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Volumn 56, Issue 2, 2007, Pages 189-196

Biophysical and biochemical characterization of reconstituted and purified Rhodobacter sphaeroides cytochrome c oxidase in phospholipid vesicles sheds insight into its functional oligomeric structure

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C OXIDASE; LIPOSOME; PHOSPHOLIPID; PROTON;

EID: 35448978743     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.07.012     Document Type: Article
Times cited : (7)

References (44)
  • 1
    • 33746349218 scopus 로고    scopus 로고
    • Energy transduction: proton transfer through the respiratory complexes
    • Hosler J.P., Ferguson-Miller S., and Mills D.A. Energy transduction: proton transfer through the respiratory complexes. Annu. Rev. Biochem. 75 (2006) 165-187
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 165-187
    • Hosler, J.P.1    Ferguson-Miller, S.2    Mills, D.A.3
  • 2
    • 0026615058 scopus 로고
    • 3 of Rhodobacter sphaeroides as a model for mitochondrial cytochrome c oxidase. The coxII/coxIII operon codes for structural and assembly proteins homologous to those in yeast
    • 3 of Rhodobacter sphaeroides as a model for mitochondrial cytochrome c oxidase. The coxII/coxIII operon codes for structural and assembly proteins homologous to those in yeast. J. Biol. Chem. 267 (1992) 24273-24278
    • (1992) J. Biol. Chem. , vol.267 , pp. 24273-24278
    • Cao, J.1    Hosler, J.2    Shapleigh, J.3    Revzin, A.4    Ferguson-Miller, S.5
  • 3
    • 0026615057 scopus 로고
    • 3 of Rhodobacter sphaeroides as a model for mitochondrial cytochrome c oxidase. Purification, kinetics, proton pumping, and spectral analysis
    • 3 of Rhodobacter sphaeroides as a model for mitochondrial cytochrome c oxidase. Purification, kinetics, proton pumping, and spectral analysis. J. Biol. Chem. 267 (1992) 24264-24272
    • (1992) J. Biol. Chem. , vol.267 , pp. 24264-24272
    • Hosler, J.P.1    Fetter, J.2    Tecklenburg, M.M.3    Espe, M.4    Lerma, C.5    Ferguson-Miller, S.6
  • 6
    • 0035852838 scopus 로고    scopus 로고
    • C-terminal truncation and histidine-tagging of cytochrome c oxidase subunit II reveals the native processing site, shows involvement of the C-terminus in cytochrome c binding, and improves the assay for proton pumping
    • Hiser C., Mills D.A., Schall M., and Ferguson-Miller S. C-terminal truncation and histidine-tagging of cytochrome c oxidase subunit II reveals the native processing site, shows involvement of the C-terminus in cytochrome c binding, and improves the assay for proton pumping. Biochemistry 40 (2001) 1606-1615
    • (2001) Biochemistry , vol.40 , pp. 1606-1615
    • Hiser, C.1    Mills, D.A.2    Schall, M.3    Ferguson-Miller, S.4
  • 7
    • 33845573535 scopus 로고    scopus 로고
    • Altering conserved lipid binding sites in cytochrome c oxidase of Rhodobacter sphaeroides perturbs the interaction between subunits I and III and promotes suicide inactivation
    • Varanasi L., Mills D., Murphree A., Gray J., Purser C., Baker R., and Hosler J. Altering conserved lipid binding sites in cytochrome c oxidase of Rhodobacter sphaeroides perturbs the interaction between subunits I and III and promotes suicide inactivation. Biochemistry 45 (2006) 14896-14907
    • (2006) Biochemistry , vol.45 , pp. 14896-14907
    • Varanasi, L.1    Mills, D.2    Murphree, A.3    Gray, J.4    Purser, C.5    Baker, R.6    Hosler, J.7
