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Volumn 242, Issue 3, 1996, Pages 592-600

Mutational analysis of the nor gene cluster which encodes nitric-oxide reductase from Paracoccus denitrificans

Author keywords

Denitrification; Heme copper oxidase; Nitric oxide reductase; Paracoccus denitrificans; Respiratory control

Indexed keywords

CYTOCHROME B; CYTOCHROME C; NITRITE REDUCTASE;

EID: 0030438017     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0592r.x     Document Type: Article
Times cited : (105)

References (58)
  • 1
    • 85008008542 scopus 로고
    • Structure and ANR-dependent transcription of the nir genes for denitrification from Pseudomonas aeruginosa
    • Arai, H., Igarashi, Y. & Kodama, T. (1994) Structure and ANR-dependent transcription of the nir genes for denitrification from Pseudomonas aeruginosa, Biosci. Biotechnol. Biochem. 58, 1286-1291.
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 1286-1291
    • Arai, H.1    Igarashi, Y.2    Kodama, T.3
  • 2
    • 0028946836 scopus 로고
    • The structural genes for nitric oxide reductase from Pseudomonas aeruginosa
    • Arai, H., Igarashi, Y. & Kodama, T. (1995) The structural genes for nitric oxide reductase from Pseudomonas aeruginosa, Biochem. Biophys. Acta 1261, 279-284.
    • (1995) Biochem. Biophys. Acta , vol.1261 , pp. 279-284
    • Arai, H.1    Igarashi, Y.2    Kodama, T.3
  • 5
    • 0028811652 scopus 로고
    • Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions
    • Berks, B. C., Ferguson, S. J., Moir, J. W. B. & Richardson, D. J. (1995) Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions, Biochem. Biophys. Acta 1232, 97-173.
    • (1995) Biochem. Biophys. Acta , vol.1232 , pp. 97-173
    • Berks, B.C.1    Ferguson, S.J.2    Moir, J.W.B.3    Richardson, D.J.4
  • 6
    • 0020971311 scopus 로고
    • A rapid alkaline extraction method for the isolation of plasmid DNA
    • Birnboim, H. C. (1983) A rapid alkaline extraction method for the isolation of plasmid DNA, Methods Enzymol. 100, 243-255.
    • (1983) Methods Enzymol. , vol.100 , pp. 243-255
    • Birnboim, H.C.1
  • 7
    • 0018875128 scopus 로고
    • Electron transport to nitrous oxide in Paracoccus denitrificans
    • Boogerd, F. C., van Verseveld, H. W. & Stouthamer, A. H. (1980) Electron transport to nitrous oxide in Paracoccus denitrificans, FEBS Lett. 113, 279-284.
    • (1980) FEBS Lett. , vol.113 , pp. 279-284
    • Boogerd, F.C.1    Van Verseveld, H.W.2    Stouthamer, A.H.3
  • 8
    • 0014674485 scopus 로고
    • A complementation analysis of the restriction and modification of DNA in Escherichia coli
    • Boyer, H. W, & Roulland-Dussoix, D. (1969) A complementation analysis of the restriction and modification of DNA in Escherichia coli, J. Biol. Chem. 41, 459-472.
    • (1969) J. Biol. Chem. , vol.41 , pp. 459-472
    • Boyer, H.W.1    Roulland-Dussoix, D.2
  • 9
    • 0026317610 scopus 로고
    • Marker exchange of the structural genes for nitric oxide reductase blocks the denitritication pathway of Pseudomonas stutzeri at nitric oxide
    • Braun, C. & Zumft, W. G. (1991) Marker exchange of the structural genes for nitric oxide reductase blocks the denitritication pathway of Pseudomonas stutzeri at nitric oxide, J. Biol. Chem. 266, 22 785-22 788.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22785-22788
    • Braun, C.1    Zumft, W.G.2
  • 10
    • 0026516423 scopus 로고
    • The structural genes of the nitric oxide reductase complex from Pseudomonas stutzeri are part of a 30-kilobase gene cluster for denitrification
    • Braun, C. & Zumft, W. G. (1992) The structural genes of the nitric oxide reductase complex from Pseudomonas stutzeri are part of a 30-kilobase gene cluster for denitrification, J. Bacteriol. 174, 2394-2397.
