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Volumn 417, Issue 2, 2009, Pages 555-560

Characterization of cytochrome bo3 activity in a native-like surface-tethered membrane

Author keywords

Cytochrome bo3; Quinone pool; Tethered bilayer; Ubiquinol oxidase

Indexed keywords

CONCENTRATION OF; CYTOCHROME BO3; E. COLI; ELECTRON TRANSFER; FUNCTIONALIZED; GOLD ELECTRODES; HYDROPHOBIC SUBSTRATE; MEMBRANE MODELS; MICHAELIS-MENTEN KINETIC; QUINONE POOL; TERMINAL OXIDASE; TETHERED BILAYER; TETHERED MEMBRANES; TRANSMEMBRANE; UBIQUINOL; UBIQUINOL OXIDASE;

EID: 58249088448     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20081345     Document Type: Article
Times cited : (25)

References (48)
  • 1
    • 0030738589 scopus 로고    scopus 로고
    • Alternative respiratory pathways of Escherichia coli: Energetics and transcriptional regulation in response to electron acceptors
    • Unden, G. and Bongaerts, J. (1997) Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim. Biophys. Acta 1320, 217-234
    • (1997) Biochim. Biophys. Acta , vol.1320 , pp. 217-234
    • Unden, G.1    Bongaerts, J.2
  • 2
    • 0019490792 scopus 로고
    • Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implications
    • Collins, M. D. and Jones, D. (1981) Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implications. Microbiol. Rev. 45, 316-354
    • (1981) Microbiol. Rev , vol.45 , pp. 316-354
    • Collins, M.D.1    Jones, D.2
  • 4
    • 0001383847 scopus 로고
    • The aerobic respiratory chain of Escherichia coli
    • Anraku, Y. and Gennis, R. B. (1987) The aerobic respiratory chain of Escherichia coli. Trends Biochem. Sci. 12, 262-266
    • (1987) Trends Biochem. Sci , vol.12 , pp. 262-266
    • Anraku, Y.1    Gennis, R.B.2
  • 7
    • 0027996364 scopus 로고
    • Identification of a novel quinone-binding site in the cytochrome bo complex from Escherichia coli
    • Satowatanabe, M., Mogi, T., Ogura, T., Kitagawa, T., Miyoshi, H., Iwamura, H. and Anraku, Y. (1994) Identification of a novel quinone-binding site in the cytochrome bo complex from Escherichia coli. J. Biol. Chem. 269, 28908-28912
    • (1994) J. Biol. Chem , vol.269 , pp. 28908-28912
    • Satowatanabe, M.1    Mogi, T.2    Ogura, T.3    Kitagawa, T.4    Miyoshi, H.5    Iwamura, H.6    Anraku, Y.7
  • 8
    • 0028143052 scopus 로고
    • Structure-function studies on the ubiquinol oxidation site of the cytochrome bo complex from Escherichia coli using p-benzoquinones and substituted phenols
    • Satowatanabe, M., Mogi, T., Miyoshi, H., Iwamura, H., Matsushita, K., Adachi, O. and Anraku, Y. (1994) Structure-function studies on the ubiquinol oxidation site of the cytochrome bo complex from Escherichia coli using p-benzoquinones and substituted phenols. J. Biol. Chem. 269, 28899-28907
    • (1994) J. Biol. Chem , vol.269 , pp. 28899-28907
    • Satowatanabe, M.1    Mogi, T.2    Miyoshi, H.3    Iwamura, H.4    Matsushita, K.5    Adachi, O.6    Anraku, Y.7
  • 9
    • 0023852761 scopus 로고
    • A simple method for the determination of the kinetic constants of membrane enzymes utilizing hydrophobic substrates: Ubiquinol cytochrome c reductase
    • Fato, R., Castelluccio, C., Palmer, G. and Lenaz, G. (1988) A simple method for the determination of the kinetic constants of membrane enzymes utilizing hydrophobic substrates: ubiquinol cytochrome c reductase. Biochim. Biophys. Acta 932, 216-222
