메뉴 건너뛰기




Volumn 175, Issue 2, 1999, Pages 185-191

Physiological characterisation of an Azotobacter vinelandii nifU-deletion mutant and its spontaneous Nif+ revertants that over-produce cytochrome bd

Author keywords

Azotobacter vinelandii; Cytochrome bd; NifU revertant; Nitrogenase biosynthesis

Indexed keywords

ARTICLE; AZOTOBACTER VINELANDII; DELETION MUTANT; GENE OVEREXPRESSION; NITROGEN FIXATION; PRIORITY JOURNAL; REVERTANT;

EID: 0032796161     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(99)00191-3     Document Type: Article
Times cited : (5)

References (21)
  • 2
    • 0000703950 scopus 로고    scopus 로고
    • Mechanisms of molybdenum nitrogenase
    • Burgess, B.K. and Lowe, D.J. (1996) Mechanisms of molybdenum nitrogenase. Chem. Rev. 96, 2983-3011.
    • (1996) Chem. Rev. , vol.96 , pp. 2983-3011
    • Burgess, B.K.1    Lowe, D.J.2
  • 4
    • 0026548467 scopus 로고
    • The nifS, nifU, and nifV gene products are required for activity of all three nitrogenases of Azotobacter vinelandii
    • Kennedy, C. and Dean, D. (1992) The nifS, nifU, and nifV gene products are required for activity of all three nitrogenases of Azotobacter vinelandii. Mol. Gen. Genet. 231, 494-498.
    • (1992) Mol. Gen. Genet. , vol.231 , pp. 494-498
    • Kennedy, C.1    Dean, D.2
  • 5
  • 6
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NifS in metallocluster biosynthesis
    • Zheng, L., White, R.H., Cash, V.L., Jack, R.F. and Dean, D.R. (1993) Cysteine desulfurase activity indicates a role for NifS in metallocluster biosynthesis. Proc. Natl. Acad. Sci. USA 90, 2754-2758.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5
  • 7
    • 0027959635 scopus 로고
    • nifU gene product from Azotobacter vinelandii is a homodimer that contains two identical [2Fe-2S]
    • Fu, W., Jack, R.F., Morgan, T.V., Dean, D.R. and Johnson, M.K. (1994) nifU gene product from Azotobacter vinelandii is a homodimer that contains two identical [2Fe-2S]. Biochemistry 33, 10455-10463.
    • (1994) Biochemistry , vol.33 , pp. 10455-10463
    • Fu, W.1    Jack, R.F.2    Morgan, T.V.3    Dean, D.R.4    Johnson, M.K.5
  • 8
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters. Identification of an isc-SUA-hscBA-fdx gene cluster from Azotobacter vinelandii
    • Zheng, L., Cash, V.L., Flint, D.H. and Dean, D.R. (1998) Assembly of iron-sulfur clusters. Identification of an isc-SUA-hscBA-fdx gene cluster from Azotobacter vinelandii. J. Biol. Chem. 273, 13264-13272.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13264-13272
    • Zheng, L.1    Cash, V.L.2    Flint, D.H.3    Dean, D.R.4
  • 9
    • 0030663234 scopus 로고    scopus 로고
    • Respiratory protection of nitrogenase activity in Azotobacter vinelandii - roles of the terminal oxidases
    • Poole, R.K. and Hill, S. (1997) Respiratory protection of nitrogenase activity in Azotobacter vinelandii - roles of the terminal oxidases. Biosci. Rep. 17, 303-317.
    • (1997) Biosci. Rep. , vol.17 , pp. 303-317
    • Poole, R.K.1    Hill, S.2
  • 10
    • 0025030204 scopus 로고
    • Cloning and mutagenesis of the genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: Mutants deficient in the cytochrome d complex are unable to fix nitrogen in air
    • Kelly, M.J.S., Poole, R.K., Yates, M.G. and Kennedy, C. (1990) Cloning and mutagenesis of the genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: mutants deficient in the cytochrome d complex are unable to fix nitrogen in air. J. Bacteriol. 172, 6010-6019.
    • (1990) J. Bacteriol. , vol.172 , pp. 6010-6019
    • Kelly, M.J.S.1    Poole, R.K.2    Yates, M.G.3    Kennedy, C.4
  • 11
    • 0345477516 scopus 로고
    • Characterization of pseudorevertants of a nifU mutant of Azotobacter vinelandii
    • Tikhonovich, I.A., Provorov, N.A., Romanov V.I. and Newton, W.E., Eds., Kluwer Academic, London
    • Hill, S., He, L. and Kennedy, C. (1995) Characterization of pseudorevertants of a nifU mutant of Azotobacter vinelandii. In: Nitrogen Fixation: Fundamentals and Applications (Tikhonovich, I.A., Provorov, N.A., Romanov V.I. and Newton, W.E., Eds.), p. 215. Kluwer Academic, London.
