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Volumn 64, Issue 4, 2000, Pages 852-857

Gene organization for nitric oxide reduction in alcaligenes faecalis S-6

Author keywords

Alcaligenes faecalis; Cytochrome bc complex; Denitrification; Nitric oxide reductase

Indexed keywords

ALCALIGENES FAECALIS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034168650     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.64.852     Document Type: Article
Times cited : (7)

References (31)
  • 1
    • 0002204059 scopus 로고
    • Regulation of nitrite reductase in the denitrifying bacterium Al-caligenes faecalis
    • Kakutani, T., Beppu, T., and Arima, K., Regulation of nitrite reductase in the denitrifying bacterium Al-caligenes faecalis. Agric. Biol. Chem., 45, 23-28 (1981).
    • (1981) Agric. Biol. Chem , vol.45 , pp. 23-28
    • Kakutani, T.1    Beppu, T.2    Arima, K.3
  • 2
    • 0019457194 scopus 로고
    • Purification and properties of a copper-containing nitrite reductase from a denitrifying bacterium, Al-caligenes faecalis
    • Kakutani, T., Watanabe, H., Arima, K., and Beppu, T., Purification and properties of a copper-containing nitrite reductase from a denitrifying bacterium, Al-caligenes faecalis. J. Biochem., 89, 453-461 (1981).
    • (1981) J. Biochem , vol.89 , pp. 453-461
    • Kakutani, T.1    Watanabe, H.2    Arima, K.3    Beppu, T.4
  • 3
    • 0019498490 scopus 로고
    • A blue protein as an inactivating factor for nitrite reductase from Alcaligenes faecalis
    • Kakutani, T., Watanabe, H., Arima, K., and Beppu, T., A blue protein as an inactivating factor for nitrite reductase from Alcaligenes faecalis. J. Biochem., 89, 463-472 (1981).
    • (1981) J. Biochem , vol.89 , pp. 463-472
    • Kakutani, T.1    Watanabe, H.2    Arima, K.3    Beppu, T.4
  • 4
    • 0027229994 scopus 로고
    • Cloning and characterization of a nitrite reductase gene from Alcaligenes faecalis and its expression in Escherichia coli
    • Nishiyama, M., Suzuki, J., Kukimoto, M., Ohnuki, T., Horinouchi, S., and Beppu, T., Cloning and characterization of a nitrite reductase gene from Alcaligenes faecalis and its expression in Escherichia coli. J. Gen. Microbiol., 139, 725-733 (1993).
    • (1993) J. Gen. Microbiol , vol.139 , pp. 725-733
    • Nishiyama, M.1    Suzuki, J.2    Kukimoto, M.3    Ohnuki, T.4    Horinouchi, S.5    Beppu, T.6
  • 5
    • 0023512814 scopus 로고
    • The blue copper protein gene of Alcaligenes faecalis S-6 directs secretion of blue copper protein from Escherichia coli cells
    • Yamamoto, K., Uozumi, T., and Beppu, T., The blue copper protein gene of Alcaligenes faecalis S-6 directs secretion of blue copper protein from Escherichia coli cells. J. Bacteriol., 169, 5648-5652 (1987).
    • (1987) J. Bacteriol , vol.169 , pp. 5648-5652
    • Yamamoto, K.1    Uozumi, T.2    Beppu, T.3
  • 6
    • 0028298314 scopus 로고
    • X-ray structure and site-directed mutagenesis of a nitrite reductase from Alcaligenes faecalis S-6: Roles of two copper atoms in nitrite reduction
    • Kukimoto, M., Nishiyama, M., Murphy, M. E. P., Turley, S., Adman, E. T., Horinouchi, S., and Beppu, T., X-ray structure and site-directed mutagenesis of a nitrite reductase from Alcaligenes faecalis S-6: roles of two copper atoms in nitrite reduction. Biochemistry, 33, 5246-5252 (1994).
    • (1994) Biochemistry , vol.33 , pp. 5246-5252
    • Kukimoto, M.1    Nishiyama, M.2    Murphy, M.E.P.3    Turley, S.4    Adman, E.T.5    Horinouchi, S.6    Beppu, T.7
  • 7
    • 0028958832 scopus 로고
    • Identification of interaction site of pseudoazurin with its redox partner, copper-containing nitrite reductase from Alcaligenes faecalis S-6
