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Volumn 144, Issue 8, 1998, Pages 2271-2280

Redox poise and oxygenation of cytochrome bd in the diazotroph Azotobacter vinelandii assessed in vivo using diode-array reflectance spectrophotometry

Author keywords

Azotobacter vinelandii; Cytochrome bd type oxidase; Diode array spectrophotometry; O2 supply and redox changes of cytochromes

Indexed keywords

CYTOCHROME B; CYTOCHROME D;

EID: 0031708947     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-144-8-2271     Document Type: Article
Times cited : (5)

References (39)
  • 1
    • 0346596604 scopus 로고
    • Evidence for an alternative nitrogen fixation system in Azotobacter vinelandii
    • Bishop, P. E., Jarienski, D. M. & Hetherington, D. R. (1980). Evidence for an alternative nitrogen fixation system in Azotobacter vinelandii. Proc Natl Acad Sci USA 77, 7342-7346.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 7342-7346
    • Bishop, P.E.1    Jarienski, D.M.2    Hetherington, D.R.3
  • 2
    • 84981573578 scopus 로고
    • Higher derivative analysis of complex absorption spectra
    • Butler, W. L. & Hopkins, D. W. (1970). Higher derivative analysis of complex absorption spectra. Photocbem Photobiol 12, 439-450.
    • (1970) Photocbem Photobiol , vol.12 , pp. 439-450
    • Butler, W.L.1    Hopkins, D.W.2
  • 3
    • 0025708350 scopus 로고
    • Noninvasive method for monitoring ethanol in fermentation processes using fibre-optic near-infrared spectroscopy
    • Cavinato, A. G., Mayes, D. M., Ge, Z. & Callis. J. B. (1990). Noninvasive method for monitoring ethanol in fermentation processes using fibre-optic near-infrared spectroscopy. Anal Chem 62, 1977-1982.
    • (1990) Anal Chem , vol.62 , pp. 1977-1982
    • Cavinato, A.G.1    Mayes, D.M.2    Ge, Z.3    Callis, J.B.4
  • 5
    • 0007596694 scopus 로고
    • 2 permeability by noninvasive spectrophotometry of leghemoglobin
    • 2 permeability by noninvasive spectrophotometry of leghemoglobin. Plant Physiol 96, 137-143.
    • (1991) Plant Physiol , vol.96 , pp. 137-143
    • Denison, R.F.1    Layzell, D.B.2
  • 6
    • 0028263624 scopus 로고
    • Determination of the oxygen affinities of the terminal oxidases in Azotobacter vinelandii using the deoxygenation of oxyleghaemoglobin and oxymyoglobin: Cytochrome bd is a low-affinity oxidase
    • D'mello, R., Hill, S. & Poole, R. K. (1994a). Determination of the oxygen affinities of the terminal oxidases in Azotobacter vinelandii using the deoxygenation of oxyleghaemoglobin and oxymyoglobin: cytochrome bd is a low-affinity oxidase. Microbiology 140, 1395-1402.
    • (1994) Microbiology , vol.140 , pp. 1395-1402
    • D'mello, R.1    Hill, S.2    Poole, R.K.3
  • 8
    • 0029981912 scopus 로고    scopus 로고
    • The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity: Implications for regulation of activity in vivo by oxygen inhibition
    • D'mello. R., Hill, S. & Poole, R. K. (1996). The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity : implications for regulation of activity in vivo by oxygen inhibition. Microbiology 142, 755-763.
    • (1996) Microbiology , vol.142 , pp. 755-763
    • D'mello, R.1    Hill, S.2    Poole, R.K.3
  • 10
    • 0023802457 scopus 로고
    • The nucleotide sequence of the cyd locus encoding the two subunits of the cytochrome d terminal oxidase complex of Escherichia coli
    • Green, G. N., Fang, H., Lin, R.-J., Newton, G., Mathers. M., Georgiou, C. D. & Gennis, R. B. (1988). The nucleotide sequence of the cyd locus encoding the two subunits of the cytochrome d terminal oxidase complex of Escherichia coli. J Biol Chem 263, 13138-13143.