    • (1988) Biochim. Biophys. Acta , vol.932 , pp. 216-222
    • Fato, R.1    Castelluccio, C.2    Palmer, G.3    Lenaz, G.4
  • 10
    • 0029910353 scopus 로고    scopus 로고
    • Probing substrate binding site of the Escherichia coli quinol oxidases using synthetic ubiquinol analogues
    • Sakamoto, K., Miyoshi, H., Takegami, K., Mogi, T., Anraku, Y. and Iwamura, H. (1996) Probing substrate binding site of the Escherichia coli quinol oxidases using synthetic ubiquinol analogues. J. Biol. Chem. 271, 29897-29902
    • (1996) J. Biol. Chem , vol.271 , pp. 29897-29902
    • Sakamoto, K.1    Miyoshi, H.2    Takegami, K.3    Mogi, T.4    Anraku, Y.5    Iwamura, H.6
  • 11
    • 0020023005 scopus 로고
    • The active form of cytochrome c oxidase: Effects of detergent, the intact membrane, and radiation inactivation
    • Thompson, D. A., Suarez-Villafane, M. and Ferguson-Miller, S. (1982) The active form of cytochrome c oxidase: effects of detergent, the intact membrane, and radiation inactivation. Biophys. J. 37, 285-293
    • (1982) Biophys. J , vol.37 , pp. 285-293
    • Thompson, D.A.1    Suarez-Villafane, M.2    Ferguson-Miller, S.3
  • 12
    • 0021280149 scopus 로고
    • 562o complex from cells in the early exponential phase of aerobic growth
    • 562o complex from cells in the early exponential phase of aerobic growth. J. Biol. Chem. 259, 3368-3374
    • (1984) J. Biol. Chem , vol.259 , pp. 3368-3374
    • Kita, K.1    Konishi, K.2    Anraku, Y.3
  • 13
    • 0022822118 scopus 로고
    • Purification and teconstitution of the cytochrome-o type oxidase from Escherichia coli
    • Matsushita, K., Patel, L. and Kaback, H. R. (1986) Purification and teconstitution of the cytochrome-o type oxidase from Escherichia coli. Methods Enzymol. 126, 113-122
    • (1986) Methods Enzymol , vol.126 , pp. 113-122
    • Matsushita, K.1    Patel, L.2    Kaback, H.R.3
  • 14
    • 35748951001 scopus 로고    scopus 로고
    • Biomimetic tethered lipid membranes designed for membrane-protein interaction studies
    • Rossi, C. and Chopineau, J. (2007) Biomimetic tethered lipid membranes designed for membrane-protein interaction studies. Eur. Biophys. J. Biophys. Lett. 36, 955-965
    • (2007) Eur. Biophys. J. Biophys. Lett , vol.36 , pp. 955-965
    • Rossi, C.1    Chopineau, J.2
  • 15
    • 36549043460 scopus 로고    scopus 로고
    • Model membrane systems and their applications
    • Chan, Y. H. M. and Boxer, S. G. (2007) Model membrane systems and their applications. Curr. Opin. Chem. Biol. 11, 581-587
    • (2007) Curr. Opin. Chem. Biol , vol.11 , pp. 581-587
    • Chan, Y.H.M.1    Boxer, S.G.2
  • 16
    • 0030739753 scopus 로고    scopus 로고
    • The design and synthesis of simple molecular tethers for binding biomembranes to a gold surface
    • Boden, N., Bushby, R. J., Clarkson, S., Evans, S. D., Knowles, P. F. and Marsh, A. (1997) The design and synthesis of simple molecular tethers for binding biomembranes to a gold surface. Tetrahedron 53, 10939-10952
    • (1997) Tetrahedron , vol.53 , pp. 10939-10952
    • Boden, N.1    Bushby, R.J.2    Clarkson, S.3    Evans, S.D.4    Knowles, P.F.5    Marsh, A.6
  • 17
    • 0037434143 scopus 로고    scopus 로고
    • Archaea analogue thiolipids for tethered bilayer lipid membranes on ultrasmooth gold surfaces
