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Volumn 48, Issue 34, 2009, Pages 8143-8150

Sequential dissociation of subunits from bovine heart cytochrome c oxidase by urea

Author keywords

[No Author keywords available]

Indexed keywords

BOVINE HEART CYTOCHROME; CHEMICAL DENATURANTS; CONCENTRATION OF; CONCENTRATION RANGES; CONCENTRATION-DEPENDENT; CONFORMATIONAL CHANGE; CYTOCHROME C OXIDASE; DIMER INTERFACE; DISSOCIATION CURVES; DISSOCIATION DATA; FREE ENERGY CHANGE; GUANIDINIUM CHLORIDES; INDUCED DISSOCIATION; MEMBRANE PROTEINS; ROOM TEMPERATURE; SECONDARY STRUCTURES; SEQUENTIAL DISSOCIATION; SOLVENT-ACCESSIBLE SURFACE AREA; SUBUNIT DISSOCIATION; THERMODYNAMIC PARAMETER;

EID: 69249137929     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900773r     Document Type: Article
Times cited : (9)

References (44)
  • 1
    • 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
  • 4
    • 0035846967 scopus 로고    scopus 로고
    • Structure of cytochrome c oxidase: A comparison of the bacterial and mitochondrial enzymes
    • Abramson, J., Svensson-Ek, M., Byrne, B., and Iwata, S. (2001) Structure of cytochrome c oxidase: a comparison of the bacterial and mitochondrial enzymes. Biochim. Biophys. Acta 1544, 1-9.
    • (2001) Biochim. Biophys. Acta , vol.1544 , pp. 1-9
    • Abramson, J.1    Svensson-Ek, M.2    Byrne, B.3    Iwata, S.4
  • 5
    • 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., Törnroth, S., Brzezinski, P., and Iwata, S. (2002) The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides. J. Mol. Biol. 321, 329-339.
    • (2002) J. Mol. Biol , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Törnroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 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
    • 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
  • 8
    • 0343714594 scopus 로고    scopus 로고
    • Mitochondrial energy metabolism is regulated via nuclear-coded subunits of cytochrome c oxidase
    • Kadenbach, B., Huttemann, M., Arnold, S., Lee, I., and Bender, E. (2000) Mitochondrial energy metabolism is regulated via nuclear-coded subunits of cytochrome c oxidase. Free Radical Biol. Med. 29, 211-221.
    • (2000) Free Radical Biol. Med , vol.29 , pp. 211-221
    • Kadenbach, B.1    Huttemann, M.2    Arnold, S.3    Lee, I.4    Bender, E.5
  • 9
    • 0022292281 scopus 로고
    • Effect of trypsin on the kinetic properties of reconstituted beef heart cytochrome c oxidase
    • Buge, V., and Kadenbach, B. (1985) Effect of trypsin on the kinetic properties of reconstituted beef heart cytochrome c oxidase. J. Bioenerg. Biomembr. 17, 375-384.
    • (1985) J. Bioenerg. Biomembr , vol.17 , pp. 375-384
    • Buge, V.1    Kadenbach, B.2
  • 11
    • 0028153306 scopus 로고
    • Role of nuclear-encoded subunits of mitochondrial cytochrome c oxidase in proton pumping revealed by limited enzymatic proteolysis
    • Capitanio, N., Peccarisi, R., Capitanio, G., Villani, G., De Nitto, E., Scacco, S., and Papa, S. (1994) Role of nuclear-encoded subunits of mitochondrial cytochrome c oxidase in proton pumping revealed by limited enzymatic proteolysis. Biochemistry 33, 12521-12526.
    • (1994) Biochemistry , vol.33 , pp. 12521-12526
    • Capitanio, N.1    Peccarisi, R.2    Capitanio, G.3    Villani, G.4    De Nitto, E.5    Scacco, S.6    Papa, S.7
  • 12
    • 0038352169 scopus 로고    scopus 로고
    • Site-specific antibodies against hydrophilic domains of subunit III of bovine heart cytochrome c oxidase affect enzyme function
    • Lincoln, J. A., Donat, N., Palmer, G., and Prochaska, L. J. (2003) Site-specific antibodies against hydrophilic domains of subunit III of bovine heart cytochrome c oxidase affect enzyme function. Arch. Biochem. Biophys. 416, 81-91.
    • (2003) Arch. Biochem. Biophys , vol.416 , pp. 81-91
    • Lincoln, J.A.1    Donat, N.2    Palmer, G.3    Prochaska, L.J.4
  • 13
    • 0016742391 scopus 로고
    • Subunit dissociation and unfolding of rabbit muscle phosphofructokinase by guanidine by hydrochloride
    • Parr, G. R., and Hammes, G. G. (1975) Subunit dissociation and unfolding of rabbit muscle phosphofructokinase by guanidine by hydrochloride. Biochemistry 14, 1600-1605.
