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Volumn 46, Issue 24, 2007, Pages 7146-7152

Differential stability of dimeric and monomeric cytochrome c oxidase exposed to elevated hydrostatic pressure

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL STABILITY; CONFORMATIONS; ELECTROPHORESIS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROSTATIC PRESSURE; MONOMERS;

EID: 34250865041     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700548a     Document Type: Article
Times cited : (17)

References (27)
  • 2
    • 0020724790 scopus 로고
    • Separation of mammalian cytochrome c oxidase into 13 polypeptides by sodium dodecyl sulfate-gel electrophoresis procedure
    • Kadenbach, B., Jarausch, J., Hartmann, R., and Merle, P. (1983) Separation of mammalian cytochrome c oxidase into 13 polypeptides by sodium dodecyl sulfate-gel electrophoresis procedure, Anal. Biochem. 129, 517-521.
    • (1983) Anal. Biochem , vol.129 , pp. 517-521
    • Kadenbach, B.1    Jarausch, J.2    Hartmann, R.3    Merle, P.4
  • 3
    • 0027252494 scopus 로고
    • Functional binding of cardiolipin to cytochrome c oxidase
    • Robinson, N. C. (1993) Functional binding of cardiolipin to cytochrome c oxidase, J. Bioenerg. Biomembr. 25, 153-163.
    • (1993) J. Bioenerg. Biomembr , vol.25 , pp. 153-163
    • Robinson, N.C.1
  • 4
    • 0021714441 scopus 로고
    • The functional and physical form of mammalian cytochrome c oxidase determined by gel filtration, radiation inactivation, and sedimentation equilibrium analysis
    • Suarez, M. D., Revzin, A., Narlock, R., Kempner, E. S., Thompson, D. A., and Ferguson-Miller, S. (1984) The functional and physical form of mammalian cytochrome c oxidase determined by gel filtration, radiation inactivation, and sedimentation equilibrium analysis, J. Biol. Chem. 259, 13791-13799.
    • (1984) J. Biol. Chem , vol.259 , pp. 13791-13799
    • Suarez, M.D.1    Revzin, A.2    Narlock, R.3    Kempner, E.S.4    Thompson, D.A.5    Ferguson-Miller, S.6
  • 5
    • 0022495489 scopus 로고
    • Triton X-100 induced dissociation of beef heart cytochrome c oxidase into monomers
    • Robinson, N. C., and Talbert, L. (1986) Triton X-100 induced dissociation of beef heart cytochrome c oxidase into monomers, Biochemistry 25, 2328-2335.
    • (1986) Biochemistry , vol.25 , pp. 2328-2335
    • Robinson, N.C.1    Talbert, L.2
  • 6
    • 0037007002 scopus 로고    scopus 로고
    • Cholate-induced dimerization of detergent- or phospholipid-solubilized bovine cytochrome c oxidase
    • Musatov, A., and Robinson, N. C. (2002) Cholate-induced dimerization of detergent- or phospholipid-solubilized bovine cytochrome c oxidase, Biochemistry 41, 4371-4376.
    • (2002) Biochemistry , vol.41 , pp. 4371-4376
    • Musatov, A.1    Robinson, N.C.2
  • 7
    • 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. (1993) Detection of bovine heart mitochondrial cytochrome c oxidase dimers in Triton X-100 and phospholipid vesicles by chemical cross-linking, Biochemistry 32, 13270-13276.
    • (1993) Biochemistry , vol.32 , pp. 13270-13276
    • Estey, L.A.1    Prochaska, L.J.2
  • 8
    • 0035823541 scopus 로고    scopus 로고
    • Exposure of bovine cytochrome c oxidase to high Triton X-100 or to alkaline conditions causes a dramatic changes in the rate of reduction of compound F
    • Sadoski, R. C., Zaslavsky, D., Gennis, R. B., Durham, B., and Millet, F. (2001) Exposure of bovine cytochrome c oxidase to high Triton X-100 or to alkaline conditions causes a dramatic changes in the rate of reduction of compound F, J. Biol. Chem. 276, 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    Millet, F.5
  • 9
    • 0020491930 scopus 로고
    • Conformations of cytochrome c oxidase: Thermodynamic evaluation of the interconversion of the 418- and 428-nm forms
    • Kornblatt, J. A., and Hui Bon Hoa, G. (1982) Conformations of cytochrome c oxidase: Thermodynamic evaluation of the interconversion of the 418- and 428-nm forms, Biochemistry 21, 5439-5444
    • (1982) Biochemistry , vol.21 , pp. 5439-5444
