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Volumn 246, Issue 3, 1997, Pages 618-624

Expression studies on the ba3 quinol oxidase from Paracoccus denitrificans A bb3 variant is enzymatically inactive

Author keywords

CtaB; Cytochrome c oxidase; High spin heme; NarL; Nitrate nitrite regulation

Indexed keywords

OXIDOREDUCTASE; ANTIBODY; CYTOCHROME B; CYTOCHROME BA3; CYTOCHROME C OXIDASE; HEME; NITRATE; NITRITE; PEPTIDE FRAGMENT;

EID: 0030610473     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00618.x     Document Type: Article
Times cited : (16)

References (39)
  • 1
    • 0028290824 scopus 로고
    • Energy transduction by cytochrome complexes in mitochondria and bacterial respiration: The enzymology of coupling electron transfer reactions to transmembrane proton translocation
    • Trumpower, B. L. & Gennis, R. B. (1994) Energy transduction by cytochrome complexes in mitochondria and bacterial respiration: the enzymology of coupling electron transfer reactions to transmembrane proton translocation, Annu. Rev. Biochem. 63, 675-716.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 675-716
    • Trumpower, B.L.1    Gennis, R.B.2
  • 6
    • 0028238264 scopus 로고
    • An alternative cytochrome oxidase of Paracoccus denitrificans functions as a proton pump
    • Raitio, M. & Wikström, M. (1994) An alternative cytochrome oxidase of Paracoccus denitrificans functions as a proton pump, Biochim. Biophys. Acta 1186, 100-106.
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 100-106
    • Raitio, M.1    Wikström, M.2
  • 8
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., Ostermeier, C., Ludwig, B. & Michel, H. (1995) Structure at 2.8 Å 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
  • 9
    • 0027469984 scopus 로고
    • Genes for a microaerobically induced oxidase complex in Bradyrhizobium japonicum are essential for a nitrogen fixing endosymbiosis
    • Preisig, O., Anthamatten, D. & Hennecke, H. (1993) Genes for a microaerobically induced oxidase complex in Bradyrhizobium japonicum are essential for a nitrogen fixing endosymbiosis, Proc. Natl Acad. Sci. USA 90, 3309-3313.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 3309-3313
    • Preisig, O.1    Anthamatten, D.2    Hennecke, H.3
  • 10
    • 0028956071 scopus 로고
    • A homolog of the Rhizobium meliloti nitorgen fixation gene fixN is involved in the production of a microaerobically induced oxidase activity in the phytopathogenic bacterium Agrobacterium tumefaciens
    • Schlüter, A., Rühberg, S., Krämer, M., Weidner, S. & Priefer, U. B. (1995) A homolog of the Rhizobium meliloti nitorgen fixation gene fixN is involved in the production of a microaerobically induced oxidase activity in the phytopathogenic bacterium Agrobacterium tumefaciens, Mol. Gen. Genet. 247, 206-215.
    • (1995) Mol. Gen. Genet. , vol.247 , pp. 206-215
    • Schlüter, A.1    Rühberg, S.2    Krämer, M.3    Weidner, S.4    Priefer, U.B.5
  • 11
    • 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
  • 13
    • 0031054250 scopus 로고    scopus 로고
    • Isolation, analysis and deletion of the gene coding for subunit IV of cytochrome c oxidase in Paracoccus denitrificans
    • Witt, H. & Ludwig, B. (1997) Isolation, analysis and deletion of the gene coding for subunit IV of cytochrome c oxidase in Paracoccus denitrificans, J. Biol Chem. 272, 5514-5517.
    • (1997) J. Biol Chem. , vol.272 , pp. 5514-5517
    • Witt, H.1    Ludwig, B.2
  • 14
    • 0025830461 scopus 로고
    • Paracoccus denitrificans mutants deleted in the gene for subunit II of cytochrome c oxidase also lack subunit I
    • Steinrücke, P., Gerhus, E. & Ludwig, B. (1991) Paracoccus denitrificans mutants deleted in the gene for subunit II of cytochrome c oxidase also lack subunit I, J. Biol. Chem. 266, 7676-7681.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7676-7681
    • Steinrücke, P.1    Gerhus, E.2    Ludwig, B.3
  • 15
    • 0027086985 scopus 로고
    • Heme o biosynthesis in Escherichia coli: The cyoE gene in the cytochrome bo operon encodes a protoheme IX farnesyltransferase
    • Saiki, K., Mogi, T. & Anraku, Y. (1992) Heme o biosynthesis in Escherichia coli: The cyoE gene in the cytochrome bo operon encodes a protoheme IX farnesyltransferase, Biochem. Biophys. Res. Commun. 189, 1491-1497.
    • (1992) Biochem. Biophys. Res. Commun. , vol.189 , pp. 1491-1497
    • Saiki, K.1    Mogi, T.2    Anraku, Y.3
  • 16
    • 0027527547 scopus 로고
    • Bacillus subtilis CtaA and CtaB function in haem A biosynthesis
    • Svensson, B., Lübben, M. & Hederstedt, L. (1993) Bacillus subtilis CtaA and CtaB function in haem A biosynthesis, Mol. Microbiol. 10, 193-201.
    • (1993) Mol. Microbiol. , vol.10 , pp. 193-201
    • Svensson, B.1    Lübben, M.2    Hederstedt, L.3
  • 17
    • 0028152645 scopus 로고