    • (1992) J. Bacteriol. , vol.174 , pp. 2394-2397
    • Braun, C.1    Zumft, W.G.2
  • 11
    • 0025309975 scopus 로고
    • The nitric oxide reductase of Paracoccus denitrificans
    • Carr, G. J. & Ferguson, S. J. (1990) The nitric oxide reductase of Paracoccus denitrificans, Biochem. J. 269, 423-429.
    • (1990) Biochem. J. , vol.269 , pp. 423-429
    • Carr, G.J.1    Ferguson, S.J.2
  • 12
    • 0000161862 scopus 로고
    • Studies on the utilization of nitrate by Micrococcus denitrificans
    • Chang, J. P. & Morris, J. G. (1962) Studies on the utilization of nitrate by Micrococcus denitrificans, J. Gen. Microbiol. 29, 301-310.
    • (1962) J. Gen. Microbiol. , vol.29 , pp. 301-310
    • Chang, J.P.1    Morris, J.G.2
  • 13
    • 0002812235 scopus 로고
    • Atmospheric chemical processes of the oxides of nitogen, including nitrous oxide
    • (Delwiche, C. C., ed.) John Wiley & Sons, New York
    • Crutzen, P. J. (1981) Atmospheric chemical processes of the oxides of nitogen, including nitrous oxide, in Denitrification, nitrification and atmospheric nitrous oxide (Delwiche, C. C., ed.) pp. 17-44. John Wiley & Sons, New York.
    • (1981) Denitrification, Nitrification and Atmospheric Nitrous Oxide , pp. 17-44
    • Crutzen, P.J.1
  • 14
    • 0028580539 scopus 로고
    • Isolation, sequencing and mutational analysis of a gene cluster involved in nitrite reduction in Paracoccus denitrificans
    • de Boer, A. P. N., Reijnders, W. N. M. Kuenen, J. G., Stouthamer, A. H. & van Spanning, R. J. M. (1994) Isolation, sequencing and mutational analysis of a gene cluster involved in nitrite reduction in Paracoccus denitrificans, Antonie Leeuwenhoek 66, 111-127.
    • (1994) Antonie Leeuwenhoek , vol.66 , pp. 111-127
    • De Boer, A.P.N.1    Reijnders, W.N.M.2    Kuenen, J.G.3    Stouthamer, A.H.4    Van Spanning, R.J.M.5
  • 15
    • 0001888973 scopus 로고
    • Isolation and characterization of Paracoccus denitrificans mutants with increased conjugation frequencies and pleiotropic loss of a (nGATCn) DNA-modifying properly
    • de Vries, G. E., Harms, N., Hoogendijk, J. & Stouthamer, A. H. (1989) Isolation and characterization of Paracoccus denitrificans mutants with increased conjugation frequencies and pleiotropic loss of a (nGATCn) DNA-modifying properly, Arch. Microbiol. 152, 52-57.
    • (1989) Arch. Microbiol. , vol.152 , pp. 52-57
    • De Vries, G.E.1    Harms, N.2    Hoogendijk, J.3    Stouthamer, A.H.4
  • 16
    • 0025898909 scopus 로고
    • Nitric oxide reductase - Purification from Puracoccus denitrificans with use of a single column and some characteristics
    • Dermastia, M., Turk, T. & Hollocher, T. C. (1991) Nitric oxide reductase - purification from Puracoccus denitrificans with use of a single column and some characteristics, J. Biol. Chem. 266, 10 899-10 905.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10899-10905
    • Dermastia, M.1    Turk, T.2    Hollocher, T.C.3
  • 17
    • 0022000283 scopus 로고
    • Plasmids related to the broad host range vector pRK290, useful for gene cloning and monitoring gene expression
    • Ditta, G., Schmidhauser, T., Yakobson, E., Lu, P., Liang, X., Finlay, D., Guiney, D. & Helsinki, D. (1985) Plasmids related to the broad host range vector pRK290, useful for gene cloning and monitoring gene expression, Plasmid 13, 149-153.