    • (1995) Nitrogen Fixation: Fundamentals and Applications , pp. 215
    • Hill, S.1    He, L.2    Kennedy, C.3
  • 12
    • 0021848058 scopus 로고
    • Isolation and properties of mutants of Azotobacter chroococcum deficient in aerobic nitrogen fixation
    • Ramos, J.R. and Robson, R.L. (1985) Isolation and properties of mutants of Azotobacter chroococcum deficient in aerobic nitrogen fixation. J. Gen. Microbiol. 131, 1449-1458.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 1449-1458
    • Ramos, J.R.1    Robson, R.L.2
  • 14
    • 0025347063 scopus 로고
    • Roles for enteric d-type cytochrome oxidase in nitrogen fixation and microaerobiosis
    • Hill, S., Viollet, S., Smith, A.T. and Anthony, C. (1990) Roles for enteric d-type cytochrome oxidase in nitrogen fixation and microaerobiosis. J. Bacteriol. 172, 2071-2078.
    • (1990) J. Bacteriol. , vol.172 , pp. 2071-2078
    • Hill, S.1    Viollet, S.2    Smith, A.T.3    Anthony, C.4
  • 15
    • 0026653583 scopus 로고
    • Excretion of ammonium by a nifL mutant of nitrogen fixing Azotobacter vinelandii
    • Bali, A., Blanco, G., Hill, S. and Kennedy, C. (1992) Excretion of ammonium by a nifL mutant of nitrogen fixing Azotobacter vinelandii. Appl. Environ. Microbiol. 58, 1711-1718.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 1711-1718
    • Bali, A.1    Blanco, G.2    Hill, S.3    Kennedy, C.4
  • 16
    • 0031708947 scopus 로고    scopus 로고
    • Redox poise and oxygenation of cytochrome bd in the diazotroph Azotobacter vinelandii assessed in vivo using diode-array reflectance spectrophotometry
    • Kavanaugh, P.K., Callis, J.B., Edwards, S.E., Poole, R.K. and Hill, S. (1998) Redox poise and oxygenation of cytochrome bd in the diazotroph Azotobacter vinelandii assessed in vivo using diode-array reflectance spectrophotometry. Microbiology 144, 2271-2280.
    • (1998) Microbiology , vol.144 , pp. 2271-2280
    • Kavanaugh, P.K.1    Callis, J.B.2    Edwards, S.E.3    Poole, R.K.4    Hill, S.5
  • 17
    • 0030741757 scopus 로고    scopus 로고
    • The cydR gene product, required for regulation of cytochrome bd expression in the obligate aerobe Azotobacter vinelandii, is an Fnr-like protein
    • Wu, G., Hill, S., Kelly, M.J.S., Sawers, G. and Poole, R.K. (1997) The cydR gene product, required for regulation of cytochrome bd expression in the obligate aerobe Azotobacter vinelandii, is an Fnr-like protein. Microbiology 143, 2197-2207.
    • (1997) Microbiology , vol.143 , pp. 2197-2207
    • Wu, G.1    Hill, S.2    Kelly, M.J.S.3    Sawers, G.4    Poole, R.K.5
  • 18
    • 0040643267 scopus 로고    scopus 로고
    • Cytochrome bd terminal oxidases
    • Jünemann, S. (1997) Cytochrome bd terminal oxidases. Biochim. Biophys. Acta 1321, 107-127.
    • (1997) Biochim. Biophys. Acta , vol.1321 , pp. 107-127
    • Jünemann, S.1
  • 20
    • 0028839568 scopus 로고
    • Alternative function of the electron transport system in Azotobacter vinelandii: Removal of excess reductant by the cytochrome d pathway
    • Liu, J.-K., Lee, F.-T., Yao, X.-T., Davenport, J.W. and Wong, T.-Y. (1995) Alternative function of the electron transport system in Azotobacter vinelandii: removal of excess reductant by the cytochrome d pathway. Appl. Environ. Microbiol. 61, 3998-4003.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3998-4003
    • Liu, J.-K.1    Lee, F.-T.2    Yao, X.-T.3    Davenport, J.W.4    Wong, T.-Y.5
  • 21
    • 0001947282 scopus 로고    scopus 로고
    • The FNR modulon and FNR-regulated gene expression
    • Lin, E.C.C. and Lynch, A.S., Eds., R.G. Landes, Georgetown, TX
    • Guest, J.R., Green, J., Irvine, A.S. and Spiro, S. (1996) The FNR modulon and FNR-regulated gene expression. In: The Regulation of Gene Expression in Escherichia coli (Lin, E.C.C. and Lynch, A.S., Eds.), pp. 318-342. R.G. Landes, Georgetown, TX.
    • (1996) The Regulation of Gene Expression in Escherichia Coli , pp. 318-342
    • Guest, J.R.1    Green, J.2    Irvine, A.S.3    Spiro, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.