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Volumn 56, Issue 4, 2007, Pages 265-269

Cytochrome bd, a key oxidase in bacterial survival and tolerance to nitrosative stress

Author keywords

Cytochromes; Microbiology; Nitric oxide; ROS

Indexed keywords

CYTOCHROME; CYTOCHROME BD TERMINAL OXIDASE COMPLEX, E COLI; ESCHERICHIA COLI PROTEIN; MULTIENZYME COMPLEX; NITRIC OXIDE; OXIDOREDUCTASE; OXYGEN;

EID: 58249119571     PISSN: 00212938     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper
Times cited : (31)

References (39)
  • 1
    • 0040643267 scopus 로고    scopus 로고
    • Cytochrome bd terminal oxidase
    • Junemann, S. (1997) Cytochrome bd terminal oxidase. Biochim Biophys Acta 1321, 107-127.
    • (1997) Biochim Biophys Acta , vol.1321 , pp. 107-127
    • Junemann, S.1
  • 3
  • 4
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock, G. T., and Wikstrom, M. (1992) Oxygen activation and the conservation of energy in cell respiration. Nature 356, 301-309.
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikstrom, M.2
  • 5
    • 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., and 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
  • 6
    • 0034652126 scopus 로고    scopus 로고
    • Femtosecond resolution of ligand-heme interactions in the high affinity quinol oxidase bd. A di-heme active site?
    • Vos, M. H., Borisov, V. B., Liebl, U., Martin, J.-L, and Konstantinov, A. A. (2000) Femtosecond resolution of ligand-heme interactions in the high affinity quinol oxidase bd. A di-heme active site? Proc. Natl. Acad. Sci. USA 97, 1554-1559.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1554-1559
    • Vos, M.H.1    Borisov, V.B.2    Liebl, U.3    Martin, J.-L.4    Konstantinov, A.A.5
  • 7
    • 0842264185 scopus 로고    scopus 로고
    • The strict anaerobe Bacteroides fragilis grows in and benefits from nanomolar concentrations of oxygen
    • Baughn, A. D., and Malamy, M. H. (2004) The strict anaerobe Bacteroides fragilis grows in and benefits from nanomolar concentrations of oxygen. Nature 427, 441-444.
    • (2004) Nature , vol.427 , pp. 441-444
    • Baughn, A.D.1    Malamy, M.H.2
  • 8
    • 0035089129 scopus 로고    scopus 로고
    • Interruption of the cydB locus in Brucella abortus attenuates intracellular survival and virulnce in the mouse model of infection
    • Endley, S., McMurray, D., and Ficht, T. A. (2001) Interruption of the cydB locus in Brucella abortus attenuates intracellular survival and virulnce in the mouse model of infection. J Bacteriol 183, 2454-2462.
    • (2001) J Bacteriol , vol.183 , pp. 2454-2462
    • Endley, S.1    McMurray, D.2    Ficht, T.A.3
  • 9
    • 0032989878 scopus 로고    scopus 로고
    • Impact of either elevated or decreased levels of cytochrome bd expression on Shigella flexneri virulence
    • Way, S. S., Sallustio, S., Magliozzo, R. S., and Goldberg, M. B. (1999) Impact of either elevated or decreased levels of cytochrome bd expression on Shigella flexneri virulence. J. Bacteriol. 181, 1229- 1237.
    • (1999) J. Bacteriol , vol.181 , pp. 1229-1237
    • Way, S.S.1    Sallustio, S.2    Magliozzo, R.S.3    Goldberg, M.B.4
  • 10
    • 27344432975 scopus 로고    scopus 로고
    • Changes in energy metabolism of Mycobacterium tuberculosis in mouse lung and under in vitro conditions affecting aerobic respiration
