메뉴 건너뛰기




Volumn 45, Issue 23, 2006, Pages 7083-7091

Characterization of a thermostable NADPH:FMN oxidoreductase from the mesophilic bacterium Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; MELTING; OLIGOMERS; OXIDATION; POLYMERIZATION;

EID: 33745044453     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052478r     Document Type: Article
Times cited : (49)

References (25)
  • 1
    • 0035205486 scopus 로고    scopus 로고
    • Reduced flavin: Donor and acceptor enzymes and mechanisms of channeling
    • Tu, S.-C. (2001) Reduced flavin: Donor and acceptor enzymes and mechanisms of channeling, Antioxid. Redox Signaling 3, 881-897.
    • (2001) Antioxid. Redox Signaling , vol.3 , pp. 881-897
    • Tu, S.-C.1
  • 2
    • 0002117840 scopus 로고
    • DT-diaphorase, a quinone reductase with special functions in cell metabolism and detoxication
    • Ernster, L., Estabrook, R. W., Hochstein, P., and Orrenius, S. (1987) DT-diaphorase, a quinone reductase with special functions in cell metabolism and detoxication, Chem. Scr. 27A, 1-207.
    • (1987) Chem. Scr. , vol.27 , pp. 1-207
    • Ernster, L.1    Estabrook, R.W.2    Hochstein, P.3    Orrenius, S.4
  • 4
    • 0035937804 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of the gene coding for azoreductase from Bacillus sp. OY1-2 isolated from soil
    • Suzuki, Y., Yoda, T., Ruhul, A., and Sugiura, W. (2001) Molecular cloning and characterisation of the gene coding for azoreductase from Bacillus sp. OY1-2 isolated from soil, J. Biol. Chem. 276, 9059-9065.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9059-9065
    • Suzuki, Y.1    Yoda, T.2    Ruhul, A.3    Sugiura, W.4
  • 5
    • 1642354143 scopus 로고    scopus 로고
    • Molecular cloning, overexpression, purification, and characterization of an aerobic FMN-dependent azoreductase from Enterococcus faecalis
    • Chen, H., Wang, R.-F., and Cerniglia, C. E. (2004) Molecular cloning, overexpression, purification, and characterization of an aerobic FMN-dependent azoreductase from Enterococcus faecalis, Protein Expression Purif. 34, 302-310.
    • (2004) Protein Expression Purif. , vol.34 , pp. 302-310
    • Chen, H.1    Wang, R.-F.2    Cerniglia, C.E.3
  • 6
    • 0035824553 scopus 로고    scopus 로고
    • Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase
    • Nakanishi, M., Yatome, C., Ishida, N., and Kitade, Y. (2001) Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase, J. Biol. Chem. 276, 46394-46399.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46394-46399
    • Nakanishi, M.1    Yatome, C.2    Ishida, N.3    Kitade, Y.4
  • 7
    • 0043164772 scopus 로고    scopus 로고
    • Cloning and characterization of the gene coding for the aerobic azoreductase from Pigmentiphaga kullae K24
    • Blümel, S., and Stolz, A. (2003) Cloning and characterization of the gene coding for the aerobic azoreductase from Pigmentiphaga kullae K24, Appl. Microbiol. Biotechnol. 62, 186-190.
    • (2003) Appl. Microbiol. Biotechnol. , vol.62 , pp. 186-190
    • Blümel, S.1    Stolz, A.2
  • 8
    • 3042578045 scopus 로고    scopus 로고
    • Expression and characteristics of the gene encoding azoreductase from Rhodobacter sphaeroides AS1.1737
    • Bin, Y., Jiti, Z., Jing, W., Cuihong, D., Hongman, H., Zhiyong, S., and Yongming, B. (2004) Expression and characteristics of the gene encoding azoreductase from Rhodobacter sphaeroides AS1.1737, FEMS Microbiol. Lett. 236, 129-136.
    • (2004) FEMS Microbiol. Lett. , vol.236 , pp. 129-136
    • Bin, Y.1    Jiti, Z.2    Jing, W.3    Cuihong, D.4    Hongman, H.5    Zhiyong, S.6    Yongming, B.7
  • 9
    • 19044389145 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of an azoreductase from Staphylococcus aureus, a tetrameric NADPH-dependent flavoprotein
    • Chen, H., Hopper, S. L., and Cerniglia, C. E. (2005) Biochemical and molecular characterization of an azoreductase from Staphylococcus aureus, a tetrameric NADPH-dependent flavoprotein, Microbiology 151, 1433-1441.
    • (2005) Microbiology , vol.151 , pp. 1433-1441
    • Chen, H.1    Hopper, S.L.2    Cerniglia, C.E.3
  • 10
    • 0036324837 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the gene coding for the aerobic azoreductase from Xenophilus azovorans KF46F
    • Blümel, S., Knackmuss, H.-J., and Stolz, A. (2002) Molecular cloning and characterization of the gene coding for the aerobic azoreductase from Xenophilus azovorans KF46F, Appl. Environm. Microbiol. 68, 3948-3955.