    • (1975) Biochemistry , vol.14 , pp. 1600-1605
    • Parr, G.R.1    Hammes, G.G.2
  • 14
    • 0019642282 scopus 로고
    • Evidence for an intermediate in the denaturation and assembly of phosphoglucose isomerase
    • Blackburn, M. N., and Noltmann, E. A. (1981) Evidence for an intermediate in the denaturation and assembly of phosphoglucose isomerase. Arch. Biochem. Biophys. 212, 161-169.
    • (1981) Arch. Biochem. Biophys , vol.212 , pp. 161-169
    • Blackburn, M.N.1    Noltmann, E.A.2
  • 15
    • 0019545628 scopus 로고
    • Dimeric intermediates in the dissociation of lactic dehydrogenase
    • Jaenicke, R., Vogel, W., and Rudolph, R. (1981) Dimeric intermediates in the dissociation of lactic dehydrogenase. Eur. J. Biochem. 114, 525-531.
    • (1981) Eur. J. Biochem , vol.114 , pp. 525-531
    • Jaenicke, R.1    Vogel, W.2    Rudolph, R.3
  • 16
    • 0029098803 scopus 로고
    • Subunit dissociation and unfolding of macrophage NO synthase: Relationship between enzyme structure, prosthetic group binding, and catalytic function
    • Abu-Soud, H. M., Loftus, M., and Stuehr, D. J. (1995) Subunit dissociation and unfolding of macrophage NO synthase: relationship between enzyme structure, prosthetic group binding, and catalytic function. Biochemistry 34, 11167-11175.
    • (1995) Biochemistry , vol.34 , pp. 11167-11175
    • Abu-Soud, H.M.1    Loftus, M.2    Stuehr, D.J.3
  • 17
    • 0023711148 scopus 로고
    • Subunit dissociation and protein unfolding in the bovine heart cytochrome oxidase complex induced by guanidine hydrochloride
    • Hill, B. C., Cook, K., and Robinson, N. C. (1988) Subunit dissociation and protein unfolding in the bovine heart cytochrome oxidase complex induced by guanidine hydrochloride. Biochemistry 27, 4741-4747.
    • (1988) Biochemistry , vol.27 , pp. 4741-4747
    • Hill, B.C.1    Cook, K.2    Robinson, N.C.3
  • 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
    • 0017821108 scopus 로고
    • Conformational states of a hydrophobic protein. The coat protein of fd bacteriophage
    • Nozaki, Y., Reynolds, J. A., and Tanford, C. (1978) Conformational states of a hydrophobic protein. The coat protein of fd bacteriophage. Biochemistry 17, 1239-1246.
    • (1978) Biochemistry , vol.17 , pp. 1239-1246
    • Nozaki, Y.1    Reynolds, J.A.2    Tanford, C.3
  • 20
    • 0028815284 scopus 로고
    • Forces and factors that contribute to the structural stability of membrane proteins
    • Haltia, T., and Freire, E. (1995) Forces and factors that contribute to the structural stability of membrane proteins. Biochim. Biophys. Acta 1228, 1-27.
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 1-27
    • Haltia, T.1    Freire, E.2
  • 22
    • 33747793145 scopus 로고    scopus 로고
    • Energetics of membrane protein folding and stability
    • Minetti, C. A., and Remeta, D. P. (2006) Energetics of membrane protein folding and stability. Arch. Biochem. Biophys. 453, 32-53.
    • (2006) Arch. Biochem. Biophys , vol.453 , pp. 32-53
    • Minetti, C.A.1    Remeta, D.P.2
  • 23
    • 0001693643 scopus 로고
    • A rapid method for the preparation of highly purified cytochrome oxidase
    • Fowler, L. R., Richardson, S. H., and Hatefi, Y. (1962) A rapid method for the preparation of highly purified cytochrome oxidase. Biochim. Biophys. Acta 64, 170-173.
    • (1962) Biochim. Biophys. Acta , vol.64 , pp. 170-173
    • Fowler, L.R.1    Richardson, S.H.2    Hatefi, Y.3
  • 24
    • 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
  • 25
    • 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
  • 26
    • 0031673633 scopus 로고    scopus 로고
    • Analysis of detergent solubilized membrane proteins in the analytical ultracentrifuge
    • Robinson, N. C., Gomez, B., Musatov, A., and Ortega-Lopez, J. (1998) Analysis of detergent solubilized membrane proteins in the analytical ultracentrifuge. ChemTracts: Biochem. Mol. Biol. 11, 960-968.
    • (1998) ChemTracts: Biochem. Mol. Biol , vol.11 , pp. 960-968
    • Robinson, N.C.1    Gomez, B.2    Musatov, A.3    Ortega-Lopez, J.4
  • 27
    • 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
  • 28
    • 0018065968 scopus 로고