    • Schiller, S. M., Naumann, R., Lovejoy, K., Kunz, H. and Knoll, W. (2003) Archaea analogue thiolipids for tethered bilayer lipid membranes on ultrasmooth gold surfaces. Angew. Chem. Int. Edit. 42, 208-211
    • (2003) Angew. Chem. Int. Edit , vol.42 , pp. 208-211
    • Schiller, S.M.1    Naumann, R.2    Lovejoy, K.3    Kunz, H.4    Knoll, W.5
  • 19
    • 34548820167 scopus 로고    scopus 로고
    • Insulating tethered bilayer lipid membranes to study membrane proteins
    • Koper, I. (2007) Insulating tethered bilayer lipid membranes to study membrane proteins. Mol. Biosyst. 3, 651-657
    • (2007) Mol. Biosyst , vol.3 , pp. 651-657
    • Koper, I.1
  • 20
    • 16244366777 scopus 로고    scopus 로고
    • Recent developments in dynamic electrochemical studies of adsorbed enzymes and their active sites
    • Armstrong, F. A. (2005) Recent developments in dynamic electrochemical studies of adsorbed enzymes and their active sites. Curr. Opin. Chem. Biol. 9, 110-117
    • (2005) Curr. Opin. Chem. Biol , vol.9 , pp. 110-117
    • Armstrong, F.A.1
  • 22
    • 67649850909 scopus 로고    scopus 로고
    • Dodd, C. E., Johnson, B. R. G., Jeuken, L. J. C., Bugg, T. D. H., Bushby, R. J. and Evans, S. D. (2008) Native E. coli inner membrane incorporation in solid supported lipid bilayer membranes. Biointerphases 3, FA59-FA67
    • Dodd, C. E., Johnson, B. R. G., Jeuken, L. J. C., Bugg, T. D. H., Bushby, R. J. and Evans, S. D. (2008) Native E. coli inner membrane incorporation in solid supported lipid bilayer membranes. Biointerphases 3, FA59-FA67
  • 23
    • 0342378077 scopus 로고    scopus 로고
    • 3 from Escherichia coli and demonstration that associated quinone is not required for the structural integrity of the oxidase
    • 3 from Escherichia coli and demonstration that associated quinone is not required for the structural integrity of the oxidase. Biochim. Biophys. Acta 1340, 131-142
    • (1997) Biochim. Biophys. Acta , vol.1340 , pp. 131-142
    • Rumbley, J.N.1    Nickels, E.F.2    Gennis, R.B.3
  • 24
    • 0014879933 scopus 로고
    • Protein composition of cell wall and cytoplasmic membrane of Escherichia coli
    • Schnaitman, C. A. (1970) Protein composition of cell wall and cytoplasmic membrane of Escherichia coli. J. Bacteriol. 104, 890-901
    • (1970) J. Bacteriol , vol.104 , pp. 890-901
    • Schnaitman, C.A.1
  • 25
    • 0015716692 scopus 로고
    • Rapid, sensitive, and specific method for determination of protein in dilute solution
    • Schaffner, W. and Weissman, C. (1973) Rapid, sensitive, and specific method for determination of protein in dilute solution. Anal. Biochem. 56, 502-514
    • (1973) Anal. Biochem , vol.56 , pp. 502-514
    • Schaffner, W.1    Weissman, C.2
  • 26
    • 33947726133 scopus 로고    scopus 로고
    • Proton transport into a tethered bilayer lipid membrane
    • Jeuken, L. J. C., Bushby, R. J. and Evans, S. D. (2007) Proton transport into a tethered bilayer lipid membrane. Electrochem. Commun. 9, 610-614
    • (2007) Electrochem. Commun , vol.9 , pp. 610-614
    • Jeuken, L.J.C.1    Bushby, R.J.2    Evans, S.D.3
  • 27
    • 0030156804 scopus 로고    scopus 로고
    • Electrochemistry at ultrathin organic films at planar gold electrodes