  • 9
    • 0033514982 scopus 로고    scopus 로고
    • Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen
    • Jasaitis A., Verkhovsky M.I., Morgan J.E., Verkhovskaya M.L., and Wikstrom M. Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen. Biochemistry 38 (1999) 2697-2706
    • (1999) Biochemistry , vol.38 , pp. 2697-2706
    • Jasaitis, A.1    Verkhovsky, M.I.2    Morgan, J.E.3    Verkhovskaya, M.L.4    Wikstrom, M.5
  • 10
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • Svensson-Ek M., Abramson J., Larsson G., Tornroth S., Brzezinski P., and Iwata S. The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides. J. Mol. Biol. 321 (2002) 329-339
    • (2002) J. Mol. Biol. , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Tornroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 11
    • 33750807024 scopus 로고    scopus 로고
    • Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase
    • Qin L., Hiser C., Mulichak A., Garavito R.M., and Ferguson-Miller S. Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase. Proc. Natl. Acad. Sci. USA 103 (2006) 16117-16122
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16117-16122
    • Qin, L.1    Hiser, C.2    Mulichak, A.3    Garavito, R.M.4    Ferguson-Miller, S.5
  • 12
    • 0033585083 scopus 로고    scopus 로고
    • The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction
    • Harrenga A., and Michel H. The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction. J. Biol. Chem. 274 (1999) 33296-33299
    • (1999) J. Biol. Chem. , vol.274 , pp. 33296-33299
    • Harrenga, A.1    Michel, H.2
  • 13
    • 0028890031 scopus 로고    scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S., Ostermeier C., Ludwig B., and Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376 (2002) 660-669
    • (2002) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 15
    • 0027731932 scopus 로고
    • Detection of bovine heart mitochondrial cytochrome c oxidase dimers in Triton X-100 and phospholipid vesicles by chemical cross-linking
    • Estey L.A., and Prochaska L.J. Detection of bovine heart mitochondrial cytochrome c oxidase dimers in Triton X-100 and phospholipid vesicles by chemical cross-linking. Biochemistry 32 (1993) 13270-13276
    • (1993) Biochemistry , vol.32 , pp. 13270-13276
    • Estey, L.A.1    Prochaska, L.J.2
  • 16
    • 0037007002 scopus 로고    scopus 로고
    • Cholate-induced dimerization of detergent- or phospholipid-solubilized bovine cytochrome c oxidase
    • Musatov A., and Robinson N.C. Cholate-induced dimerization of detergent- or phospholipid-solubilized bovine cytochrome c oxidase. Biochemistry 41 (2002) 4371-4376
    • (2002) Biochemistry , vol.41 , pp. 4371-4376
    • Musatov, A.1    Robinson, N.C.2
  • 17
    • 0035823541 scopus 로고    scopus 로고
    • Exposure of bovine cytochrome c oxidase to high triton X-100 or to alkaline conditions causes a dramatic change in the rate of reduction of compound F
    • Sadoski R.C., Zaslavsky D., Gennis R.B., Durham B., and Millett F. Exposure of bovine cytochrome c oxidase to high triton X-100 or to alkaline conditions causes a dramatic change in the rate of reduction of compound F. J. Biol. Chem. 276 (2001) 33616-33620
    • (2001) J. Biol. Chem. , vol.276 , pp. 33616-33620
    • Sadoski, R.C.1    Zaslavsky, D.2    Gennis, R.B.3    Durham, B.4    Millett, F.5
  • 18
    • 23244466489 scopus 로고    scopus 로고
