메뉴 건너뛰기




Volumn 37, Issue 4, 2009, Pages 707-712

Electrodes modified with lipid membranes to study quinone oxidoreductases

Author keywords

Coenzyme Q; Enzyme kinetics; Oxidative phosphorylation; Protein film voltammetry; Solid supported bilayer lipid membrane; Ubiquinone

Indexed keywords

OXIDOREDUCTASE; QUINONE DERIVATIVE; QUINONE OXIDOREDUCTASE; UNCLASSIFIED DRUG; MEMBRANE LIPID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE);

EID: 70349306206     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST0370707     Document Type: Conference Paper
Times cited : (10)

References (46)
  • 1
    • 28444437064 scopus 로고    scopus 로고
    • Membranes are more mosaic than fluid
    • Engelman, D.M. (2005) Membranes are more mosaic than fluid. Nature 438, 578-580
    • (2005) Nature , vol.438 , pp. 578-580
    • Engelman, D.M.1
  • 4
    • 0026716564 scopus 로고
    • On coenzyme-Q orientation in membranes: A linear dichroism study of ubiquinones in a model bilayer
    • Samori, B., Lenaz, G., Battino, M., Marconi, G. and Domini, I. (1992) On coenzyme-Q orientation in membranes: a linear dichroism study of ubiquinones in a model bilayer. J. Membr. Biol. 128, 193-203
    • (1992) J. Membr. Biol , vol.128 , pp. 193-203
    • Samori, B.1    Lenaz, G.2    Battino, M.3    Marconi, G.4    Domini, I.5
  • 6
    • 0023340216 scopus 로고
    • A method for estimating lateral diffusion-coefficients in membranes from steady-state fluorescence quenching studies
    • Blackwell, M.F., Gounaris, K., Zara, S.J. and Barber, J. (1987) A method for estimating lateral diffusion-coefficients in membranes from steady-state fluorescence quenching studies. Biophys. J. 51, 735-744
    • (1987) Biophys. J , vol.51 , pp. 735-744
    • Blackwell, M.F.1    Gounaris, K.2    Zara, S.J.3    Barber, J.4
  • 7
    • 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
  • 8
    • 0032843484 scopus 로고    scopus 로고
    • Microbial ubiquinones: Multiple roles in respiration, gene regulation and oxidative stress management
    • Soballe, B. and Poole, R.K. (1999) Microbial ubiquinones: multiple roles in respiration, gene regulation and oxidative stress management. Microbiology 145, 1817-1830
    • (1999) Microbiology , vol.145 , pp. 1817-1830
    • Soballe, B.1    Poole, R.K.2
  • 9
    • 0033928977 scopus 로고    scopus 로고
    • Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation
    • Poole, R.K. and Cook, G.M. (2000) Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation. Adv. Microb. Physiol. 43, 165-224
    • (2000) Adv. Microb. Physiol , vol.43 , pp. 165-224
    • Poole, R.K.1    Cook, G.M.2
  • 10
    • 0034693765 scopus 로고    scopus 로고
    • New insight into the structure and function of the alternative oxidase
    • Berthold, D.A., Andersson, M.E. and Nordlund, P. (2000) New insight into the structure and function of the alternative oxidase. Biochim. Biophys. Acta 1460, 241-254
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 241-254
    • Berthold, D.A.1    Andersson, M.E.2    Nordlund, P.3
  • 11
    • 33746329868 scopus 로고    scopus 로고
    • Energy converting NADH:quinone oxidoreductase (complex I)
    • Brandt, U. (2006) Energy converting NADH:quinone oxidoreductase (complex I). Annu. Rev. Biochem. 75, 69-92
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 69-92
    • Brandt, U.1
  • 12
    • 0033734197 scopus 로고    scopus 로고
    • Probing molecular structure of dioxygen reduction site of bacterial quinol oxidases through ligand binding to the redox metal centers
    • Tsubaki, M., Hori, H. and Mogi, T. (2000) Probing molecular structure of dioxygen reduction site of bacterial quinol oxidases through ligand binding to the redox metal centers. J. Inorg. Biochem. 82, 19-25
    • (2000) J. Inorg. Biochem , vol.82 , pp. 19-25
    • Tsubaki, M.1    Hori, H.2    Mogi, T.3
  • 14
    • 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
  • 15
    • 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
  • 16
    • 0022822118 scopus 로고
    • Purification and reconstitution of the cytochrome o-type oxidase from Escherichia coli
    • Matsushita, K., Patel, L. and Kaback, H.R. (1986) Purification and reconstitution 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
  • 17
    • 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
  • 18
    • 0021280149 scopus 로고
    • 562-o complex from cells in the early exponential phase of aerobic growth
    • 562-o 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
  • 19
    • 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
  • 20
    • 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
  • 21
    • 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
    • Sato-Watanabe, 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
    • Sato-Watanabe, M.1    Mogi, T.2    Miyoshi, H.3    Iwamura, H.4    Matsushita, K.5    Adachi, O.6    Anraku, Y.7
  • 22
    • 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
  • 24
    • 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
  • 26
    • 0000559465 scopus 로고
    • Reconstitution of cell membrane structure in vitro and its transformation into an excitable system
