메뉴 건너뛰기




Volumn 360, Issue 3, 2007, Pages 666-672

P450 enzymes from the bacterium Novosphingobium aromaticivorans

Author keywords

Electron transfer; Monooxygenases; Novosphingobium aromaticivorans; P450 enzymes; Substrate specificity

Indexed keywords

CYTOCHROME P450; POLYCYCLIC AROMATIC HYDROCARBON; PUTIDAREDOXIN;

EID: 34447268241     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.06.119     Document Type: Article
Times cited : (59)

References (22)
  • 1
    • 0025847131 scopus 로고
    • Isolation and characterization of a subsurface bacterium capable of growth on toluene, naphthalene, and other aromatic compounds
    • Fredrickson J.K., Brockman F.J., Workman D.J., Li S.W., and Stevens T.O. Isolation and characterization of a subsurface bacterium capable of growth on toluene, naphthalene, and other aromatic compounds. Appl. Environ. Microbiol. 57 (1991) 796-803
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 796-803
    • Fredrickson, J.K.1    Brockman, F.J.2    Workman, D.J.3    Li, S.W.4    Stevens, T.O.5
  • 3
    • 33645460847 scopus 로고    scopus 로고
    • Ortiz de Montellano P.R. (Ed), Kluwer Academic/Plenum Publishers, New York
    • In: Ortiz de Montellano P.R. (Ed). Cytochrome P450: Structure, Mechanism, and Biochemistry (2005), Kluwer Academic/Plenum Publishers, New York
    • (2005) Cytochrome P450: Structure, Mechanism, and Biochemistry
  • 4
    • 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
  • 6
    • 33745177792 scopus 로고    scopus 로고
    • Cytochrome P450 nomenclature, 2004
    • Nelson D.R. Cytochrome P450 nomenclature, 2004. Methods Mol. Biol. 320 (2006) 1-10
    • (2006) Methods Mol. Biol. , vol.320 , pp. 1-10
    • Nelson, D.R.1
  • 8
    • 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
  • 10
    • 0024208742 scopus 로고
    • The roles of active site hydrogen bonding in cytochrome P-450cam as revealed by site-directed mutagenesis
    • Atkins W.M., and Sligar S.G. The roles of active site hydrogen bonding in cytochrome P-450cam as revealed by site-directed mutagenesis. J. Biol. Chem. 263 (1988) 18842-18849
    • (1988) J. Biol. Chem. , vol.263 , pp. 18842-18849
    • Atkins, W.M.1    Sligar, S.G.2
  • 11
    • 0022271371 scopus 로고
    • P450cam gene cloning and expression in Pseudomonas putida and Escherichia coli
    • Koga H., Rauchfuss B., and Gunsalus I.C. P450cam gene cloning and expression in Pseudomonas putida and Escherichia coli. Biochem. Biophys. Res. Commun. 130 (1985) 412-417
    • (1985) Biochem. Biophys. Res. Commun. , vol.130 , pp. 412-417
    • Koga, H.1    Rauchfuss, B.2    Gunsalus, I.C.3
  • 14
    • 0027267603 scopus 로고
    • Cloning and expression of a member of a new cytochrome P-450 family: cytochrome P-450lin (CYP111) from Pseudomonas incognita
    • Ropp J.D., Gunsalus I.C., and Sligar S.G. Cloning and expression of a member of a new cytochrome P-450 family: cytochrome P-450lin (CYP111) from Pseudomonas incognita. J. Bacteriol. 175 (1993) 6028-6037
    • (1993) J. Bacteriol. , vol.175 , pp. 6028-6037
    • Ropp, J.D.1    Gunsalus, I.C.2    Sligar, S.G.3
  • 15
    • 19144369096 scopus 로고    scopus 로고
    • Substrate-induced gene-expression screening of environmental metagenome libraries for isolation of catabolic genes
    • Uchiyama T., Abe T., Ikemura T., and Watanabe K. Substrate-induced gene-expression screening of environmental metagenome libraries for isolation of catabolic genes. Nat. Biotechnol. 23 (2005) 88-93
    • (2005) Nat. Biotechnol. , vol.23 , pp. 88-93
    • Uchiyama, T.1    Abe, T.2    Ikemura, T.3    Watanabe, K.4
  • 16
    • 33846473252 scopus 로고    scopus 로고
    • Cytochrome P450 systems-biological variations of electron transport chains
    • Hannemann F., Bichet A., Ewen K.M., and Bernhardt R. Cytochrome P450 systems-biological variations of electron transport chains. Biochim. Biophys. Acta 1770 (2007) 330-344
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 330-344
    • Hannemann, F.1    Bichet, A.2    Ewen, K.M.3    Bernhardt, R.4
  • 17
    • 0037145071 scopus 로고    scopus 로고
    • Specific and non-specific effects of potassium cations on substrate-protein interactions in cytochromes P450cam and P450lin
    • Deprez E., Gill E., Helms V., Wade R.C., and Hui Bon Hoa G. Specific and non-specific effects of potassium cations on substrate-protein interactions in cytochromes P450cam and P450lin. J. Inorg. Biochem. 91 (2002) 597-606
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 597-606
    • Deprez, E.1    Gill, E.2    Helms, V.3    Wade, R.C.4    Hui Bon Hoa, G.5
  • 18
    • 0033230093 scopus 로고    scopus 로고
    • Mutations of glutamate-84 at the putative potassium-binding site affect camphor binding and oxidation by cytochrome p450cam
    • Westlake A.C., Harford-Cross C.F., Donovan J., and Wong L.L. 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
  • 20
    • 0032980919 scopus 로고    scopus 로고
    • The thermodynamics and kinetics of electron transfer in the cytochrome P450cam enzyme system
    • Honeychurch M.J., Hill H.A.O., and Wong L.L. 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
  • 21
    • 33845379583 scopus 로고
    • Control of heme protein redox potential and reduction rate: linear free energy relation between potential and ferric spin state equilibrium
    • Fisher M.T., and Sligar S.G. Control of heme protein redox potential and reduction rate: linear free energy relation between potential and ferric spin state equilibrium. J. Am. Chem. Soc. 107 (1985) 5018-5019
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 5018-5019
    • Fisher, M.T.1    Sligar, S.G.2
  • 22
    • 0001127948 scopus 로고
    • A thermodynamic model of regulation: modulation of redox equilibria in camphor monooxygenase
    • Sligar S.G., and Gunsalus I.C. A thermodynamic model of regulation: modulation of redox equilibria in camphor monooxygenase. PNAS 73 (1976) 1078-1082
    • (1976) PNAS , vol.73 , pp. 1078-1082
    • Sligar, S.G.1    Gunsalus, I.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.