메뉴 건너뛰기




Volumn 99, Issue 6, 2005, Pages 577-585

Gene cloning and characterization of Mycobacterium phlei flavin reductase involved in dibenzothiophene desulfurization

Author keywords

Desulfurization; Dibenzothiophene; Ferric reductase; Flavin reductase; Mycobacterium phlei

Indexed keywords

AMINO ACIDS; BACTERIA; BACTERIOLOGY; CELLS; DESULFURIZATION; ENZYMES; THERMAL EFFECTS;

EID: 27644446409     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1263/jbb.99.577     Document Type: Article
Times cited : (15)

References (41)
  • 5
    • 0035205486 scopus 로고    scopus 로고
    • Reduced flavin: Donor and acceptor enzymes and mechanisms of channeling
    • Tu, S.-C.: Reduced flavin: donor and acceptor enzymes and mechanisms of channeling. Antioxid. Redox Signal., 3, 881-897 (2001).
    • (2001) Antioxid. Redox Signal. , vol.3 , pp. 881-897
    • Tu, S.-C.1
  • 6
    • 0342514774 scopus 로고    scopus 로고
    • Functional analysis of the small component of the 4-hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: A prototype of a new flavin:NAD(P)H reductase subfamily
    • Galán, B., Díaz, E., Prieto, M. A., and García, J. L.: Functional analysis of the small component of the 4-hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: a prototype of a new flavin:NAD(P)H reductase subfamily. J. Bacteriol., 182, 627-636 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 627-636
    • Galán, B.1    Díaz, E.2    Prieto, M.A.3    García, J.L.4
  • 7
    • 0036843901 scopus 로고    scopus 로고
    • Biochemistry, genetics and physiology of microbial styrene degradation
    • O'Leary, N. D., O'Connor, K. E., and Dobson, A. D. W.: Biochemistry, genetics and physiology of microbial styrene degradation. FEMS Microbiol. Rev., 26, 403-417 (2002).
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 403-417
    • O'Leary, N.D.1    O'Connor, K.E.2    Dobson, A.D.W.3
  • 8
    • 0346220289 scopus 로고    scopus 로고
    • Phenol hydroxylase from Bacillus thermoglucosidasius A7: A two-protein component monooxygenase with a dual role for FAD
    • Kirchner, U., Westphal, A. H., Müller, R., and van Berkel, W. J. H.: Phenol hydroxylase from Bacillus thermoglucosidasius A7: a two-protein component monooxygenase with a dual role for FAD. J. Biol. Chem., 278, 47545-47553 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 47545-47553
    • Kirchner, U.1    Westphal, A.H.2    Müller, R.3    Van Berkel, W.J.H.4
  • 9
    • 0030697519 scopus 로고    scopus 로고
    • Two-component flavin-dependent pyrrole-2-carboxylate monooxygenase from Rhodococcus sp
    • Becker, D., Schrader, T., and Andreesen, J. R.: Two-component flavin-dependent pyrrole-2-carboxylate monooxygenase from Rhodococcus sp. Eur. J. Biochem., 249, 739-747 (1997).
    • (1997) Eur. J. Biochem. , vol.249 , pp. 739-747
    • Becker, D.1    Schrader, T.2    Andreesen, J.R.3
  • 10
    • 0026532662 scopus 로고
    • Purification and characterization of a two-component monooxygenase that hydroxylates nitrilotriacetate from "Chelatobacter" strain ATCC 29600
    • Uetz, T., Schneider, R., Snozzi, M., and Egli, T.: Purification and characterization of a two-component monooxygenase that hydroxylates nitrilotriacetate from "Chelatobacter" strain ATCC 29600. J. Bacteriol., 174, 1179-1188 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 1179-1188
    • Uetz, T.1    Schneider, R.2    Snozzi, M.3    Egli, T.4
  • 11
    • 0030728465 scopus 로고    scopus 로고
    • Identification and characterization of the two-enzyme system catalyzing oxidation of EDTA in the EDTA-degrading bacterial strain DSM 9103
    • Witschel, M., Nagel, S., and Egli, T.: Identification and characterization of the two-enzyme system catalyzing oxidation of EDTA in the EDTA-degrading bacterial strain DSM 9103. J. Bacteriol., 179, 6937-6943 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 6937-6943