    • (1988) J Biol Chem , vol.263 , pp. 13138-13143
    • Green, G.N.1    Fang, H.2    Lin, R.-J.3    Newton, G.4    Mathers, M.5    Georgiou, C.D.6    Gennis, R.B.7
  • 11
    • 0001883695 scopus 로고
    • Physiology of nitrogen fixation in free-living heterotrophs
    • Edited by G. Stacey, R. H. Burris & H. J. Evans. New York & London : Chapman & Hall
    • Hill, S. (1992). Physiology of nitrogen fixation in free-living heterotrophs. In Biological Nitrogen Fixation, pp. 86-134. Edited by G. Stacey, R. H. Burris & H. J. Evans. New York & London : Chapman & Hall.
    • (1992) Biological Nitrogen Fixation , pp. 86-134
    • Hill, S.1
  • 12
    • 0027299607 scopus 로고
    • Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli
    • Hill, J. J., Alben, J. O. & Gennis, R. B. (1993). Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli. Proc Natl Acad Sci USA 90, 5863-5867.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5863-5867
    • Hill, J.J.1    Alben, J.O.2    Gennis, R.B.3
  • 13
    • 0028625501 scopus 로고
    • The room temperature reactions of carbon monoxide and oxygen with the cytochrome bd quinol oxidase from Escherichia coli
    • Hill, B. C, Hill, J. J. & Gennis. R. B. (1994). The room temperature reactions of carbon monoxide and oxygen with the cytochrome bd quinol oxidase from Escherichia coli. Biochemistry 33, 15110-15115.
    • (1994) Biochemistry , vol.33 , pp. 15110-15115
    • Hill, B.C.1    Hill, J.J.2    Gennis, R.B.3
  • 14
    • 0040643267 scopus 로고    scopus 로고
    • Cytochrome bd terminal oxidase
    • Jünemann, S. (1997). Cytochrome bd terminal oxidase. Biochim Biophys Acta 1321, 107-127.
    • (1997) Biochim Biophys Acta , vol.1321 , pp. 107-127
    • Jünemann, S.1
  • 15
    • 0029839729 scopus 로고    scopus 로고
    • Does the cytochrome bd terminal oxidase complex have a 'pulsed form'?
    • Jünemann. S. & Rich. P. R. (1996). Does the cytochrome bd terminal oxidase complex have a 'pulsed form'? Biochem Soc Trans 24, 400S.
    • (1996) Biochem Soc Trans , vol.24
    • Jünemann, S.1    Rich, P.R.2
  • 16
    • 0029062502 scopus 로고
    • Cytochrome bd oxidase from Azotobacter vinelandii: Purification and quantitation of ligand binding to the oxygen reactive site
    • Jünemann, S. & Wrigglesworth, J. M. (1995). Cytochrome bd oxidase from Azotobacter vinelandii: purification and quantitation of ligand binding to the oxygen reactive site. J Biol Chem 270, 16213-16220.
    • (1995) J Biol Chem , vol.270 , pp. 16213-16220
    • Jünemann, S.1    Wrigglesworth, J.M.2
  • 17
    • 0028818107 scopus 로고
    • A suggested mechanism for the catalytic cycle of cytochrome bd terminal oxidase based on kinetic analysis
    • Jünemann, S., Butterworth, P. J. & Wrigglesworth, J. M. (1995). A suggested mechanism for the catalytic cycle of cytochrome bd terminal oxidase based on kinetic analysis. Biochemistry 34, 14861-14867.
    • (1995) Biochemistry , vol.34 , pp. 14861-14867
    • Jünemann, S.1    Butterworth, P.J.2    Wrigglesworth, J.M.3
  • 18
    • 0026337648 scopus 로고
    • Identification of a ferryl intermediate of Escherichia coli cytochrome d terminal oxidase by resonance Raman spectroscopy
    • Kahlow, M. A., Zuberi, T. M., Gennis, R. B. & Loehr, T. M. (1991). Identification of a ferryl intermediate of Escherichia coli cytochrome d terminal oxidase by resonance Raman spectroscopy. Biochemistry 30, 11485-11489.
    • (1991) Biochemistry , vol.30 , pp. 11485-11489
    • Kahlow, M.A.1    Zuberi, T.M.2    Gennis, R.B.3    Loehr, T.M.4
  • 19
    • 0015876797 scopus 로고