    • Kornblatt, J.A.1    Hui Bon Hoa, G.2
  • 10
    • 0021755235 scopus 로고
    • Volume changes associated with cytochrome c oxidase-porphyrin cytochrome c equilibrium
    • Kornblatt, J. A., Hui Bon Hoa, G., and English, A. M. (1984) Volume changes associated with cytochrome c oxidase-porphyrin cytochrome c equilibrium, Biochemistry 23, 5906-5911
    • (1984) Biochemistry , vol.23 , pp. 5906-5911
    • Kornblatt, J.A.1    Hui Bon Hoa, G.2    English, A.M.3
  • 11
    • 0024284991 scopus 로고
    • Pressure-induced effects on cytochrome c oxidase: The aerobic steady state
    • Kornblatt, J. A., Hui Bon Hoa, G., and Heremans K. (1988) Pressure-induced effects on cytochrome c oxidase: The aerobic steady state, Biochemistry 27, 5122-5128.
    • (1988) Biochemistry , vol.27 , pp. 5122-5128
    • Kornblatt, J.A.1    Hui Bon Hoa, G.2    Heremans, K.3
  • 12
    • 0025185780 scopus 로고
    • A nontraditional role for water in the cytochrome c oxidase reaction
    • Kornblatt, J. A., and Hui Bon Hoa, G. (1990) A nontraditional role for water in the cytochrome c oxidase reaction, Biochemistry 29, 9370-9376.
    • (1990) Biochemistry , vol.29 , pp. 9370-9376
    • Kornblatt, J.A.1    Hui Bon Hoa, G.2
  • 13
    • 0025061009 scopus 로고
    • Effect of changing the detergent bound to bovine cytochrome c oxidase upon its individual electron-transfer steps
    • Mahapatro, S. N., and Robinson, N. C. (1990) Effect of changing the detergent bound to bovine cytochrome c oxidase upon its individual electron-transfer steps, Biochemistry 29, 764-770.
    • (1990) Biochemistry , vol.29 , pp. 764-770
    • Mahapatro, S.N.1    Robinson, N.C.2
  • 14
    • 0034711042 scopus 로고    scopus 로고
    • Detergent-solubilized bovine cytochrome c oxidase: Dimerization depends upon the amphiphilic environment
    • Musatov, A., Ortega-Lopez, J., and Robinson, N. C. (2000) Detergent-solubilized bovine cytochrome c oxidase: Dimerization depends upon the amphiphilic environment, Biochemistry 39, 12996-13004.
    • (2000) Biochemistry , vol.39 , pp. 12996-13004
    • Musatov, A.1    Ortega-Lopez, J.2    Robinson, N.C.3
  • 15
    • 0035794197 scopus 로고    scopus 로고
    • High hydrostatic pressure can probe the effects of functionally related ligands on the quaternary structures of the chaperonins GroEL and GroES
    • Panda, M., Ybarra, J., and Horowitz, P. M. (2001) High hydrostatic pressure can probe the effects of functionally related ligands on the quaternary structures of the chaperonins GroEL and GroES, J. Biol. Chem. 276, 6253-6259.
    • (2001) J. Biol. Chem , vol.276 , pp. 6253-6259
    • Panda, M.1    Ybarra, J.2    Horowitz, P.M.3
  • 16
    • 0037065675 scopus 로고    scopus 로고
    • Conformational heterogeneity is revealed in the dissociation of the oligomeric chaperonin GroEL by high hydrostatic pressure
    • Panda, M., and Horowitz, P. M. (2002) Conformational heterogeneity is revealed in the dissociation of the oligomeric chaperonin GroEL by high hydrostatic pressure, Biochemistry 41, 1869-1876.
    • (2002) Biochemistry , vol.41 , pp. 1869-1876
    • Panda, M.1    Horowitz, P.M.2
  • 17
    • 0023807789 scopus 로고
    • Synthesis of cardiolipin derivatives with protection of the free hydroxyl: Its application to the study of cardiolipin stimulation of cytochrome c oxidase
    • Dale, M. P., and Robinson, N. C. (1988) Synthesis of cardiolipin derivatives with protection of the free hydroxyl: Its application to the study of cardiolipin stimulation of cytochrome c oxidase, Biochemistry 27, 8270-8275.
    • (1988) Biochemistry , vol.27 , pp. 8270-8275
    • Dale, M.P.1    Robinson, N.C.2
  • 18
    • 0033539647 scopus 로고    scopus 로고
    • 2 digestion of cardiolipin bound to bovine cytochrome c oxidase alters both activity and quaternary structure
    • 2 digestion of cardiolipin bound to bovine cytochrome c oxidase alters both activity and quaternary structure, Biochemistry 38, 14966-14972.
    • (1999) Biochemistry , vol.38 , pp. 14966-14972
    • Sedlák, E.1    Robinson, N.C.2
  • 19
    • 0019317502 scopus 로고