    • Witschel, M.1    Nagel, S.2    Egli, T.3
  • 13
    • 0031104980 scopus 로고    scopus 로고
    • Purification and characterization of isobutylamine N-hydroxylase from the valanimycin producer Streptomyces viridifaciens MG456-hF10
    • Parry, R. J. and Li, W.: Purification and characterization of isobutylamine N-hydroxylase from the valanimycin producer Streptomyces viridifaciens MG456-hF10. Arch. Biochem. Biophys., 339, 47-54 (1997).
    • (1997) Arch. Biochem. Biophys. , vol.339 , pp. 47-54
    • Parry, R.J.1    Li, W.2
  • 14
    • 0034600905 scopus 로고    scopus 로고
    • Purification and partial characterization of tryptophan 7-halogenase (PrnA) from Pseudomonas fluorescens
    • Keller, S., Wage, T., Hohaus, K., Hölzer, M., Eichhorn, E., and van Pee, K-H.: Purification and partial characterization of tryptophan 7-halogenase (PrnA) from Pseudomonas fluorescens. Angew. Chem. Int. Ed., 39, 2300-2302 (2000).
    • (2000) Angew. Chem. Int. Ed. , vol.39 , pp. 2300-2302
    • Keller, S.1    Wage, T.2    Hohaus, K.3    Hölzer, M.4    Eichhorn, E.5    Van Pee, K.-H.6
  • 15
    • 0036330524 scopus 로고    scopus 로고
    • Biodesulfurization of naphthothiophene and benzothiophene through selective cleavage of carbon-sulfur bonds by Rhodococcus sp. strain WU-K2R
    • Kirimura, K., Furuya, T., Sato, R., Ishii, Y., Kino, K., and Usami, S.: Biodesulfurization of naphthothiophene and benzothiophene through selective cleavage of carbon-sulfur bonds by Rhodococcus sp. strain WU-K2R. Appl. Environ. Microbiol., 68, 3867-3872 (2002).
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3867-3872
    • Kirimura, K.1    Furuya, T.2    Sato, R.3    Ishii, Y.4    Kino, K.5    Usami, S.6
  • 16
    • 0033635712 scopus 로고    scopus 로고
    • Biodesulfurization and the upgrading of petroleum distillates
    • Monticello, D. J.: Biodesulfurization and the upgrading of petroleum distillates. Curr. Opin. Biotechnol., 11, 540-546 (2000).
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 540-546
    • Monticello, D.J.1
  • 17
    • 0035055057 scopus 로고    scopus 로고
    • Biodesulfurization of dibenzothiophene and its derivatives through the selective cleavage of carbon-sulfur bonds by a moderately thermophilic bacterium Bacillus subtilis WU-S2B
    • Kirimura, K., Furuya, T., Nishii, Y., Ishii, Y., Kino, K., and Usami, S.: Biodesulfurization of dibenzothiophene and its derivatives through the selective cleavage of carbon-sulfur bonds by a moderately thermophilic bacterium Bacillus subtilis WU-S2B. J. Biosci. Bioeng., 91, 262-266 (2001).
    • (2001) J. Biosci. Bioeng. , vol.91 , pp. 262-266
    • Kirimura, K.1    Furuya, T.2    Nishii, Y.3    Ishii, Y.4    Kino, K.5    Usami, S.6
  • 18
    • 0347423247 scopus 로고    scopus 로고
    • Desulfurization of fossil fuels
    • Bitton, G. (ed.). Wiley and Sons, New York
    • Ohshiro, T. and Izumi, Y.: Desulfurization of fossil fuels, p. 1041-1051. In Bitton, G. (ed.), Encyclopedia of environmental microbiology, vol.II. Wiley and Sons, New York (2002).
    • (2002) Encyclopedia of Environmental Microbiology , vol.2 , pp. 1041-1051
    • Ohshiro, T.1    Izumi, Y.2
  • 19
    • 0030763260 scopus 로고    scopus 로고
    • Elucidation of the metabolic pathway for dibenzothiophene desulfurization by Rhodococcus sp. IGTS8 (ATCC53968)
    • Oldfield, C., Pogrebinsky, O., Simmonds, J., Olson, E. S., and Kulpa, C. F.: Elucidation of the metabolic pathway for dibenzothiophene desulfurization by Rhodococcus sp. IGTS8 (ATCC53968). Microbiology, 143, 2961-2973 (1997).
    • (1997) Microbiology , vol.143 , pp. 2961-2973
    • Oldfield, C.1    Pogrebinsky, O.2    Simmonds, J.3    Olson, E.S.4    Kulpa, C.F.5
  • 20
    • 0345802687 scopus 로고    scopus 로고
    • Cloning of a gene encoding flavin reductase coupling with dibenzothiophene monooxygenase through coexpression screening using indigo production as selective indication
