 2005 561 566
    • (2005) Biotechnol. Lett. , vol.27 , pp. 561-566
    • Berne, C.1    Allainmat, B.2    Garcia, D.3
  • 13
    • 0036844477 scopus 로고    scopus 로고
    • A novel class of self-sufficient cytochrome P450 monooxygenases in prokaryotes
    • R. De Mot, and A.H. 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.2
  • 14
    • 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. Hunter, T.W. Ost, J.H. 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.3    Ost, T.W.4    White, J.H.5    Chapman, S.K.6    Turner, N.J.7    Flitsch, S.L.8
  • 15
    • 0000350777 scopus 로고
    • Twenty-five years of P450cam research. Mechanistic insights into oxygenase catalysis
    • P.R. Ortiz de Montellano Plenum Press New York
    • E.J. Mueller, P.J. Loida, and S.G. Sligar Twenty-five years of P450cam research. Mechanistic insights into oxygenase catalysis P.R. Ortiz de Montellano Cytochrome P450: Structure, Mechanism, and Biochemistry 1995 Plenum Press New York 83 124
    • (1995) Cytochrome P450: Structure, Mechanism, and Biochemistry , pp. 83-124
    • Mueller, E.J.1    Loida, P.J.2    Sligar, S.G.3
  • 16
    • 0025257597 scopus 로고
    • Putidaredoxin reductase and putidaredoxin-cloning, sequence determination, and heterologous expression of the proteins
    • J.A. Peterson, M.C. Lorence, and B. Amarneh 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
  • 17
    • 0034801865 scopus 로고    scopus 로고
    • Molecular characterization of the 56-kDa CYP153 from Acinetobacter sp. EB104
    • T. Maier, H.H. Forster, O. Asperger, and U. Hahn Molecular characterization of the 56-kDa CYP153 from Acinetobacter sp. EB104 Biochem. Biophys. Res. Commun. 286 2001 652 658
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 652-658
    • Maier, T.1    Forster, H.H.2    Asperger, O.3    Hahn, U.4
  • 18
    • 20444375861 scopus 로고    scopus 로고
    • Expanding the alkane oxygenase toolbox: New enzymes and applications
    • J.B. van Beilen, and E.G. Funhoff Expanding the alkane oxygenase toolbox: new enzymes and applications Curr. Opin. Biotechnol. 16 2005 308 314
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 308-314
    • Van Beilen, J.B.1    Funhoff, E.G.2
  • 19
    • 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
    • J.B. van Beilen, R. Holtackers, D. Luscher, U. Bauer, B. Witholt, and W.A. Duetz 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
  • 20
    • 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
    • M. Nodate, M. Kubota, and N. Misawa 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
  • 21
    • 84886603628 scopus 로고
    • P-450 hemeproteins of Rhizobium japonicum. Purification by affinity chromatography and relationship to P-450CAM and P-450LM-2
    • K. Dus, R. Goewert, C.C. Weaver, D. Carey, and C.A. Appleby P-450 hemeproteins of Rhizobium japonicum. Purification by affinity chromatography and relationship to P-450CAM and P-450LM-2 Biochem. Biophys. Res. Commun. 69 1976 437 445
    • (1976) Biochem. Biophys. Res. Commun. , vol.69 , pp. 437-445
    • Dus, K.1    Goewert, R.2    Weaver, C.C.3    Carey, D.4    Appleby, C.A.5
  • 22
    • 0016837969 scopus 로고
    • Involvement of oxyleghemoglobin and cytochrome P 450 in an efficient oxidative phosphorylation pathway which supports nitrogen fixation in Rhizobium
    • C.A. Appleby, G.L. Turner, and P.K. Macnicol Involvement of oxyleghemoglobin and cytochrome P 450 in an efficient oxidative phosphorylation pathway which supports nitrogen fixation in Rhizobium Biochim. Biophys. Acta 387 1975 461 474
    • (1975) Biochim. Biophys. Acta , vol.387 , pp. 461-474
    • Appleby, C.A.1    Turner, G.L.2    MacNicol, P.K.3
  • 25
    • 0028277594 scopus 로고
    • Effects of monovalent cations on cytochrome P-450 camphor. Evidence for preferential binding of potassium
    • E. Deprez, C. Di Primo, G.H. Hoa, and P. Douzou Effects of monovalent cations on cytochrome P-450 camphor. Evidence for preferential binding of potassium FEBS Lett. 347 1994 207 210
    • (1994) FEBS Lett. , vol.347 , pp. 207-210
    • Deprez, E.1    Di Primo, C.2    Hoa, G.H.3    Douzou, P.4
  • 26
    • 0033230093 scopus 로고    scopus 로고
    • Mutations of glutamate-84 at the putative potassium-binding site affect camphor binding and oxidation by cytochrome P450cam
    • A.C. Westlake, C.F. Harford-Cross, J. Donovan, and L.L. Wong Mutations of glutamate-84 at the putative potassium-binding site affect camphor binding and oxidation by cytochrome P450cam Eur. J. Biochem. 265 1999 929 935
    • (1999) Eur. J. Biochem. , vol.265 , pp. 929-935
    • Westlake, A.C.1    Harford-Cross, C.F.2    Donovan, J.3    Wong, L.L.4
  • 27
    • 0032980919 scopus 로고    scopus 로고
    • The thermodynamics and kinetics of electron transfer in the cytochrome P450cam enzyme system
    • M.J. Honeychurch, H.A.O. Hill, and L.L. Wong The thermodynamics and kinetics of electron transfer in the cytochrome P450cam enzyme system FEBS Lett. 451 1999 351 353
    • (1999) FEBS Lett. , vol.451 , pp. 351-353
    • Honeychurch, M.J.1    Hill, H.A.O.2    Wong, L.L.3
  • 28
    • 0026442895 scopus 로고
    • Genetic-variants in the putidaredoxin cytochrome P450cam electron-transfer complex-Identification of the residue responsible for redox-state-dependent conformers
    • M.D. Davies, and S.G. Sligar Genetic-variants in the putidaredoxin cytochrome P450cam electron-transfer complex-Identification of the residue responsible for redox-state-dependent conformers Biochemistry 31 1992 11383 11389
    • (1992) Biochemistry , vol.31 , pp. 11383-11389
    • Davies, M.D.1    Sligar, S.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.