    • Investigation of the essential boundary layers phospholipids of cytochrome c oxidase using Triton X-100
    • Robinson, N. C., Strey, F., and Talbert, L. (1980) Investigation of the essential boundary layers phospholipids of cytochrome c oxidase using Triton X-100, Biochemistry 19, 3656-3661.
    • (1980) Biochemistry , vol.19 , pp. 3656-3661
    • Robinson, N.C.1    Strey, F.2    Talbert, L.3
  • 20
    • 0017806223 scopus 로고
    • Boundary analysis of sedimentation-velocity experiments with monodisperse and polydisperse solutes
    • Van Holde, K. E., and Weischet, W. O. (1978) Boundary analysis of sedimentation-velocity experiments with monodisperse and polydisperse solutes, Biopolymers 17, 1387-1403.
    • (1978) Biopolymers , vol.17 , pp. 1387-1403
    • Van Holde, K.E.1    Weischet, W.O.2
  • 21
    • 0034009520 scopus 로고    scopus 로고
    • Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. (2000) Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling, Biophys. J. 78, 1606-1619.
    • (2000) Biophys. J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 22
    • 0031673633 scopus 로고    scopus 로고
    • Analysis of Detergent-Solubilized Membrane Proteins in the Analytical Ultracentrifuge
    • Robinson, N. C., Gomez, B., and Musatov, A. (1998) Analysis of Detergent-Solubilized Membrane Proteins in the Analytical Ultracentrifuge, Chemtracts: Biochem. Mol. Biol. 11, 980-968.
    • (1998) Chemtracts: Biochem. Mol. Biol , vol.11 , pp. 980-968
    • Robinson, N.C.1    Gomez, B.2    Musatov, A.3
  • 23
    • 31044445705 scopus 로고    scopus 로고
    • Photolabeling of cardiolipin binding subunits within bovine heart cytochrome c oxidase
    • Sedlák, E., Panda, M., Dale, M. P., Weintraub, S. T., and Robinson, N. C. (2006) Photolabeling of cardiolipin binding subunits within bovine heart cytochrome c oxidase, Biochemistry 45, 746-754.
    • (2006) Biochemistry , vol.45 , pp. 746-754
    • Sedlák, E.1    Panda, M.2    Dale, M.P.3    Weintraub, S.T.4    Robinson, N.C.5
  • 24
    • 0025879301 scopus 로고
    • Subunit III of cytochrome c oxidase is not involved in proton translocation: A site-directed mutagenesis study
    • Haltia, T., Saraste, M., and Wikström, M. (1991) Subunit III of cytochrome c oxidase is not involved in proton translocation: A site-directed mutagenesis study, EMBO J. 10, 2015-2021.
    • (1991) EMBO J , vol.10 , pp. 2015-2021
    • Haltia, T.1    Saraste, M.2    Wikström, M.3
  • 25
    • 0942290629 scopus 로고    scopus 로고
    • Specific modification of two tryptophans within the nuclear-encoded subunits of bovine cytochrome c oxidase by hydrogen peroxide
    • Musatov, A., Hebert, E., Carroll, C. A., Weintraub, S. T., and Robinson, N. C. (2004) Specific modification of two tryptophans within the nuclear-encoded subunits of bovine cytochrome c oxidase by hydrogen peroxide, Biochemistry 43, 1003-1009.
    • (2004) Biochemistry , vol.43 , pp. 1003-1009
    • Musatov, A.1    Hebert, E.2    Carroll, C.A.3    Weintraub, S.T.4    Robinson, N.C.5
  • 26
    • 31044445705 scopus 로고    scopus 로고
    • Photolabeling of cardiolipin binding subunits within bovine heart cytochrome c oxidase
    • Sedlák, E., Panda, M., Dale, M. P., Weintraub, S. T., and Robinson, N. C. (2006) Photolabeling of cardiolipin binding subunits within bovine heart cytochrome c oxidase, Biochemistry 45, 746-754.
    • (2006) Biochemistry , vol.45 , pp. 746-754
    • Sedlák, E.1    Panda, M.2    Dale, M.P.3    Weintraub, S.T.4    Robinson, N.C.5
  • 27
    • 0028879242 scopus 로고
    • Separation and quantitation of cytochrome c oxidase subunits by mono Q fast liquid chromatography and C18 reverse phase HPLC
    • Liu, Y.-C., Sowdal, L., and Robinson, N. C. (1995) Separation and quantitation of cytochrome c oxidase subunits by mono Q fast liquid chromatography and C18 reverse phase HPLC, Arch. Biochem. Biophys. 324, 135-142.
    • (1995) Arch. Biochem. Biophys , vol.324 , pp. 135-142
    • Liu, Y.-C.1    Sowdal, L.2    Robinson, N.C.3


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