    • Furuya, T., Takahashi, S., Ishii, Y., Kino, K., and Kirimura, K.: Cloning of a gene encoding flavin reductase coupling with dibenzothiophene monooxygenase through coexpression screening using indigo production as selective indication. Biochem. Biophys. Res. Commun., 313, 570-575 (2004).
    • (2004) Biochem. Biophys. Res. Commun. , vol.313 , pp. 570-575
    • Furuya, T.1    Takahashi, S.2    Ishii, Y.3    Kino, K.4    Kirimura, K.5
  • 22
    • 0037432724 scopus 로고    scopus 로고
    • Thermophilic biodesulfurization of hydrodesulfurized light gas oils by Mycobacterium phlei WU-F1
    • Furuya, T., Ishii, Y., Noda, K., Kino, K., and Kirimura, K.: Thermophilic biodesulfurization of hydrodesulfurized light gas oils by Mycobacterium phlei WU-F1. FEMS Microbiol. Lett., 221, 137-142 (2003).
    • (2003) FEMS Microbiol. Lett. , vol.221 , pp. 137-142
    • Furuya, T.1    Ishii, Y.2    Noda, K.3    Kino, K.4    Kirimura, K.5
  • 23
    • 0036158703 scopus 로고    scopus 로고
    • Thermophilic biodesulfurization of naphthothiophene and 2-ethylnaphthothiophene by dibenzothiophene-desulfurizing bacterium, Mycobacterium phlei WU-F1
    • Furuya, T., Kirimura, K., Kino, K., and Usami, S.: Thermophilic biodesulfurization of naphthothiophene and 2-ethylnaphthothiophene by dibenzothiophene-desulfurizing bacterium, Mycobacterium phlei WU-F1. Appl. Microbiol. Biotechnol., 58, 237-240 (2002).
    • (2002) Appl. Microbiol. Biotechnol. , vol.58 , pp. 237-240
    • Furuya, T.1    Kirimura, K.2    Kino, K.3    Usami, S.4
  • 24
    • 0035899927 scopus 로고    scopus 로고
    • Thermophilic biodesulfurization of dibenzothiophene and its derivatives by Mycobacterium phlei WU-F1
    • Furuya, T., Kirimura, K., Kino, K., and Usami, S.: Thermophilic biodesulfurization of dibenzothiophene and its derivatives by Mycobacterium phlei WU-F1. FEMS Microbiol. Lett., 204, 129-133 (2001).
    • (2001) FEMS Microbiol. Lett. , vol.204 , pp. 129-133
    • Furuya, T.1    Kirimura, K.2    Kino, K.3    Usami, S.4
  • 25
    • 5144225412 scopus 로고    scopus 로고
    • Identification and function analysis of the genes encoding dibenzothiophene-desulfurizing enzymes from thermophilic bacteria
    • Kirimura, K., Harada, K., Iwasawa, H., Tanaka, T., Iwasaki, Y., Furuya, T., Ishii, Y., and Kino, K.: Identification and function analysis of the genes encoding dibenzothiophene-desulfurizing enzymes from thermophilic bacteria. Appl. Microbiol. Biotechnol., 65, 703-713 (2004).
    • (2004) Appl. Microbiol. Biotechnol. , vol.65 , pp. 703-713
    • Kirimura, K.1    Harada, K.2    Iwasawa, H.3    Tanaka, T.4    Iwasaki, Y.5    Furuya, T.6    Ishii, Y.7    Kino, K.8
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M.: A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 31
    • 0033579438 scopus 로고    scopus 로고
    • Identification and characterization of a novel ferric reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus
    • Vadas, A., Monbouquette, H. G, Johnson, E., and Schröder, I.: Identification and characterization of a novel ferric reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus. J. Biol. Chem., 274, 36715-36721 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 36715-36721
    • Vadas, A.1    Monbouquette, H.G.2    Johnson, E.3    Schröder, I.4
  • 33
    • 0033967890 scopus 로고    scopus 로고
    • Characterization of 4-hydroxyphenylacetate 3-hydroxygenase (HpaB) of Escherichia coli as a reduced flavin adenine dinucleotide-utilizing monooxygenase
    • Xun, L. and Sandvik, E. R.: Characterization of 4-hydroxyphenylacetate 3-hydroxygenase (HpaB) of Escherichia coli as a reduced flavin adenine dinucleotide-utilizing monooxygenase. Appl. Environ. Microbiol., 66, 481-486 (2000).
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 481-486
    • Xun, L.1    Sandvik, E.R.2