    • The respiratory chain of Azotobacter vinelandii. I. Spectral properties of cytochrome d
    • Kauffman, H. F. & van Gelder, B. F. (1973). The respiratory chain of Azotobacter vinelandii. I. Spectral properties of cytochrome d. Biochim Biophys Acta 305, 260-267.
    • (1973) Biochim Biophys Acta , vol.305 , pp. 260-267
    • Kauffman, H.F.1    Van Gelder, B.F.2
  • 20
    • 0025185915 scopus 로고
    • The automatic maintenance of low dissolved oxygen using a photobacterial oxygen sensor for the study of microaerobiosis
    • Kavanagh, E. P. & Hill, S. (1990). The automatic maintenance of low dissolved oxygen using a photobacterial oxygen sensor for the study of microaerobiosis. J Appl Bacterial 69, 539-549.
    • (1990) J Appl Bacterial , vol.69 , pp. 539-549
    • Kavanagh, E.P.1    Hill, S.2
  • 21
    • 3543009085 scopus 로고
    • Application of diodearray spectrophotometry for the analysis of bacterial cytochromes in vivo
    • Edited by I. A. Tikhonovich, N. A. Provorov, V. I. Romanov & W.E.Newton. London: Kluwer Academic Publishers
    • Kavanagh, E. P., Callis, J. B. & Hill, S. (1995). Application of diodearray spectrophotometry for the analysis of bacterial cytochromes in vivo. In Nitrogen Fixation: Fundamentals and Applications, pp. 217. Edited by I. A. Tikhonovich, N. A. Provorov, V. I. Romanov & W.E.Newton. London: Kluwer Academic Publishers.
    • (1995) Nitrogen Fixation: Fundamentals and Applications , pp. 217
    • Kavanagh, E.P.1    Callis, J.B.2    Hill, S.3
  • 23
    • 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. & 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 Bacterial 172, 6010-6019.
    • (1990) J Bacterial , vol.172 , pp. 6010-6019
    • Kelly, M.J.S.1    Poole, R.K.2    Yates, M.G.3    Kennedy, C.4
  • 24
    • 0021272743 scopus 로고
    • 558-d complex from cells grown with limited oxygen and evidence of branched electron-carrying systems
    • 558-d complex from cells grown with limited oxygen and evidence of branched electron-carrying systems. J Biol Chem 259, 3375-3381.
    • (1984) J Biol Chem , vol.259 , pp. 3375-3381
    • Kita, K.1    Konishi, K.2    Anraku, Y.3
  • 25
    • 0028332212 scopus 로고
    • Purification and characterisation of the cytochrome bd complex from Azotobacter vinelandii: Comparison to the complex from Escherichia coli
    • Kolonay, J. F., Moshiri, F., Gennis. R. B., Kaysser, T. M. & Maier, R. J. (1994). Purification and characterisation of the cytochrome bd complex from Azotobacter vinelandii: comparison to the complex from Escherichia coli. J Bacterial 176, 4177-4181.
    • (1994) J Bacterial , vol.176 , pp. 4177-4181
    • Kolonay, J.F.1    Moshiri, F.2    Gennis, R.B.3    Kaysser, T.M.4    Maier, R.J.5
  • 26
    • 0022573635 scopus 로고
    • 560-d complex, a terminal oxidase of the aerobic respiratory chain of Photobacterium phosphoreum
    • 560-d complex, a terminal oxidase of the aerobic respiratory chain of Photobacterium phosphoreum. J Biochem 99, 1227-1236.
    • (1986) J Biochem , vol.99 , pp. 1227-1236
    • Konishi, K.1    Ouchi, M.2    Kita, K.3    Horikoshi, I.4
  • 27
    • 0028178937 scopus 로고
    • Mutagenesis of a gene encoding a cytochrome o-like terminal oxidase of Azotobacter vinelandii: A cytochrome o mutant is aero-tolerant during nitrogen fixation
    • Leung, D., van der Oost, J., Kelly, M., Saraste, M., Hill, S. & Poole, R. K. (1994). Mutagenesis of a gene encoding a cytochrome o-like terminal oxidase of Azotobacter vinelandii: a cytochrome o mutant is aero-tolerant during nitrogen fixation. FEMS Microbiol Lett 119, 351-358.