    • (1985) Plasmid , vol.13 , pp. 149-153
    • Ditta, G.1    Schmidhauser, T.2    Yakobson, E.3    Lu, P.4    Liang, X.5    Finlay, D.6    Guiney, D.7    Helsinki, D.8
  • 18
    • 0024999332 scopus 로고
    • Improved detection of helix-turn-helix DNA-binding motifs in protein sequences
    • Dodd, I. B. & Egan, J. B. (1990) Improved detection of helix-turn-helix DNA-binding motifs in protein sequences, Nucleic Acids Res. 18, 5019-5026.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5019-5026
    • Dodd, I.B.1    Egan, J.B.2
  • 19
    • 0028606311 scopus 로고
    • Denitrification and its control
    • Ferguson, S. J. (1994) Denitrification and its control, Antonie Leeuwenhoek 66, 89-110.
    • (1994) Antonie Leeuwenhoek , vol.66 , pp. 89-110
    • Ferguson, S.J.1
  • 20
    • 0029988772 scopus 로고    scopus 로고
    • Cytochrome cb-type nitric oxide reductase with cytochrome c oxidase activity from Paracoccus denitrificans ATCC 35512
    • Fujiwara, T. & Fukumori, Y. (1996) Cytochrome cb-type nitric oxide reductase with cytochrome c oxidase activity from Paracoccus denitrificans ATCC 35512, J. Bacteriol. 178, 1866-1871.
    • (1996) J. Bacteriol. , vol.178 , pp. 1866-1871
    • Fujiwara, T.1    Fukumori, Y.2
  • 21
    • 0025361382 scopus 로고
    • Paracoccus denitrificans cytochrome c, gene replacement mutants
    • Gerhus, E., Steinrücke, P. & Ludwig, B. (1990) Paracoccus denitrificans cytochrome c, gene replacement mutants, J. Bacteriol. 172, 2392-2400.
    • (1990) J. Bacteriol. , vol.172 , pp. 2392-2400
    • Gerhus, E.1    Steinrücke, P.2    Ludwig, B.3
  • 22
    • 0024845389 scopus 로고
    • Deletion of the gene for subunit III leads to defective assembly of bacterial cytochrome oxidase
    • Haltia, T., Finel, M., Harms, N., Nakari, T., Raitio, M., Wikström, M. & Saraste, M (1989) Deletion of the gene for subunit III leads to defective assembly of bacterial cytochrome oxidase, EMBO J. 8, 3571-3579.
    • (1989) EMBO J. , vol.8 , pp. 3571-3579
    • Haltia, T.1    Finel, M.2    Harms, N.3    Nakari, T.4    Raitio, M.5    Wikström, M.6    Saraste, M.7
  • 24
    • 0028038094 scopus 로고
    • Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans
    • Haltia, T., Semo, N., Arrondo, J. L. R., Goni, F. M. & Freire, E. (1994) Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans, Biochem. 33, 9731-9740.
    • (1994) Biochem. , vol.33 , pp. 9731-9740
    • Haltia, T.1    Semo, N.2    Arrondo, J.L.R.3    Goni, F.M.4    Freire, E.5
  • 25
    • 0024335650 scopus 로고
    • Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome bc complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri
    • Heiss, B., Frunzke, K. & Zumft, W. G. (1989) Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome bc complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri, J. Bacteriol. 171, 3288-3297.