    • An arginine to lysine mutation in the vicinity of the heme propionates affects the redox potentials of the hemes and associated electron and proton transfer in cytochrome c oxidase
    • Mills D.A., Geren L., Hiser C., Schmidt B., Durham B., Millett F., and Ferguson-Miller S. An arginine to lysine mutation in the vicinity of the heme propionates affects the redox potentials of the hemes and associated electron and proton transfer in cytochrome c oxidase. Biochemistry 44 (2005) 10457-10465
    • (2005) Biochemistry , vol.44 , pp. 10457-10465
    • Mills, D.A.1    Geren, L.2    Hiser, C.3    Schmidt, B.4    Durham, B.5    Millett, F.6    Ferguson-Miller, S.7
  • 19
    • 33645101080 scopus 로고    scopus 로고
    • An evaluation of methods for the reconstitution of cytochromes P450 and NADPH P450 reductase into lipid vesicles
    • Reed J.R., Kelley R.W., and Backes W.L. An evaluation of methods for the reconstitution of cytochromes P450 and NADPH P450 reductase into lipid vesicles. Drug. Metab. Dispos. 34 (2006) 660-666
    • (2006) Drug. Metab. Dispos. , vol.34 , pp. 660-666
    • Reed, J.R.1    Kelley, R.W.2    Backes, W.L.3
  • 20
    • 0028885093 scopus 로고
    • Reconstitution of purified P-glycoprotein into liposomes
    • Naito M., and Tsuruo T. Reconstitution of purified P-glycoprotein into liposomes. J. Cancer Res. Clin. Oncol. 121 (1995) 582-586
    • (1995) J. Cancer Res. Clin. Oncol. , vol.121 , pp. 582-586
    • Naito, M.1    Tsuruo, T.2
  • 21
    • 0022309511 scopus 로고
    • Morphology of proteoliposomes containing fluorescein-phosphatidylethanolamine reconstituted with native and subunit III-depleted cytochrome c oxidase
    • Muller M., and Azzi A. Morphology of proteoliposomes containing fluorescein-phosphatidylethanolamine reconstituted with native and subunit III-depleted cytochrome c oxidase. J. Bioenerg. Biomembr. 17 (1985) 385-393
    • (1985) J. Bioenerg. Biomembr. , vol.17 , pp. 385-393
    • Muller, M.1    Azzi, A.2
  • 22
    • 0021147659 scopus 로고
    • Preparation of monodisperse vesicles with variable size by dilution of mixed micellar solutions of bile salt and phosphatidylcholine
    • Schurtenberger P., Mazer N., Waldvogel S., and Kanzig W. Preparation of monodisperse vesicles with variable size by dilution of mixed micellar solutions of bile salt and phosphatidylcholine. Biochim. Biophys. Acta 775 (1984) 111-114
    • (1984) Biochim. Biophys. Acta , vol.775 , pp. 111-114
    • Schurtenberger, P.1    Mazer, N.2    Waldvogel, S.3    Kanzig, W.4
  • 23
    • 0023656052 scopus 로고
    • Dynamics of proteoliposome formation: intermediate states during detergent dialysis
    • Wrigglesworth J.M., Wooster M.S., Elsden J., and Danneel H.J. Dynamics of proteoliposome formation: intermediate states during detergent dialysis. Biochem. J. 246 (1987) 737-744
    • (1987) Biochem. J. , vol.246 , pp. 737-744
    • Wrigglesworth, J.M.1    Wooster, M.S.2    Elsden, J.3    Danneel, H.J.4
  • 24
    • 0018185852 scopus 로고
    • Proton-translocating cytochrome c oxidase in artificial phospholipid vesicles
    • Krab K., and Wikstrom M. Proton-translocating cytochrome c oxidase in artificial phospholipid vesicles. Biochim. Biophys. Acta 504 (1978) 200-214
    • (1978) Biochim. Biophys. Acta , vol.504 , pp. 200-214
    • Krab, K.1    Wikstrom, M.2
  • 25
    • 0026077354 scopus 로고
    • Phopholipid vesicles containing bovine heart mitochondrial cytochrome c oxidase exhibit proton translocating activity in the presence of gramicidin