    • Shi, L., Sohaskey, C. D., Kana, B. D., Dawes, S., North, R. J., Mizrahi, V., and Gennaro, M. L. (2005) Changes in energy metabolism of Mycobacterium tuberculosis in mouse lung and under in vitro conditions affecting aerobic respiration. Proc. Natl. Acad. Sci. U S A 102, 15629-15634.
    • (2005) Proc. Natl. Acad. Sci. U S A , vol.102 , pp. 15629-15634
    • Shi, L.1    Sohaskey, C.D.2    Kana, B.D.3    Dawes, S.4    North, R.J.5    Mizrahi, V.6    Gennaro, M.L.7
  • 11
    • 0034680875 scopus 로고    scopus 로고
    • Flavohemoglobin Hmp affords inducible protection for Escherichia coli respiration, catalyzed by cytochromes bo′ or bd, from nitric oxide
    • Stevanin, T. M., loannidis, N., Mills, C. E., Kim, S. O., Hughes, M. N., and Poole, R. K. (2000) Flavohemoglobin Hmp affords inducible protection for Escherichia coli respiration, catalyzed by cytochromes bo′ or bd, from nitric oxide. J. Biol. Chem. 275, 35868-35875.
    • (2000) J. Biol. Chem , vol.275 , pp. 35868-35875
    • Stevanin, T.M.1    loannidis, N.2    Mills, C.E.3    Kim, S.O.4    Hughes, M.N.5    Poole, R.K.6
  • 12
    • 0028134892 scopus 로고
    • Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase
    • Brown, G. C, and Cooper, C. E. (1994) Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase. FEBS Lett 356, 295-298.
    • (1994) FEBS Lett , vol.356 , pp. 295-298
    • Brown, G.C.1    Cooper, C.E.2
  • 13
    • 28044464985 scopus 로고
    • Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases
    • Cleeter, M. W., Cooper, J. M., Darley-Usmar, V. M., Moncada, S., and Schapira, A. H. (1994) Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases. FEBS Lett 345, 50-54.
    • (1994) FEBS Lett , vol.345 , pp. 50-54
    • Cleeter, M.W.1    Cooper, J.M.2    Darley-Usmar, V.M.3    Moncada, S.4    Schapira, A.H.5
  • 14
    • 0027945838 scopus 로고
    • Nitric oxide potently and reversibly deenergizes mitochondria at low oxygen tension
    • Schweizer, M., and Richter, C. (1994) Nitric oxide potently and reversibly deenergizes mitochondria at low oxygen tension. Biochem Biophys Res Commun 204, 169-175.
    • (1994) Biochem Biophys Res Commun , vol.204 , pp. 169-175
    • Schweizer, M.1    Richter, C.2
  • 16
    • 0031559913 scopus 로고    scopus 로고
    • Nitric oxide ejects electrons from the binuclear centre of cytochrome c oxidase by reacting with oxidised copper: A general mechanism for the interaction of copper proteins with nitric oxide?
    • Cooper, C. E., Torres, J., Sharpe, M. A., and Wilson, M. T. (1997) Nitric oxide ejects electrons from the binuclear centre of cytochrome c oxidase by reacting with oxidised copper: a general mechanism for the interaction of copper proteins with nitric oxide? FEBS Lett 414, 281-284.
    • (1997) FEBS Lett , vol.414 , pp. 281-284
    • Cooper, C.E.1    Torres, J.2    Sharpe, M.A.3    Wilson, M.T.4
  • 17
    • 0034687716 scopus 로고    scopus 로고
    • Reaction of nitric oxide with the turnover intermediates of cytochrome c oxidase: Reaction pathway and functional effects
    • Giuffrè, A., Barone, M. C, Mastronicola, D., D'ltri, E., Sarti, P., and Brunori, M. (2000) Reaction of nitric oxide with the turnover intermediates of cytochrome c oxidase: reaction pathway and functional effects. Biochemistry 39, 15446-15453.
    • (2000) Biochemistry , vol.39 , pp. 15446-15453
    • Giuffrè, A.1    Barone, M.C.2    Mastronicola, D.3    D'ltri, E.4    Sarti, P.5    Brunori, M.6
  • 18
    • 0034705673 scopus 로고    scopus 로고