    • (2002) Appl. Environm. Microbiol. , vol.68 , pp. 3948-3955
    • Blümel, S.1    Knackmuss, H.-J.2    Stolz, A.3
  • 12
    • 4544232470 scopus 로고    scopus 로고
    • Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities
    • Liger, D., Graille, M., Zhou, C-Z., Leulliot, N., Quevillon-Cheruel, S., Blondeau, K., Janin, J., and van Tilbeurgh, H. (2004) Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities, J. Biol. Chem. 279, 34890-34897.
    • (2004) J. Biol. Chem. , vol.279 , pp. 34890-34897
    • Liger, D.1    Graille, M.2    Zhou, C.-Z.3    Leulliot, N.4    Quevillon-Cheruel, S.5    Blondeau, K.6    Janin, J.7    Van Tilbeurgh, H.8
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0030646652 scopus 로고    scopus 로고
    • A microoptode array for fine-scale measurement of oxygen distribution
    • Holst, G., Glud, R. N., Kuhl, M., and Klimant, I. (1997) A microoptode array for fine-scale measurement of oxygen distribution, Sens. Actuators, B 38, 122-129.
    • (1997) Sens. Actuators, B , vol.38 , pp. 122-129
    • Holst, G.1    Glud, R.N.2    Kuhl, M.3    Klimant, I.4
  • 16
    • 0034737320 scopus 로고    scopus 로고
    • The crystal structure of dihydrofolate reductase from Thermotoga maritima: Molecular features of thermostability
    • Dams, T., Auerbach, G., Bader, G., Jacob, U., Ploom, T., Huber, R., and Jaenicke, R. (2000) The crystal structure of dihydrofolate reductase from Thermotoga maritima: Molecular features of thermostability, J. Mol. Biol. 297, 659-672.
    • (2000) J. Mol. Biol. , vol.297 , pp. 659-672
    • Dams, T.1    Auerbach, G.2    Bader, G.3    Jacob, U.4    Ploom, T.5    Huber, R.6    Jaenicke, R.7
  • 18
    • 0032174885 scopus 로고    scopus 로고
    • Purification and characterization of NfrA1, a Bacillus subtilis Nitro/flavin reductase capable of interacting with the bacterial luciferase
    • Zenno, S., Kobori, T., Tanokura, M., and Saigo, K. (1998) Purification and characterization of NfrA1, a Bacillus subtilis Nitro/flavin reductase capable of interacting with the bacterial luciferase, Biosci. Biotechnol. Biochem. 62, 1978-1987.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1978-1987
    • Zenno, S.1    Kobori, T.2    Tanokura, M.3    Saigo, K.4
  • 19
    • 0029068515 scopus 로고
    • The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: Mechanism of the two-electron reduction
    • Li, R., Bianchet, M. A., Talalay, P., and Amzel, L. M. (1995) The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: Mechanism of the two-electron reduction, Proc. Natl. Acad. Sci. U.S.A. 92, 8846-8850.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8846-8850
    • Li, R.1    Bianchet, M.A.2    Talalay, P.3    Amzel, L.M.4
  • 21
    • 0034625317 scopus 로고    scopus 로고
    • Strengthening the dimerisation interface of Lac repressor increases its thermostability by 40 °C
    • Gerk, L. P., Leven, O., and Müller-Hill, B. (2000) Strengthening the dimerisation interface of Lac repressor increases its thermostability by 40 °C, J. Mol. Biol. 299, 805-812.
    • (2000) J. Mol. Biol. , vol.299 , pp. 805-812
    • Gerk, L.P.1    Leven, O.2    Müller-Hill, B.3
  • 22
    • 0019256228 scopus 로고
    • Structure-function relations in flavodoxins
    • Simondsen, R. P., and Tollin, G. (1980) Structure-function relations in flavodoxins, Mol. Cell. Biochem. 33, 13-24.
    • (1980) Mol. Cell. Biochem. , vol.33 , pp. 13-24
    • Simondsen, R.P.1    Tollin, G.2
  • 24
    • 0013954466 scopus 로고
    • On the existence of spectrally distinct classes of flavoprotein semiquinones. A new method for the quantitative production of flavoprotein semiquinones
    • Massey, V., and Palmer, G. H. (1966) On the existence of spectrally distinct classes of flavoprotein semiquinones. A new method for the quantitative production of flavoprotein semiquinones, Biochemistry 5, 3181-3189.
    • (1966) Biochemistry , vol.5 , pp. 3181-3189
    • Massey, V.1    Palmer, G.H.2
  • 25
    • 0034816360 scopus 로고    scopus 로고
    • Multiple mechanisms regulate expression of low-temperature responsive (LOT) genes in Saccharomyces cerevisiae
    • Zhang, L., Ohta, A., Horiuchi, H., Takagi, M., and Imai, R. (2001) Multiple mechanisms regulate expression of low-temperature responsive (LOT) genes in Saccharomyces cerevisiae, Biochem. Biophys. Res. Commun. 283, 531-535.
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 531-535
    • Zhang, L.1    Ohta, A.2    Horiuchi, H.3    Takagi, M.4    Imai, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.