    • (1989) J. Bacteriol. , vol.171 , pp. 3288-3297
    • Heiss, B.1    Frunzke, K.2    Zumft, W.G.3
  • 26
    • 0028890031 scopus 로고
    • Structure at 2.8 angstrom resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., Ostermeier, C., Ludwig, B. & Michel, H. (1995) Structure at 2.8 angstrom resolution of cytochrome c oxidase from Paracoccus denitrificans, Nature 376, 660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 27
    • 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
    • Jüngst, A. & Zumft, W. G. (1992) 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) FEBS Lett. , vol.314 , pp. 308-314
    • Jüngst, A.1    Zumft, W.G.2
  • 28
    • 0027405737 scopus 로고
    • Anaerobic expression of nitric oxide reductase from denitrifying Pseudomonas stutzeri
    • Körner, H. (1993) Anaerobic expression of nitric oxide reductase from denitrifying Pseudomonas stutzeri, Arch. Microbiol. 159, 410-416.
    • (1993) Arch. Microbiol. , vol.159 , pp. 410-416
    • Körner, H.1
  • 29
    • 0027062910 scopus 로고
    • The molecule of the year
    • Koshland, D. E. Jr (1992) The molecule of the year, Science 258, 1861.
    • (1992) Science , vol.258 , pp. 1861
    • Koshland Jr., D.E.1
  • 30
    • 0025107826 scopus 로고
    • Formation of a potent respiratory inhibitor at nitrite reduction by nitrite reductase isolated from the bacterium Paracoccus denitrificans
    • Kucera, I. & Skaldal, P. (1990) Formation of a potent respiratory inhibitor at nitrite reduction by nitrite reductase isolated from the bacterium Paracoccus denitrificans, J. Basic Microbiol. 7, 515-522.
    • (1990) J. Basic Microbiol. , vol.7 , pp. 515-522
    • Kucera, I.1    Skaldal, P.2
  • 31
    • 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
  • 32
    • 0014665074 scopus 로고
    • A nitrite reductase with cytochrome oxidase activity from Micrococcus denitrificans
    • Lam, Y. & Nicholas, D. J. D. (1969) A nitrite reductase with cytochrome oxidase activity from Micrococcus denitrificans, Biochem. Biophys. Acta 180, 459-472.
    • (1969) Biochem. Biophys. Acta , vol.180 , pp. 459-472
    • Lam, Y.1    Nicholas, D.J.D.2
  • 33
    • 0017113635 scopus 로고
    • Electron transport in aerobically grown Paracoccus denitrificans: Kinetic characterization of the membrane-bound cytochromes and the stoichiometry of respiratory-driven proto translocation
    • Lawford, H. G., Cox, J. C., Garland, P. B. & Hadock, B. A. (1976) Electron transport in aerobically grown Paracoccus denitrificans: kinetic characterization of the membrane-bound cytochromes and the stoichiometry of respiratory-driven proto translocation, FEBS Lett. 64, 369-374.
    • (1976) FEBS Lett. , vol.64 , pp. 369-374
    • Lawford, H.G.1    Cox, J.C.2    Garland, P.B.3    Hadock, B.A.4
  • 34
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell, M. A., Haas, S. M., Bieber, L. L. & Tolbert, N. E. (1978) A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples, Anal. Biochem. 87, 206-210.
    • (1978) Anal. Biochem. , vol.87 , pp. 206-210
    • Markwell, M.A.1    Haas, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 36
    • 0021196998 scopus 로고
    • Protein-DNA recognition
    • Pabo, C. O. (1984) Protein-DNA recognition, Annu. Rev. Biochem. 53, 293-321.
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 293-321
    • Pabo, C.O.1
  • 37
    • 0015723979 scopus 로고
    • Reduction of nitrogenous oxides by microorganisms
    • Payne, W. J. (1973) Reduction of nitrogenous oxides by microorganisms, Bacterial Rev. 37, 409-452.