    • Mueller, P., Rudin, D.O., Tien, H.T. and Wescott, W.C. (1962) Reconstitution of cell membrane structure in vitro and its transformation into an excitable system. Nature 194, 979-980
    • (1962) Nature , vol.194 , pp. 979-980
    • Mueller, P.1    Rudin, D.O.2    Tien, H.T.3    Wescott, W.C.4
  • 27
    • 33750302132 scopus 로고    scopus 로고
    • Solid supported lipid bilayers: From biophysical studies to sensor design
    • Castellana, E.T. and Cremer, P.S. (2006) Solid supported lipid bilayers: from biophysical studies to sensor design. Surf. Sci. Rep. 61, 429-444
    • (2006) Surf. Sci. Rep , vol.61 , pp. 429-444
    • Castellana, E.T.1    Cremer, P.S.2
  • 28
    • 26944478236 scopus 로고    scopus 로고
    • Polymer-supported membranes as models of the cell surface
    • Tanaka, M. and Sackmann, E. (2005) Polymer-supported membranes as models of the cell surface. Nature 437, 656-663
    • (2005) Nature , vol.437 , pp. 656-663
    • Tanaka, M.1    Sackmann, E.2
  • 29
    • 0033637072 scopus 로고    scopus 로고
    • Molecular transport and organization in supported lipid membranes
    • Boxer, S.G. (2000) Molecular transport and organization in supported lipid membranes. Curr. Opin. Chem. Biol. 4, 704-709
    • (2000) Curr. Opin. Chem. Biol , vol.4 , pp. 704-709
    • Boxer, S.G.1
  • 30
    • 33646948800 scopus 로고    scopus 로고
    • Transport across artificial membranes: An analytical perspective
    • Janshoff, A. and Steinem, C. (2006) Transport across artificial membranes: an analytical perspective. Anal. Bioanal. Chem. 385, 433-451
    • (2006) Anal. Bioanal. Chem , vol.385 , pp. 433-451
    • Janshoff, A.1    Steinem, C.2
  • 31
    • 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
  • 36
    • 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
  • 37
    • 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
  • 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
    • 49049115593 scopus 로고    scopus 로고
    • Direct electrochemistry of redox enzymes as a tool for mechanistic studies
    • Leger, C. and Bertrand, P. (2008) Direct electrochemistry of redox enzymes as a tool for mechanistic studies. Chem. Rev. 108, 2379-2438
    • (2008) Chem. Rev , vol.108 , pp. 2379-2438
    • Leger, C.1    Bertrand, P.2
  • 40
    • 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
  • 41
    • 50949128131 scopus 로고    scopus 로고
    • Direct and mediated electron transfer between intact succinate: Quinone oxidoreductase from Bacillus subtilis and a surface modified gold electrode reveals redox state-dependent conformational changes
    • Christenson, A., Gustavsson, T., Gorton, L. and Hagerhall, C. (2008) Direct and mediated electron transfer between intact succinate: quinone oxidoreductase from Bacillus subtilis and a surface modified gold electrode reveals redox state-dependent conformational changes. Biochim. Biophys. Acta 1777, 1203-1210
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1203-1210
    • Christenson, A.1    Gustavsson, T.2    Gorton, L.3    Hagerhall, C.4
  • 42
    • 1642453844 scopus 로고    scopus 로고
    • Voltammetric studies of the catalytic mechanism of the respiratory nitrate reductase from Escherichia coli: How nitrate reduction and inhibition depend on the oxidation state of the active site
    • Elliott, S.J., Hoke, K.R., Heffron, K., Palak, M., Rothery, R.A., Weiner, J.H. and Armstrong, F.A. (2004) Voltammetric studies of the catalytic mechanism of the respiratory nitrate reductase from Escherichia coli: how nitrate reduction and inhibition depend on the oxidation state of the active site. Biochemistry 43, 799-807
    • (2004) Biochemistry , vol.43 , pp. 799-807
    • Elliott, S.J.1    Hoke, K.R.2    Heffron, K.3    Palak, M.4    Rothery, R.A.5    Weiner, J.H.6    Armstrong, F.A.7
  • 43
    • 33747757594 scopus 로고    scopus 로고
    • Kinetics of bimolecular reactions in model bilayers and biological membranes: A critical review
    • Melo, E. and Martins, J. (2006) Kinetics of bimolecular reactions in model bilayers and biological membranes: a critical review. Biophys. Chem. 123, 77-94
    • (2006) Biophys. Chem , vol.123 , pp. 77-94
    • Melo, E.1    Martins, J.2
  • 45
    • 0031042359 scopus 로고    scopus 로고
    • Proton pumping of mitochondrial complex I: Differential activation by analogs of ubiquinone
    • Helfenbaum, L., Ngo, A., Ghelli, A., Linnane, A.W. and Esposti, M.D. (1997) Proton pumping of mitochondrial complex I: differential activation by analogs of ubiquinone. J. Bioenerg. Biomembr. 29, 71-80
    • (1997) J. Bioenerg. Biomembr , vol.29 , pp. 71-80
    • Helfenbaum, L.1    Ngo, A.2    Ghelli, A.3    Linnane, A.W.4    Esposti, M.D.5
  • 46
    • 57449099513 scopus 로고    scopus 로고
    • Impedance spectroscopy of bacterial membranes: Coenzyme-Q diffusion in a finite diffusion layer
    • Jeuken, L.J.C., Weiss, S.A., Henderson, P.J.F., Evans, S.D. and Bushby, R.J. (2008) Impedance spectroscopy of bacterial membranes: coenzyme-Q diffusion in a finite diffusion layer. Anal. Chem. 80, 9084-9090
    • (2008) Anal. Chem , vol.80 , pp. 9084-9090
    • Jeuken, L.J.C.1    Weiss, S.A.2    Henderson, P.J.F.3    Evans, S.D.4    Bushby, R.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.