    • Biosynthesis and functional role of haem o and heam a
    • Mogi, T., Saiki, K. & Anraku, Y. (1994) Biosynthesis and functional role of haem o and heam a, Mol. Microbiol. 14, 391-398.
    • (1994) Mol. Microbiol. , vol.14 , pp. 391-398
    • Mogi, T.1    Saiki, K.2    Anraku, Y.3
  • 18
    • 0001888973 scopus 로고
    • Isolation and characterization of Paracoccus denitrificans mutants with increased conjugation frequencies and pleiotropic loss of a (nGATCn) DNA-modifying property
    • 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 property, 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
  • 20
    • 0022821996 scopus 로고
    • Cytochrome c oxidase from Paracoccus denitrificans
    • Ludwig, B. (1986) Cytochrome c oxidase from Paracoccus denitrificans, Methods Enzymol. 126, 153-159.
    • (1986) Methods Enzymol. , vol.126 , pp. 153-159
    • Ludwig, B.1
  • 23
  • 25
    • 0018178434 scopus 로고
    • A modification of the lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell, M. A. K., Haas, S. M., Bieber, 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.K.1    Haas, S.M.2    Bieber, L.3    Tolbert, N.E.4
  • 26
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range of 1 to 100 kDa
    • Schägger, H. & von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range of 1 to 100 kDa, Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 29
    • 0006975835 scopus 로고
    • A manual of quantitative immunelectrophoresis
    • Axelsen, N. H., Kroll, J. & Weekke, B. (1973) A manual of quantitative immunelectrophoresis, Scand. J. Immunol. 2, Suppl. 1.
    • (1973) Scand. J. Immunol. , vol.2 , Issue.1 SUPPL.
    • Axelsen, N.H.1    Kroll, J.2    Weekke, B.3
  • 30
    • 0023653927 scopus 로고
    • Simultaneous determination of heines a, b, and c from pyridine hemochrome spectra
    • Berry, E. A. & Trumpower, B. L. (1987) Simultaneous determination of heines a, b, and c from pyridine hemochrome spectra, Anal. Biochem. 161, 1-15.
    • (1987) Anal. Biochem. , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 31
    • 0345536682 scopus 로고
    • Metabolic pathways in Paracoccus denitrificans and closely related bacteria in relation to the phylogeny of procaryotes
    • Stouthamer, A. H. (1992) Metabolic pathways in Paracoccus denitrificans and closely related bacteria in relation to the phylogeny of procaryotes, Antonie ran Leeuwenhoek 61, 1-33.
    • (1992) Antonie ran Leeuwenhoek , vol.61 , pp. 1-33
    • Stouthamer, A.H.1
  • 32
    • 0027452664 scopus 로고
    • Definition of nitrite and nitrate response elements at the anaerobically inducible Escherichia nirB promoter: Interactions between FNR and NarL
    • Tyson, K. L., Bell, A. I., Cole, J. A. & Busby, S. J. W. (1993) Definition of nitrite and nitrate response elements at the anaerobically inducible Escherichia nirB promoter: interactions between FNR and NarL, Mol. Microbiol. 7, 151-157.
    • (1993) Mol. Microbiol. , vol.7 , pp. 151-157
    • Tyson, K.L.1    Bell, A.I.2    Cole, J.A.3    Busby, S.J.W.4
  • 33
    • 0027321764 scopus 로고
    • Nitrate regulation of anaerobic respiratory gene expression in Escherichia coli
    • Stewart, V. (1993) Nitrate regulation of anaerobic respiratory gene expression in Escherichia coli, Mol. Microbiol. 9, 425-434.
    • (1993) Mol. Microbiol. , vol.9 , pp. 425-434
    • Stewart, V.1
  • 35
    • 0026559542 scopus 로고
    • Regulation of gene expression by oxygen in Saccharomyces cerevisiae
    • Zitomer, R. S. & Lowry, C. V. (1992) Regulation of gene expression by oxygen in Saccharomyces cerevisiae, Microbiol. Rev 56, 1-11.
    • (1992) Microbiol. Rev , vol.56 , pp. 1-11
    • Zitomer, R.S.1    Lowry, C.V.2
  • 36
    • 0029785523 scopus 로고    scopus 로고
    • 550 expression in Paracoccus denitrificans strongly depends on growth condition: Identification of promoter region for cycA by transcription start analysis
    • 550 expression in Paracoccus denitrificans strongly depends on growth condition: identification of promoter region for cycA by transcription start analysis, Microbiology 142, 2577-2585.
    • (1996) Microbiology , vol.142 , pp. 2577-2585
    • Stoll, R.1    Page, M.D.2    Sambongi, Y.3    Ferguson, S.J.4
  • 37
    • 0026438826 scopus 로고
    • The low-spin heme site of cytochrome fco from Escherichia coli is promiscuous with respect to heme type
    • Puustinen, A., Morgan, J. E., Verkhovsky, M., Thomas, J. W., Gennis, R. B. & Wikström, M. (1992) The low-spin heme site of cytochrome fco from Escherichia coli is promiscuous with respect to heme type, Biochemistry 31, 10363-10369.
    • (1992) Biochemistry , vol.31 , pp. 10363-10369
    • Puustinen, A.1    Morgan, J.E.2    Verkhovsky, M.3    Thomas, J.W.4    Gennis, R.B.5    Wikström, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.