    • (1973) Bacterial Rev. , vol.37 , pp. 409-452
    • Payne, W.J.1
  • 38
    • 0000673426 scopus 로고
    • Isolation and analysis of the genes for cytochrome c oxidase in Paracoccus denitrificans
    • Raitio, M., Jalli, T. & Saraste, M. (1987) Isolation and analysis of the genes for cytochrome c oxidase in Paracoccus denitrificans, EMBO J. 6, 2825-2833.
    • (1987) EMBO J. , vol.6 , pp. 2825-2833
    • Raitio, M.1    Jalli, T.2    Saraste, M.3
  • 39
    • 0025135467 scopus 로고
    • Are there isoenzymes of cytochrome c oxidase in Paracoccus denitrificans?
    • Raitio, M., Pispa, J. M., Metso, T. & Saraste, M. (1990) Are there isoenzymes of cytochrome c oxidase in Paracoccus denitrificans? FEBS Lett. 261, 431-435.
    • (1990) FEBS Lett. , vol.261 , pp. 431-435
    • Raitio, M.1    Pispa, J.M.2    Metso, T.3    Saraste, M.4
  • 40
    • 0030038634 scopus 로고    scopus 로고
    • Topology prediction for helical transmembrane proteins at 86% accuracy
    • Rost, B., Fariselli, P. & Casadio, R. (1996) Topology prediction for helical transmembrane proteins at 86% accuracy, Protein Sci. 5, 1704-1718.
    • (1996) Protein Sci. , vol.5 , pp. 1704-1718
    • Rost, B.1    Fariselli, P.2    Casadio, R.3
  • 41
    • 0025640889 scopus 로고
    • Structural features of cytochrome oxidase
    • Saraste, M. (1990) Structural features of cytochrome oxidase, Quart. Rev. Biophys. 23, 331-366.
    • (1990) Quart. Rev. Biophys. , vol.23 , pp. 331-366
    • Saraste, M.1
  • 42
    • 0028226882 scopus 로고
    • Cytochrome oxidase evolved by tinkering with denitrification enzymes
    • Saraste, M. & Castresana, J. (1994) Cytochrome oxidase evolved by tinkering with denitrification enzymes, FEBS Lett. 341, 1-4.
    • (1994) FEBS Lett. , vol.341 , pp. 1-4
    • Saraste, M.1    Castresana, J.2
  • 43
    • 0002433715 scopus 로고
    • Vector plasmids for in vivo and in vitro manipulations of gram-negative bacteria
    • (Pühler, A., ed.) Springer-Verlag, Berlin
    • Simon, R., Priefer, U. & Pühler, A. (1983) Vector plasmids for in vivo and in vitro manipulations of gram-negative bacteria, in Molecular genetics of the bacteria-plant interactions (Pühler, A., ed.) pp. 98-106, Springer-Verlag, Berlin.
    • (1983) Molecular Genetics of the Bacteria-plant Interactions , pp. 98-106
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 44
    • 0026457799 scopus 로고
    • An FNR-dependent promoter from Escherichia coli is active and anaerobically inducible in Paracoccus denitrificans
    • Spiro, S. (1992) An FNR-dependent promoter from Escherichia coli is active and anaerobically inducible in Paracoccus denitrificans, FEMS Microbiol. Lett. 98, 145-148.
    • (1992) FEMS Microbiol. Lett. , vol.98 , pp. 145-148
    • Spiro, S.1
  • 45
    • 0028556430 scopus 로고
    • The FNR family of transcriptional regulators
    • Spiro, S. (1994) The FNR family of transcriptional regulators, Antonie Leeuwenhaek 66, 23-36.
    • (1994) Antonie Leeuwenhaek , vol.66 , pp. 23-36
    • Spiro, S.1
  • 46
  • 47
    • 0025863275 scopus 로고
    • Metabolic regulation including anaerobic metabolism in Paracoccus denitrificans
    • Stouthamer, A. H. (1991) Metabolic regulation including anaerobic metabolism in Paracoccus denitrificans, J. Bioenerg. Biomembr. 23, 163-185.