  • 34
    • 0036384898 scopus 로고    scopus 로고
    • Flavin reductase coupling with two monooxygenases involved in dibenzothiophene desulfurization: Purification and characterization from a non-desulfurizing bacterium, Paenibacillus polymyxa A-1
    • Ohshiro, T., Aoi, Y., Torii, K., and Izumi, Y.: Flavin reductase coupling with two monooxygenases involved in dibenzothiophene desulfurization: purification and characterization from a non-desulfurizing bacterium, Paenibacillus polymyxa A-1. Appl. Microbiol. Biotechnol., 59, 649-657 (2002).
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 649-657
    • Ohshiro, T.1    Aoi, Y.2    Torii, K.3    Izumi, Y.4
  • 35
    • 4644291654 scopus 로고    scopus 로고
    • Thermostable flavin reductase that couples with dibenzothiophene monooxygenase, from thermophilic Bacillus sp. DSM411: Purification, characterization and gene cloning
    • Ohshiro, T., Yamada, H., Shimoda, T., Matsubara, T., and Izumi, Y.: Thermostable flavin reductase that couples with dibenzothiophene monooxygenase, from thermophilic Bacillus sp. DSM411: purification, characterization and gene cloning. Biosci. Biotechnol. Biochem., 68, 1712-1721 (2004).
    • (2004) Biosci. Biotechnol. Biochem. , vol.68 , pp. 1712-1721
    • Ohshiro, T.1    Yamada, H.2    Shimoda, T.3    Matsubara, T.4    Izumi, Y.5
  • 36
    • 0031550218 scopus 로고    scopus 로고
    • A flavin reductase stimulates DszA and DszC proteins of Rhodococcus erythropolis IGTS8 in vitro
    • Xi, L., Squires, C. H., Monticello, D. J., and Childs, J. D.: A flavin reductase stimulates DszA and DszC proteins of Rhodococcus erythropolis IGTS8 in vitro. Biochem. Biophys. Res. Commun., 230, 73-75 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 73-75
    • Xi, L.1    Squires, C.H.2    Monticello, D.J.3    Childs, J.D.4
  • 37
    • 0027996697 scopus 로고
    • Characterization of the desulfurization genes from Rhodococcus sp. strain IGTS8
    • Denome, S. A., Oldfield, C., Nash, L. J., and Young, K. D.: Characterization of the desulfurization genes from Rhodococcus sp. strain IGTS8. J. Bacteriol., 176, 6707-6716 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 6707-6716
    • Denome, S.A.1    Oldfield, C.2    Nash, L.J.3    Young, K.D.4
  • 38
    • 0035289693 scopus 로고    scopus 로고
    • Purification, characterization, and overexpression of flavin reductase involved in dibenzothiophene desulfurization by Rhodococcus erythropolis D-1
    • Matsubara, T., Ohshiro, T., Nishina, Y., and Izumi, Y.: Purification, characterization, and overexpression of flavin reductase involved in dibenzothiophene desulfurization by Rhodococcus erythropolis D-1. Appl. Environ. Microbiol., 67, 1179-1184 (2001).
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 1179-1184
    • Matsubara, T.1    Ohshiro, T.2    Nishina, Y.3    Izumi, Y.4
  • 39
    • 0037414756 scopus 로고    scopus 로고
    • Mechanism and substrate specificity of the flavin reductase ActVB from Streptomyces coelicolor
    • Filisetti, L., Fontecave, M., and Nivière, V.: Mechanism and substrate specificity of the flavin reductase ActVB from Streptomyces coelicolor. J. Biol. Chem., 278, 296-303 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 296-303
    • Filisetti, L.1    Fontecave, M.2    Nivière, V.3
  • 41
    • 0031908540 scopus 로고    scopus 로고
    • Identification and characterization of a novel extracellular ferrie reductase from Mycobacterium paratuberculosis
    • Homuth, M., Valentin-Weigand, P., Rohde, M., and Gerlach, G.-F.: Identification and characterization of a novel extracellular ferrie reductase from Mycobacterium paratuberculosis. Infect. Immun., 66, 710-716 (1998).
    • (1998) Infect. Immun. , vol.66 , pp. 710-716
    • Homuth, M.1    Valentin-Weigand, P.2    Rohde, M.3    Gerlach, G.-F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.