    • Prochaska L.J., and Wilson K.S. Phopholipid vesicles containing bovine heart mitochondrial cytochrome c oxidase exhibit proton translocating activity in the presence of gramicidin. Arch. Biochem. Biophys. 290 (1991) 179-185
    • (1991) Arch. Biochem. Biophys. , vol.290 , pp. 179-185
    • Prochaska, L.J.1    Wilson, K.S.2
  • 26
    • 16344379576 scopus 로고    scopus 로고
    • Cytochrome c adsorption to supported, anionic lipid bilayers studied via atomic force microscopy
    • Choi E.J., and Dimitriais E.K. Cytochrome c adsorption to supported, anionic lipid bilayers studied via atomic force microscopy. Biophys. J. 87 (2004) 3234-3241
    • (2004) Biophys. J. , vol.87 , pp. 3234-3241
    • Choi, E.J.1    Dimitriais, E.K.2
  • 27
    • 33744942614 scopus 로고    scopus 로고
    • Cytochrome c interaction with cardiolipin/phosphatidylcholine model membranes: effect of cardiolipid protonation
    • Gorbenko G.P., Molotkovsy J.G., and Kinnunen P.K.J. Cytochrome c interaction with cardiolipin/phosphatidylcholine model membranes: effect of cardiolipid protonation. Biophys. J. 90 (2006) 4093-4103
    • (2006) Biophys. J. , vol.90 , pp. 4093-4103
    • Gorbenko, G.P.1    Molotkovsy, J.G.2    Kinnunen, P.K.J.3
  • 31
    • 0017076962 scopus 로고
    • Hereditary retinal dystrophy in the rat: lipid composition of debris
    • Organisciak D., and Noell W. Hereditary retinal dystrophy in the rat: lipid composition of debris. Exp. Eye Res. 22 (1976) 101-113
    • (1976) Exp. Eye Res. , vol.22 , pp. 101-113
    • Organisciak, D.1    Noell, W.2
  • 32
    • 0000972361 scopus 로고
    • Geometric packing constraints in egg phosphatidylcholine vesicles
    • Huang C., and Mason J.T. Geometric packing constraints in egg phosphatidylcholine vesicles. Proc. Natl. Acad. Sci. USA 75 (1978) 308-310
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 308-310
    • Huang, C.1    Mason, J.T.2
  • 34
    • 0021771665 scopus 로고
    • Influence of vesicle size and oxidase content on respiratory control in reconstituted cytochrome oxidase vesicles
    • Madden T.D., Hope M.J., and Cullis P.R. Influence of vesicle size and oxidase content on respiratory control in reconstituted cytochrome oxidase vesicles. Biochemistry 23 (1984) 1413-1418
    • (1984) Biochemistry , vol.23 , pp. 1413-1418
    • Madden, T.D.1    Hope, M.J.2    Cullis, P.R.3
  • 35
    • 0033829802 scopus 로고    scopus 로고
    • Photoinduced intracomplex electron transfer between cytochrome c oxidase and TUPS-modified cytochrome c
    • Kotlyar A., Borovok N., Hazani M., Szundi I., and Einarsdóttir O. Photoinduced intracomplex electron transfer between cytochrome c oxidase and TUPS-modified cytochrome c. Eur. J. Biochem. 267 (2000) 5805-5809
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5805-5809
    • Kotlyar, A.1    Borovok, N.2    Hazani, M.3    Szundi, I.4    Einarsdóttir, O.5
  • 37
    • 18244378019 scopus 로고    scopus 로고
    • Stability of bovine cytochrome c oxidase as studied after exposure to high hydrostatic pressure
    • Stanicova J., Musatov A., and Robinson N.C. Stability of bovine cytochrome c oxidase as studied after exposure to high hydrostatic pressure. Acta Medica (Hradac Kralove) 47 (2004) 335-338
    • (2004) Acta Medica (Hradac Kralove) , vol.47 , pp. 335-338
    • Stanicova, J.1    Musatov, A.2    Robinson, N.C.3
  • 38
    • 34250865041 scopus 로고    scopus 로고
    • Differential stability of dimeric and monomeric cytochrome c oxidase exposed to elevated hydrostatic pressure