    • Kukimoto, M., Nishiyama, M., Ohnuki, T., Turley, S., Adman, E. T., Horinouchi, S., and Beppu, T., Identification of interaction site of pseudoazurin with its redox partner, copper-containing nitrite reductase from Alcaligenes faecalis S-6. Protein Eng., 8, 153-158 (1995).
    • (1995) Protein Eng , vol.8 , pp. 153-158
    • Kukimoto, M.1    Nishiyama, M.2    Ohnuki, T.3    Turley, S.4    Adman, E.T.5    Horinouchi, S.6    Beppu, T.7
  • 8
    • 0029995615 scopus 로고    scopus 로고
    • Studies on protein-protein interaction between copper-containing nitrite reductase and pseudoazurin from Alcaligenes faecalis S-6
    • Kukimoto, M., Nishiyama, M., Tanokura, M., Adman, E. T., and Horinouchi, S., Studies on protein-protein interaction between copper-containing nitrite reductase and pseudoazurin from Alcaligenes faecalis S-6. J. Biol. Chem., 271, 13680-13683 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 13680-13683
    • Kukimoto, M.1    Nishiyama, M.2    Tanokura, M.3    Adman, E.T.4    Horinouchi, S.5
  • 9
    • 0030599129 scopus 로고    scopus 로고
    • Site-directed mutagenesis of azurin from Pseudomonas aeruginosa enhances the formation of an electron-transfer complex with a copper-containing nitrite reductase from Alcaligenes faecalis S-6
    • Kukimoto, M., Nishiyama, M., Tanokura, M., Murphy, M. E. P., Adman, E. T., and Horinouchi, S., Site-directed mutagenesis of azurin from Pseudomonas aeruginosa enhances the formation of an electron-transfer complex with a copper-containing nitrite reductase from Alcaligenes faecalis S-6. FEBS Lett., 394, 87-90 (1996).
    • (1996) FEBS Lett , vol.394 , pp. 87-90
    • Kukimoto, M.1    Nishiyama, M.2    Tanokura, M.3    Murphy, M.E.P.4    Adman, E.T.5    Horinouchi, S.6
  • 10
    • 0028219699 scopus 로고
    • Denitrification: Production and consumption of nitric oxide
    • Ye, R. W., Aver ill, B. A., and Tiedje, J. M., Denitrification: production and consumption of nitric oxide. Appl. Environ. Microbiol., 60, 1053-1058 (1994).
    • (1994) Appl. Environ. Microbiol , vol.60 , pp. 1053-1058
    • Ye, R.W.1    Aver Ill, B.A.2    Tiedje, J.M.3
  • 11
    • 0027326619 scopus 로고
    • The biological role of nitric oxide in bacteria
    • Zumft, W. G., The biological role of nitric oxide in bacteria. Arch. Microbiol., 160, 253-264 (1993).
    • (1993) Arch. Microbiol , vol.160 , pp. 253-264
    • Zumft, W.G.1
  • 12
    • 0026697255 scopus 로고
    • Mutants of Pseudomonas fluorescens deficient in dissimilatory nitrite reduction are also altered in nitric oxide reduction
    • Ye, R. W., Arunakumari, A., Averill, B. A., and Tiedje, J. M., Mutants of Pseudomonas fluorescens deficient in dissimilatory nitrite reduction are also altered in nitric oxide reduction. J. Bacteriol., 174, 2560-2564 (1992).
    • (1992) J. Bacteriol , vol.174 , pp. 2560-2564
    • Ye, R.W.1    Arunakumari, A.2    Averill, B.A.3    Tiedje, J.M.4
  • 13
    • 0026667697 scopus 로고
    • Characterization of Tn5 mutants deficient in dissimilatory nitrite reduction in Pseudomonas sp. Strain G-179, which contains a copper nitrite reductase
    • Ye, R. W., Averill, B. A., and Tiedje, J. M., Characterization of Tn5 mutants deficient in dissimilatory nitrite reduction in Pseudomonas sp. strain G-179, which contains a copper nitrite reductase. J. Bacteriol., 174, 6653-6658 (1992).
    • (1992) J. Bacteriol , vol.174 , pp. 6653-6658
    • Ye, R.W.1    Averill, B.A.2    Tiedje, J.M.3
  • 14
    • 0024335650 scopus 로고
    • Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome be complex of nitrate-respiring (Denitrifying) Pseudomonas stutzeri
    • Heiss, B., Frunzke, K., and Zumft, W. G., Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome be complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri. J. Bacteriol., Vol III, 3288-3297 (1989).
    • (1989) J. Bacteriol , vol.Vol III , pp. 3288-3297