    • Lindholm Sethson, B. (1996) Electrochemistry at ultrathin organic films at planar gold electrodes. Langmuir 12, 3305-3314
    • (1996) Langmuir , vol.12 , pp. 3305-3314
    • Lindholm Sethson, B.1
  • 28
    • 0031920484 scopus 로고    scopus 로고
    • Electrochemical measurement of lateral diffusion coefficients of ubiquinones and plastoquinones of various isoprenoid chain lengths incorporated in model bilayers
    • Marchal, D., Boireau, W., Laval, J. M., Moiroux, J. and Bourdillon, C. (1998) Electrochemical measurement of lateral diffusion coefficients of ubiquinones and plastoquinones of various isoprenoid chain lengths incorporated in model bilayers. Biophys. J. 74, 1937-1948
    • (1998) Biophys. J , vol.74 , pp. 1937-1948
    • Marchal, D.1    Boireau, W.2    Laval, J.M.3    Moiroux, J.4    Bourdillon, C.5
  • 29
    • 0035814806 scopus 로고    scopus 로고
    • Rate constants in two dimensions of electron transfer between pyruvate oxidase, a membrane enzyme, and ubiquinone (coenzyme Q(8)), its water-insoluble electron carrier
    • Marchal, D., Pantigny, J., Laval, J. M., Moiroux, J. and Bourdillon, C. (2001) Rate constants in two dimensions of electron transfer between pyruvate oxidase, a membrane enzyme, and ubiquinone (coenzyme Q(8)), its water-insoluble electron carrier. Biochemistry 40, 1248-1256
    • (2001) Biochemistry , vol.40 , pp. 1248-1256
    • Marchal, D.1    Pantigny, J.2    Laval, J.M.3    Moiroux, J.4    Bourdillon, C.5
  • 30
    • 0028909392 scopus 로고    scopus 로고
    • m values for oxygen are in the submicromolar range. J. Bacteriol. 177, 867-870
    • m values for oxygen are in the submicromolar range. J. Bacteriol. 177, 867-870
  • 32
    • 0017858515 scopus 로고
    • Oxygen limited continuous culture and respiratory energy: Conservation in Escherichia coli
    • Rice, C. W. and Hempfling, W. P. (1978) Oxygen limited continuous culture and respiratory energy: conservation in Escherichia coli. J. Bacteriol. 134, 115-124
    • (1978) J. Bacteriol , vol.134 , pp. 115-124
    • Rice, C.W.1    Hempfling, W.P.2
  • 33
    • 0022821977 scopus 로고
    • Purification and properties of 2 terminal oxidase complexes of Escherichia coli aerobic respiratory chain
    • Kita, K., Konishi, K. and Anraku, Y. (1986) Purification and properties of 2 terminal oxidase complexes of Escherichia coli aerobic respiratory chain. Methods Enzymol. 126, 94-113
    • (1986) Methods Enzymol , vol.126 , pp. 94-113
    • Kita, K.1    Konishi, K.2    Anraku, Y.3
  • 34
    • 0030851244 scopus 로고    scopus 로고
    • Comparison of the ligand-binding properties of native and copper-less cytochromes bo from Escherichia coli
    • Moody, A. J., Mitchell, R., Jeal, A. E. and Rich, P. R. (1997) Comparison of the ligand-binding properties of native and copper-less cytochromes bo from Escherichia coli. Biochem. J. 324, 743-752
    • (1997) Biochem. J , vol.324 , pp. 743-752
    • Moody, A.J.1    Mitchell, R.2    Jeal, A.E.3    Rich, P.R.4
  • 35
    • 0032573198 scopus 로고    scopus 로고
    • Role of the isoprenyl tail of ubiquinone in reaction with respiratory enzymes: Studies with bovine heart mitochondrial complex I and Escherichia coli bo-type ubiquinol oxidase
    • Sakamoto, K., Miyoshi, H., Ohshima, M., Kuwabara, K., Kano, K., Akagi, T., Mogi, T. and Iwamura, H. (1998) Role of the isoprenyl tail of ubiquinone in reaction with respiratory enzymes: studies with bovine heart mitochondrial complex I and Escherichia coli bo-type ubiquinol oxidase. Biochemistry 37, 15106-15113