    • Stanicova J., Sedlak E., Musatov A., and Robinson N.C. Differential stability of dimeric and monomeric cytochrome c oxidase exposed to elevated hydrostatic pressure. Biochemistry 46 (2007) 7146-7152
    • (2007) Biochemistry , vol.46 , pp. 7146-7152
    • Stanicova, J.1    Sedlak, E.2    Musatov, A.3    Robinson, N.C.4
  • 39
    • 15444369621 scopus 로고    scopus 로고
    • Slow proton transfer through the pathways for pumped protons in cytochrome c oxidase induces suicide inactivation of the enzyme
    • Mills D.A., and Hosler J.P. Slow proton transfer through the pathways for pumped protons in cytochrome c oxidase induces suicide inactivation of the enzyme. Biochemistry 44 (2005) 4656-4666
    • (2005) Biochemistry , vol.44 , pp. 4656-4666
    • Mills, D.A.1    Hosler, J.P.2
  • 40
    • 0038408885 scopus 로고    scopus 로고
    • Subunit III of cytochrome c oxidase of Rhodobacter sphaeroides is required to maintain rapid proton uptake through the D pathway at physiologic pH
    • Gilderson G., Salomonsson L., Aagaard A., Gray J., Brzezinski P., and Hosler J. Subunit III of cytochrome c oxidase of Rhodobacter sphaeroides is required to maintain rapid proton uptake through the D pathway at physiologic pH. Biochemistry 42 (2003) 7400-7409
    • (2003) Biochemistry , vol.42 , pp. 7400-7409
    • Gilderson, G.1    Salomonsson, L.2    Aagaard, A.3    Gray, J.4    Brzezinski, P.5    Hosler, J.6
  • 41
    • 0033534165 scopus 로고    scopus 로고
    • Suicide inactivation of cytochrome c oxidase: catalytic turnover in the absence of subunit III alters the active site
    • Bratton M.R., Pressler M.A., and Hosler J.P. Suicide inactivation of cytochrome c oxidase: catalytic turnover in the absence of subunit III alters the active site. Biochemistry 38 (1999) 16236-16245
    • (1999) Biochemistry , vol.38 , pp. 16236-16245
    • Bratton, M.R.1    Pressler, M.A.2    Hosler, J.P.3
  • 42
    • 27144542653 scopus 로고    scopus 로고
    • Pressure-induced shape change of phospholipid vesicles: implication of compression and phase transition
    • Perrier-Cornet J.M., Baddouj K., and Gervais P. Pressure-induced shape change of phospholipid vesicles: implication of compression and phase transition. J. Membr. Biol. 204 (2005) 101-107
    • (2005) J. Membr. Biol. , vol.204 , pp. 101-107
    • Perrier-Cornet, J.M.1    Baddouj, K.2    Gervais, P.3
  • 43
    • 0031056520 scopus 로고    scopus 로고
    • Shape modification of phospholipid vesicles induced by high pressure: influence of bilayer compressibility
    • Beney L., Perrier-Cornet J.M., Hayert M., and Gervais P. Shape modification of phospholipid vesicles induced by high pressure: influence of bilayer compressibility. Biophys. J. 72 (1997) 1258-1263
    • (1997) Biophys. J. , vol.72 , pp. 1258-1263
    • Beney, L.1    Perrier-Cornet, J.M.2    Hayert, M.3    Gervais, P.4
  • 44
    • 0022428013 scopus 로고
    • Preparation of reconstituted cytochrome oxidase vesicles with defined trans-membrane protein orientations employing a cytochrome c affinity column
    • Madden T.D., and Cullis P.R. Preparation of reconstituted cytochrome oxidase vesicles with defined trans-membrane protein orientations employing a cytochrome c affinity column. Biochim. Biophys. Acta 808 (1985) 219-224
    • (1985) Biochim. Biophys. Acta , vol.808 , pp. 219-224
    • Madden, T.D.1    Cullis, P.R.2


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