    • Heiss, B.1    Frunzke, K.2    Zumft, W.G.3
  • 15
    • 0025309975 scopus 로고
    • The nitric oxide reductase of Paracoccus denitrificans
    • Carr, G. J. and Ferguson, S., The nitric oxide reductase of Paracoccus denitrificans. Biochem. J., 269, 423-429 (1990).
    • (1990) Biochem. J , vol.269 , pp. 423-429
    • Carr, G.J.1    Ferguson, S.2
  • 16
    • 0025898909 scopus 로고
    • Nitric oxide reductase: Purification from Paracoccus denitrificans with use of a single column and some characteristics
    • Dermastia, M., Turk, T., and Hollocher, T. C., Nitric oxide reductase: purification from Paracoccus denitrificans with use of a single column and some characteristics. J. Biol. Chem., 266, 10899-10905 (1992).
    • (1992) J. Biol. Chem , vol.266 , pp. 10899-10905
    • Dermastia, M.1    Turk, T.2    Hollocher, T.C.3
  • 17
    • 0027438769 scopus 로고
    • Nitric oxide reductase of Achromobacter cycloclastes
    • Jones, A. M. and Hollocher, T. C., Nitric oxide reductase of Achromobacter cycloclastes. Biochim. Biophys. Acta, 1144, 359-366 (1993).
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 359-366
    • Jones, A.M.1    Hollocher, T.C.2
  • 18
    • 0027418338 scopus 로고
    • Cytochrome P-450 55A1 (P-450dNIR) acts as nitric oxide reductase employing NADH as the direct electron donor
    • Nakahara, K., Tanimoto, T., Hatano, K., Usuda, K., and Shoun, H., Cytochrome P-450 55A1 (P-450dNIR) acts as nitric oxide reductase employing NADH as the direct electron donor. J. Biol. Chem., 268, 8350-8355 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 8350-8355
    • Nakahara, K.1    Tanimoto, T.2    Hatano, K.3    Usuda, K.4    Shoun, H.5
  • 19
    • 0017170673 scopus 로고
    • An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels
    • Thomas, P. E., Ryan, D., and Levin, W., An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels. Anal. Biochem., 75, 168-176 (1976).
    • (1976) Anal. Biochem , vol.75 , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Levin, W.3
  • 20
    • 0032900142 scopus 로고    scopus 로고
    • The periplas-mic nitrate reductase in Pseudomonas sp. Strain G-179 catalyzes the first step of denitrificaion
    • Bedzyk, L., Wang, T., and Ye, R. W., The periplas-mic nitrate reductase in Pseudomonas sp. strain G-179 catalyzes the first step of denitrificaion. J. Bacteriol., 181, 2802-2806 (1999).
    • (1999) J. Bacteriol , vol.181 , pp. 2802-2806
    • Bedzyk, L.1    Wang, T.2    Ye, R.W.3
  • 22
    • 0030984912 scopus 로고    scopus 로고
    • Characterization of the nitric oxide reductase-encoding region in Rhodobac-ter sphaeroides 2.4.3
    • Bartnikas, T. B., Tosques, I. E., Laratta, W. P., Shi, J., and Shapleigh, J. P., Characterization of the nitric oxide reductase-encoding region in Rhodobac-ter sphaeroides 2.4.3. J. Bacteriol., 179, 3534-3540 (1997).
    • (1997) J. Bacteriol , vol.179 , pp. 3534-3540
    • Bartnikas, T.B.1    Tosques, I.E.2    Laratta, W.P.3    Shi, J.4    Shapleigh, J.P.5
  • 23
    • 0028946836 scopus 로고
    • The structural genes for nitric oxide reductase from Pseudomonas aeruginosa
    • Arai, H., Igarashi, Y., and Kodama, T., The structural genes for nitric oxide reductase from Pseudomonas aeruginosa. Biochim. Biophys. Acta, 1261, 279-284 (1995).
    • (1995) Biochim. Biophys. Acta , vol.1261 , pp. 279-284
    • Arai, H.1    Igarashi, Y.2    Kodama, T.3
  • 24
    • 0028158048 scopus 로고
    • Nitric oxide reductase from Pseudomonas stutzeri: Primary structure and gene organization of a novel bacterial cytochrome be complex
    • Zumft, W. G., Braun, C., and Cuypers, H., Nitric oxide reductase from Pseudomonas stutzeri: primary structure and gene organization of a novel bacterial cytochrome be complex. Eur. J. Biochem., 219, 481-490 (1994).
    • (1994) Eur. J. Biochem , vol.219 , pp. 481-490