    • (1998) Biochemistry , vol.37 , pp. 15106-15113
    • Sakamoto, K.1    Miyoshi, H.2    Ohshima, M.3    Kuwabara, K.4    Kano, K.5    Akagi, T.6    Mogi, T.7    Iwamura, H.8
  • 36
    • 0026700972 scopus 로고
    • Modified, large-scale purification of the cytochrome o complex (bo-type oxidase) of Escherichia coli yields a 2 heme one copper terminal oxidase with high specific activity
    • Minghetti, K. C., Goswitz, V. C., Gabriel, N. E., Hill, J. J., Barassi, C. A., Georgiou, C. D., Chan, S. I. and Gennis, R. B. (1992) Modified, large-scale purification of the cytochrome o complex (bo-type oxidase) of Escherichia coli yields a 2 heme one copper terminal oxidase with high specific activity. Biochemistry 31, 6917-6924
    • (1992) Biochemistry , vol.31 , pp. 6917-6924
    • Minghetti, K.C.1    Goswitz, V.C.2    Gabriel, N.E.3    Hill, J.J.4    Barassi, C.A.5    Georgiou, C.D.6    Chan, S.I.7    Gennis, R.B.8
  • 37
    • 33745641297 scopus 로고    scopus 로고
    • Kinetic mechanism of quinol oxidation by cytochrome bd studied with ubiquinone-2 analogs
    • Matsumoto, Y., Muneyuki, E., Fujita, D., Sakamoto, K., Miyoshi, H., Yoshida, M. and Mogi, T. (2006) Kinetic mechanism of quinol oxidation by cytochrome bd studied with ubiquinone-2 analogs. J. Biochem. 139, 779-788
    • (2006) J. Biochem , vol.139 , pp. 779-788
    • Matsumoto, Y.1    Muneyuki, E.2    Fujita, D.3    Sakamoto, K.4    Miyoshi, H.5    Yoshida, M.6    Mogi, T.7
  • 38
    • 14044268662 scopus 로고    scopus 로고
    • Direct electrochemical interaction between a modified gold electrode and a bacterial membrane extract
    • Jeuken, L. J. C., Connell, S. D., Nurnabi, M., O'Reilly, J., Henderson, P. J. F., Evans, S. D. and Bushby, R. J. (2005) Direct electrochemical interaction between a modified gold electrode and a bacterial membrane extract. Langmuir 21, 1481-1488
    • (2005) Langmuir , vol.21 , pp. 1481-1488
    • Jeuken, L.J.C.1    Connell, S.D.2    Nurnabi, M.3    O'Reilly, J.4    Henderson, P.J.F.5    Evans, S.D.6    Bushby, R.J.7
  • 39
    • 18844455281 scopus 로고    scopus 로고
    • Self-assembly of solid-supported membranes using a triggered fusion of phospholipid-enriched proteoliposomes prepared from the inner mitochondrial membrane
    • Elie-Caille, C., Fliniaux, O., Pantigny, J., Maziere, J. C. and Bourdillon, C. (2005) Self-assembly of solid-supported membranes using a triggered fusion of phospholipid-enriched proteoliposomes prepared from the inner mitochondrial membrane. Langmuir 21, 4661-4668
    • (2005) Langmuir , vol.21 , pp. 4661-4668
    • Elie-Caille, C.1    Fliniaux, O.2    Pantigny, J.3    Maziere, J.C.4    Bourdillon, C.5
  • 40
    • 43049173742 scopus 로고    scopus 로고
    • Fabrication of highly insulating tethered bilayer lipid membrane using yeast cell membrane fractions for measuring ion channel activity
    • Jadhav, S. R., Sui, D., Garavito, R. M. and Worden, R. M. (2008) Fabrication of highly insulating tethered bilayer lipid membrane using yeast cell membrane fractions for measuring ion channel activity. J. Colloid Interface Sci. 322, 465-472
    • (2008) J. Colloid Interface Sci , vol.322 , pp. 465-472