    • Cytochrome c oxidase rapidly metabolises nitric oxide to nitrite
    • Torres, J., Sharpe, M. A., Rosquist, A., Cooper, C. E., and Wilson, M. T. (2000) Cytochrome c oxidase rapidly metabolises nitric oxide to nitrite. FEBS Lett 475, 263-266.
    • (2000) FEBS Lett , vol.475 , pp. 263-266
    • Torres, J.1    Sharpe, M.A.2    Rosquist, A.3    Cooper, C.E.4    Wilson, M.T.5
  • 19
    • 0032502730 scopus 로고    scopus 로고
    • A common mechanism for the interaction of nitric oxide with the oxidized binuclear centre and oxygen intermediates of cytochrome c oxidase
    • Torres, J., Cooper, C. E., and Wilson, M. T. (1998) A common mechanism for the interaction of nitric oxide with the oxidized binuclear centre and oxygen intermediates of cytochrome c oxidase. J. Biol. Chem. 273, 8756-8766.
    • (1998) J. Biol. Chem , vol.273 , pp. 8756-8766
    • Torres, J.1    Cooper, C.E.2    Wilson, M.T.3
  • 20
    • 34447509483 scopus 로고    scopus 로고
    • Nitric oxide regulation of mitochondrial oxygen consumption II: Molecular mechanism and tissue physiology
    • Cooper, C. E., and Giulivi, C. (2007) Nitric oxide regulation of mitochondrial oxygen consumption II: Molecular mechanism and tissue physiology. Am J Physiol Cell Physiol 292, C1993-2003.
    • (2007) Am J Physiol Cell Physiol , vol.292 , Issue.C1993-2003
    • Cooper, C.E.1    Giulivi, C.2
  • 21
    • 0033593029 scopus 로고    scopus 로고
    • The heme-copper oxidases of Thermus thermophilus catalyze the reduction of nitric oxide: Evolutionary implications
    • Giuffrè, A., Stubauer, G., Sarti, P., Brunori, M., Zumft, W. G., Buse, G., and Soulimane, T. (1999) The heme-copper oxidases of Thermus thermophilus catalyze the reduction of nitric oxide: evolutionary implications. Proc Natl Acad Sci U S A 96, 14718-14723.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 14718-14723
    • Giuffrè, A.1    Stubauer, G.2    Sarti, P.3    Brunori, M.4    Zumft, W.G.5    Buse, G.6    Soulimane, T.7
  • 24
    • 0028226882 scopus 로고
    • Cytochrome oxidase evolved by tinkering with denitrification enzymes
    • Saraste, M., and 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
  • 25
    • 0028083666 scopus 로고
    • The heme-copper oxidase family consists of three distinct types of terminal oxidases and is related to nitric oxide reductase
    • van der Oost, J., deBoer, A. P. N., deGier, J.-W. L, Zumft, W. G., Stouthamer, A. H., and van Spanning, R. J. M. (1994) The heme-copper oxidase family consists of three distinct types of terminal oxidases and is related to nitric oxide reductase. FEMS Microbiol. Lett. 121, 1-10.
    • (1994) FEMS Microbiol. Lett , vol.121 , pp. 1-10
    • van der Oost, J.1    deBoer, A.P.N.2    deGier, J.-W.L.3    Zumft, W.G.4    Stouthamer, A.H.5    van Spanning, R.J.M.6
  • 26
    • 0029062502 scopus 로고
    • Cytochrome bd oxidase from Azotobacter vinelandii. Purification and quantitation of ligand binding to the oxygen reduction site
    • Junemann, S., and Wrigglesworth, J. M. (1995) Cytochrome bd oxidase from Azotobacter vinelandii. Purification and quantitation of ligand binding to the oxygen reduction site. J. Biol. Chem. 270, 16213-16220.
    • (1995) J. Biol. Chem , vol.270 , pp. 16213-16220
    • Junemann, S.1    Wrigglesworth, J.M.2
  • 27
    • 0029942493 scopus 로고    scopus 로고
    • EPR Study of NO Complex of bd-type Ubiquinol Oxidase from Escherichia coli