    • (1994) FEMS Microbiol Lett , vol.119 , pp. 351-358
    • Leung, D.1    Van Der Oost, J.2    Kelly, M.3    Saraste, M.4    Hill, S.5    Poole, R.K.6
  • 28
    • 0025945337 scopus 로고
    • Cloning, characterization, and expression in Escherichia coli of the genes encoding the cytochrome d oxidase complex from Azotobacter vinelandii
    • Moshiri, F., Chawla, A. & Maier, R. J. (1991). Cloning, characterization, and expression in Escherichia coli of the genes encoding the cytochrome d oxidase complex from Azotobacter vinelandii. J Bacterial 173, 6230-6241.
    • (1991) J Bacterial , vol.173 , pp. 6230-6241
    • Moshiri, F.1    Chawla, A.2    Maier, R.J.3
  • 30
    • 0030663234 scopus 로고    scopus 로고
    • Respiratory protection of nitrogenase activity in Azotobacter vinelandii - roles of the terminal oxidases
    • Poole, R. K. & 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
  • 31
    • 0018653542 scopus 로고
    • The reaction of cytochrome o in Escherichia coli with oxygen
    • Poole, R. K., Waring. A. J. & Chance, B. (1979). The reaction of cytochrome o in Escherichia coli with oxygen. Biochem J 184, 379-389.
    • (1979) Biochem J , vol.184 , pp. 379-389
    • Poole, R.K.1    Waring, A.J.2    Chance, B.3
  • 32
    • 0020627779 scopus 로고
    • The 650 nm chromophore in Escherichia coli is an 'oxy-' or oxy-genated compound, not the oxidized form of cytochrome oxidase d: An hypothesis
    • Poole. R. K., Kumar, C., Salmon, I. & Chance, B. (1983). The 650 nm chromophore in Escherichia coli is an 'oxy-' or oxy-genated compound, not the oxidized form of cytochrome oxidase d: an hypothesis. J Gen Microbiol 129, 1335-1344.
    • (1983) J Gen Microbiol , vol.129 , pp. 1335-1344
    • Poole, R.K.1    Kumar, C.2    Salmon, I.3    Chance, B.4
  • 35
    • 0024033476 scopus 로고
    • A haemoprotein is not involved in the control by oxygen of enteric nitrogenase synthesis
    • Smith, A., Hill, S. & Anthony. C. (1988). A haemoprotein is not involved in the control by oxygen of enteric nitrogenase synthesis. J Gen Microbiol 134, 1499-1507.
    • (1988) J Gen Microbiol , vol.134 , pp. 1499-1507
    • Smith, A.1    Hill, S.2    Anthony, C.3
  • 36
    • 0025057311 scopus 로고
    • The purification, characterisation and role of the d-type cytochrome oxidase of Klebsiella pnenmoniae during nitrogen fixation
    • Smith, A., Hill, S. & Anthony, C. (1990). The purification, characterisation and role of the d-type cytochrome oxidase of Klebsiella pnenmoniae during nitrogen fixation. J Gen Microbiol 136, 171-180.
    • (1990) J Gen Microbiol , vol.136 , pp. 171-180
    • Smith, A.1    Hill, S.2    Anthony, C.3
  • 37
    • 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. & 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
  • 38
    • 0022644482 scopus 로고
    • Biochemical and biophysical properties of cytochrome o of Azotobacter vinelandii
    • Yang, T. (1986). Biochemical and biophysical properties of cytochrome o of Azotobacter vinelandii. Biochim Biophys Acta 848, 342-351.
    • (1986) Biochim Biophys Acta , vol.848 , pp. 342-351
    • Yang, T.1
  • 39
    • 0343402727 scopus 로고
    • The role of oxygen and hydrogen in nitrogen fixation
    • Edited by J. A. Cole & S. Ferguson. Cambridge: Cambridge University Press
    • Yates, M. G. (1988). The role of oxygen and hydrogen in nitrogen fixation. In The Nitrogen and Sulphur Cycles, pp. 383-416. Edited by J. A. Cole & S. Ferguson. Cambridge: Cambridge University Press.
    • (1988) The Nitrogen and Sulphur Cycles , pp. 383-416
    • Yates, M.G.1


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