    • Jadhav, S.R.1    Sui, D.2    Garavito, R.M.3    Worden, R.M.4
  • 41
    • 0032530646 scopus 로고    scopus 로고
    • Isolation and characterizations of quinone analogue-resistant mutants of bo-type ubiquinol oxidase from Escherichia coli
    • Sato-Watanabe, M., Mogi, T., Sakamoto, K., Miyoshi, H. and Anraku, Y. (1998) Isolation and characterizations of quinone analogue-resistant mutants of bo-type ubiquinol oxidase from Escherichia coli. Biochemistry 37, 12744-12752
    • (1998) Biochemistry , vol.37 , pp. 12744-12752
    • Sato-Watanabe, M.1    Mogi, T.2    Sakamoto, K.3    Miyoshi, H.4    Anraku, Y.5
  • 43
    • 0026778904 scopus 로고
    • Saturation kinetics of coenzyme-Q in NADH and succinate oxidation in beef-heart mitochondria
    • Estornell, E., Fato, R., Castelluccio, C., Cavazzoni, M., Castelli, G. P. and Lenaz, G. (1992) Saturation kinetics of coenzyme-Q in NADH and succinate oxidation in beef-heart mitochondria. FEBS Lett. 311, 107-109
    • (1992) FEBS Lett , vol.311 , pp. 107-109
    • Estornell, E.1    Fato, R.2    Castelluccio, C.3    Cavazzoni, M.4    Castelli, G.P.5    Lenaz, G.6
  • 44
    • 0016288208 scopus 로고
    • Studies with ubiquinone-depleted submitochondrial particles: Quantitative incorporation of small amounts of ubiquinone and its effects on NAHD and succinate oxidase activities
    • Norling, B., Glazek, E., Nelson, B. D. and Ernster, L. (1974) Studies with ubiquinone-depleted submitochondrial particles: quantitative incorporation of small amounts of ubiquinone and its effects on NAHD and succinate oxidase activities. Eur. J. Biochem. 47, 475-482
    • (1974) Eur. J. Biochem , vol.47 , pp. 475-482
    • Norling, B.1    Glazek, E.2    Nelson, B.D.3    Ernster, L.4
  • 45
    • 33745617033 scopus 로고    scopus 로고
    • DSC and Raman studies of the side chain length effect of ubiquinones on the thermotropic phase behavior of liposomes
    • Roche, Y., Peretti, P. and Bernard, S. (2006) DSC and Raman studies of the side chain length effect of ubiquinones on the thermotropic phase behavior of liposomes. Thermochim. Acta 447, 81-88
    • (2006) Thermochim. Acta , vol.447 , pp. 81-88
    • Roche, Y.1    Peretti, P.2    Bernard, S.3
  • 46
    • 33646810851 scopus 로고    scopus 로고
    • Influence of the chain length of ubiquinones on their interaction with DPPC in mixed monolayers
    • Roche, Y., Peretti, P. and Bernard, S. (2006) Influence of the chain length of ubiquinones on their interaction with DPPC in mixed monolayers. Biochim. Biophys. Acta 1758, 468-478
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 468-478
    • Roche, Y.1    Peretti, P.2    Bernard, S.3
  • 48
    • 0031306837 scopus 로고    scopus 로고
    • Kinetics of membrane-bound nitrate reductase A from Escherichia coli with analogues of physiological electron donors: Different reaction sites for menadiol and duroquinol
    • Giordani, R., Buc, J., Cornish-Bowden, A. and Cardenas, M. L. (1997) Kinetics of membrane-bound nitrate reductase A from Escherichia coli with analogues of physiological electron donors: different reaction sites for menadiol and duroquinol. Eur. J. Biochem. 250, 567-577
    • (1997) Eur. J. Biochem , vol.250 , pp. 567-577
    • Giordani, R.1    Buc, J.2    Cornish-Bowden, A.3    Cardenas, M.L.4


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