    • (1991) J. Bioenerg. Biomembr. , vol.23 , pp. 163-185
    • Stouthamer, A.H.1
  • 50
    • 0028959433 scopus 로고
    • Nitrite and nitric oxide reduction in Paracoccus denitrificans is under the control of NNR, a regulatory protein that belongs to the FNR family of transcriptional activators
    • van Spanning, R. J. M., de Boer, A. P. N., Reijnders, W. N. M., Spiro, S., Westerhoff, H. V., Stouthamer, A. H. & van der Oost, J. (1995) Nitrite and nitric oxide reduction in Paracoccus denitrificans is under the control of NNR, a regulatory protein that belongs to the FNR family of transcriptional activators, FEBS Lett. 360, 151-154.
    • (1995) FEBS Lett. , vol.360 , pp. 151-154
    • Van 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
  • 52
    • 0001607723 scopus 로고
    • Distantly related sequences in the a- and b-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., Saraste, M., Runswick, M. J. & Gay, N. J. (1982) Distantly related sequences in the a- and b-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold, EMBO J. 1, 945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 53
    • 0028219699 scopus 로고
    • Denitrification: Production and consumption of nitric oxide
    • Ye, R. W., Averill, B. A. & Tiedje, J. M. (1994) Denitrification: production and consumption of nitric oxide, Appl. Environ. Microbiol. 60, 1053-1058.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1053-1058
    • Ye, R.W.1    Averill, B.A.2    Tiedje, J.M.3
  • 54
    • 0028834124 scopus 로고
    • Genes encoding RubisCO in Pseudomonas hydrogenothermophila are followed by a novel cbbQ gene similar to nirQ of the denitrification gene cluster from Pseudomonas species
    • Yokoyama, K., Hayashi, N. R., Arai, H., Chung, S. Y., Igarashi, Y. & Kodama, T. (1995) Genes encoding RubisCO in Pseudomonas hydrogenothermophila are followed by a novel cbbQ gene similar to nirQ of the denitrification gene cluster from Pseudomonas species, Gene (Amst.) 153, 75-79.
    • (1995) Gene (Amst.) , vol.153 , pp. 75-79
    • Yokoyama, K.1    Hayashi, N.R.2    Arai, H.3    Chung, S.Y.4    Igarashi, Y.5    Kodama, T.6
  • 55
    • 0028796334 scopus 로고
    • A common topology of proteins catalyzing ATP-triggered reactions
    • Yoshida, M. & Amano, T. (1995) A common topology of proteins catalyzing ATP-triggered reactions, FEBS Lett. 359, 1-5.
    • (1995) FEBS Lett. , vol.359 , pp. 1-5
    • Yoshida, M.1    Amano, T.2
  • 56
    • 0022382102 scopus 로고
    • Amperometric method for determining nitrous oxide in denitrification and in nitrogenase-catalyzed nitrous oxide reduction
    • Zimmer, W., Danneberg, G. & Bothe, H. (1985) Amperometric method for determining nitrous oxide in denitrification and in nitrogenase-catalyzed nitrous oxide reduction, Curr. Microbiol. 12, 341-346.
    • (1985) Curr. Microbiol. , vol.12 , pp. 341-346
    • Zimmer, W.1    Danneberg, G.2    Bothe, H.3
  • 57
    • 0027326619 scopus 로고
    • The biological role of nitric oxide in bacteria
    • Zumft, W. G. (1993) The biological role of nitric oxide in bacteria, Arch. Microbiol. 160, 253-264.
    • (1993) Arch. Microbiol. , vol.160 , pp. 253-264
    • Zumft, W.G.1
  • 58
    • 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. & Cuypers, H. (1994) 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) Eur. J. Biochem. , vol.219 , pp. 481-490
    • Zumft, W.G.1    Braun, C.2    Cuypers, H.3


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