    • Zumft, W.G.1    Braun, C.2    Cuypers, H.3
  • 25
    • 85008008542 scopus 로고
    • Structure and ANR-dependent transcription of the nir genes for denitrification from Pseudomonas aeruginosa
    • Arai, H., Igarashi, Y., and Kodama, T., Structure and ANR-dependent transcription of the nir genes for denitrification from Pseudomonas aeruginosa. Biosci. Biotechnol. Biochem., 58, 1286-1291 (1994).
    • (1994) Biosci. Biotechnol. Biochem , vol.58 , pp. 1286-1291
    • Arai, H.1    Igarashi, Y.2    Kodama, T.3
  • 26
    • 0024989737 scopus 로고
    • FNR and its role in oxygen-regulated gene expression in Escherichia coli
    • Spiro, S. and Guest, J. R., FNR and its role in oxygen-regulated gene expression in Escherichia coli. FEMS Microbiol. Rev., 75, 399-428 (1990).
    • (1990) FEMS Microbiol. Rev , vol.75 , pp. 399-428
    • Spiro, S.1    Guest, J.R.2
  • 27
    • 0031938612 scopus 로고    scopus 로고
    • Localization of denitrification genes on the chromosomal map of Pseudomonas aeruginosa
    • Vollack, K. U., Xie, J., Hartig, E., Romling, U., and Zumft, W. G., Localization of denitrification genes on the chromosomal map of Pseudomonas aeruginosa. Microbiology, 144, 441-448 (1998).
    • (1998) Microbiology , vol.144 , pp. 441-448
    • Vollack, K.U.1    Xie, J.2    Hartig, E.3    Romling, U.4    Zumft, W.G.5
  • 28
    • 0028959433 scopus 로고
    • Nitrite and nitric oxide reduction in Paracoccus denitrificans is under the controle of NNR, a regulatory protein that belongs to the FNR family of transcriptional activators
    • Spanning, R. J. M., De Boer, A. P. N., Reijnders, W. N. M., Spiro, S., Westerhoff, H. V., Stouthamer, A. H., and Van der Oost, J., Nitrite and nitric oxide reduction in Paracoccus denitrificans is under the controle of NNR, a regulatory protein that belongs to the FNR family of transcriptional activators. FEBS Lett., 360, 151-154 (1995).
    • (1995) FEBS Lett , vol.360 , pp. 151-154
    • Spanning, R.J.M.1    De Boer, A.P.N.2    Reijnders, W.N.M.3    Spiro, S.4    Westerhoff, H.V.5    Stouthamer, A.H.6    Van Der Oost, J.7
  • 29
    • 0026620454 scopus 로고
    • Interdependence of respiratory NO reduction and nitrite reduction revealed by mutagenesis of nirQ, a novel gene in the denitrification gene cluster of Pseudomonas stutzeri
    • Jlingst, A. and Zumft, W. G., Interdependence of respiratory NO reduction and nitrite reduction revealed by mutagenesis of nirQ, a novel gene in the denitrification gene cluster of Pseudomonas stutzeri. FEBS Lett., 314, 308-314 (1992).
    • (1992) FEBS Lett , vol.314 , pp. 308-314
    • Jlingst, A.1    Zumft, W.G.2
  • 30
    • 0032176419 scopus 로고    scopus 로고
    • The role of the nirQOP genes in energy conservation during anaerobic growth of Pseudomonas aeruginosa
    • Arai, H., Kodama, T., and Igarashi, Y., The role of the nirQOP genes in energy conservation during anaerobic growth of Pseudomonas aeruginosa. Biosci. Biotechnol. Biochem., 62, 1995-1999 (1998).
    • (1998) Biosci. Biotechnol. Biochem , vol.62 , pp. 1995-1999
    • Arai, H.1    Kodama, T.2    Igarashi, Y.3
  • 31
    • 0033060309 scopus 로고    scopus 로고
    • Multiple transcription factors of the FNR family in denitrifying Pseudomonas stutzeri: Characterization of four fnr-like genes, regulatory responses and cognate metabolic processes
    • Vollack, K. U., Hartig, E., Korner, H., and Zumft, W. G., Multiple transcription factors of the FNR family in denitrifying Pseudomonas stutzeri: characterization of four fnr-like genes, regulatory responses and cognate metabolic processes. Mol. Microbiol., 31, 1681-1694 (1999).
    • (1999) Mol. Microbiol , vol.31 , pp. 1681-1694
    • Vollack, K.U.1    Hartig, E.2    Korner, H.3    Zumft, W.G.4


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