    • Hori, H., Tsubaki, M., Mogi, T., and Anraku, Y. (1996) EPR Study of NO Complex of bd-type Ubiquinol Oxidase from Escherichia coli. J. Biol. Chem. 271, 9254-9258.
    • (1996) J. Biol. Chem , vol.271 , pp. 9254-9258
    • Hori, H.1    Tsubaki, M.2    Mogi, T.3    Anraku, Y.4
  • 28
    • 4944233196 scopus 로고    scopus 로고
    • Interaction of the bacterial terminal oxidase cytochrome bd with nitric oxide
    • Borisov, V. B., Forte, E., Konstantinov, A. A., Poole, R. K., Sarti, P., and Giuffrè, A. (2004) Interaction of the bacterial terminal oxidase cytochrome bd with nitric oxide. FEBS Lett. 576, 201-204.
    • (2004) FEBS Lett , vol.576 , pp. 201-204
    • Borisov, V.B.1    Forte, E.2    Konstantinov, A.A.3    Poole, R.K.4    Sarti, P.5    Giuffrè, A.6
  • 31
    • 0034839839 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies of the reactions of nitrogen monoxide and nitrite with ferryl myoglobin
    • Herold, S., and Rehmann, F.-J. K. (2001) Kinetic and mechanistic studies of the reactions of nitrogen monoxide and nitrite with ferryl myoglobin. J. Biol. Inorg. Chem. 6, 543-555.
    • (2001) J. Biol. Inorg. Chem , vol.6 , pp. 543-555
    • Herold, S.1    Rehmann, F.-J.K.2
  • 32
    • 0037371492 scopus 로고    scopus 로고
    • Kinetic of the reactions of nitrogen monoxide and nitrite with ferryl hemoglobin
    • Herold, S., and Rehmann, F.-J. K. (2003) Kinetic of the reactions of nitrogen monoxide and nitrite with ferryl hemoglobin. Free Radic. Biol. Med. 34, 531-545.
    • (2003) Free Radic. Biol. Med , vol.34 , pp. 531-545
    • Herold, S.1    Rehmann, F.-J.K.2
  • 35
    • 0027359220 scopus 로고
    • The gateway to the active site of heme-copper oxidases
    • Lemon, D. D., Calhoun, M. W., Gennis, R. B., and Woodruff, W. H. (1993) The gateway to the active site of heme-copper oxidases. Biochemistry 32, 11953-11956.
    • (1993) Biochemistry , vol.32 , pp. 11953-11956
    • Lemon, D.D.1    Calhoun, M.W.2    Gennis, R.B.3    Woodruff, W.H.4
  • 36
    • 0037040921 scopus 로고    scopus 로고
    • Flavorubredoxin, an inducible catalyst for nitric oxide reduction and detoxification in Escherichia coli
    • Gardner, A. M., Helmick, R. A., and Gardner, P. R. (2002) Flavorubredoxin, an inducible catalyst for nitric oxide reduction and detoxification in Escherichia coli. J Biol Chem 277, 8172-8177.
    • (2002) J Biol Chem , vol.277 , pp. 8172-8177
    • Gardner, A.M.1    Helmick, R.A.2    Gardner, P.R.3
  • 39
    • 33747813904 scopus 로고    scopus 로고
    • Borisov, V. B., Forte, E., Sarti, P., Brunori, M., Konstantinov, A. A., and Giuffrè, A. (2006) Nitric oxide reacts with the ferryl-oxo catalytic intermediate of the CuB-lacking cytochrome bd terminal oxidase. FEBS Lett 580, 4823-4826. 40. Richardson, A. R., Dunman, P. M., and Fang, F. C. (2006) The nitrosative stress respons e of Staphylococcus aureus is required for resistance to innate immunity. Mol Microbiol 61, 927-939.
    • Borisov, V. B., Forte, E., Sarti, P., Brunori, M., Konstantinov, A. A., and Giuffrè, A. (2006) Nitric oxide reacts with the ferryl-oxo catalytic intermediate of the CuB-lacking cytochrome bd terminal oxidase. FEBS Lett 580, 4823-4826. 40. Richardson, A. R., Dunman, P. M., and Fang, F. C. (2006) The nitrosative stress respons e of Staphylococcus aureus is required for resistance to innate immunity. Mol Microbiol 61, 927-939.


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