    • Optical properties of cytochromes from beef heart mitochondria, submitochondrial vesicles, and derived preparations
    • van Gelder, B. F. (1978) Optical properties of cytochromes from beef heart mitochondria, submitochondrial vesicles, and derived preparations. Methods Enzymol. 53, 125-128.
    • (1978) Methods Enzymol , vol.53 , pp. 125-128
    • van Gelder, B.F.1
  • 29
    • 0028879242 scopus 로고
    • Separation and quantitation of cytochrome c oxidase subunits by mono Q fast liquid chromatography and C18 reverse phase HPLC
    • Liu, Y.-Ch., Sowdal, L. H., 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.H.2    Robinson, N.C.3
  • 30
    • 0019317502 scopus 로고
    • Investigation of the essential boundary layer phospholipids of cytochrome c oxidase using Triton X-100 delipidation
    • Robinson, N. C., Strey, F., and Talbert, L. (1980) Investigation of the essential boundary layer phospholipids of cytochrome c oxidase using Triton X-100 delipidation. Biochemistry 19, 3656-3661.
    • (1980) Biochemistry , vol.19 , pp. 3656-3661
    • Robinson, N.C.1    Strey, F.2    Talbert, L.3
  • 31
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131, 266-280.
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 32
    • 0027211743 scopus 로고
    • Long-distance cofactor interactions in terminal oxidases studied by second-derivative absorption spectroscopy
    • Copeland, R. A. (1993) Long-distance cofactor interactions in terminal oxidases studied by second-derivative absorption spectroscopy. J. Bioenerg. Biomembr. 25, 93-102.
    • (1993) J. Bioenerg. Biomembr , vol.25 , pp. 93-102
    • Copeland, R.A.1
  • 33
    • 0037133522 scopus 로고    scopus 로고
    • Guanidinium chloride- and urea-induced unfolding of the dimeric enzyme glucose oxidase
    • Akhtar, M. S., Ahmad, A., and Bhakuni, V. (2002) Guanidinium chloride- and urea-induced unfolding of the dimeric enzyme glucose oxidase. Biochemistry 41, 3819-3827.
    • (2002) Biochemistry , vol.41 , pp. 3819-3827
    • Akhtar, M.S.1    Ahmad, A.2    Bhakuni, V.3
  • 34
    • 34250865041 scopus 로고    scopus 로고
    • Differential stability of dimeric and monomeric cytochrome c oxidase exposed to elevated hydrostatic pressure
    • Stanicová, J., Sedlák, E., Musatov, A., and Robinson, N. C. (2007) Differential stability of dimeric and monomeric cytochrome c oxidase exposed to elevated hydrostatic pressure. Biochemistry 46, 7146-7152.
    • (2007) Biochemistry , vol.46 , pp. 7146-7152
    • Stanicová, J.1    Sedlák, E.2    Musatov, A.3    Robinson, N.C.4
  • 35
    • 0023642560 scopus 로고
    • Identification of different quaternary structures of beef heart cytochrome-c oxidase by two-dimensional polyacrylamide gel electrophoresis
    • Heinrichs, M., and Schönert, H. (1987) Identification of different quaternary structures of beef heart cytochrome-c oxidase by two-dimensional polyacrylamide gel electrophoresis. FEBS Lett. 223, 255-261.
    • (1987) FEBS Lett , vol.223 , pp. 255-261
    • Heinrichs, M.1    Schönert, H.2
  • 37
    • 0034866945 scopus 로고    scopus 로고
    • Assembly of cytochrome c oxidase: What can we learn from patients with cytochrome c oxidase deficiency?
    • Taanman, J.-W., and Williams, S. L. (2001) Assembly of cytochrome c oxidase: what can we learn from patients with cytochrome c oxidase deficiency? Biochem. Soc. Trans. 29, 446-451.
    • (2001) Biochem. Soc. Trans , vol.29 , pp. 446-451
    • Taanman, J.-W.1    Williams, S.L.2
  • 38
    • 0345426282 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of dimer formation and dissociation for a recombinant humanized monoclonal antibody to vascular endothelial growth factor
    • Moore, J. M. R., Patapoff, T. W., and Cromwell, M. E. M. (1999) Kinetics and thermodynamics of dimer formation and dissociation for a recombinant humanized monoclonal antibody to vascular endothelial growth factor. Biochemistry 38, 13960-13967.
    • (1999) Biochemistry , vol.38 , pp. 13960-13967
    • Moore, J.M.R.1    Patapoff, T.W.2    Cromwell, M.E.M.3
  • 39
    • 0035942355 scopus 로고    scopus 로고
    • Equilibrium unfolding of dimeric desulfoferrodoxin involves a monomeric intermediate: Iron cofactors dissociate after polypeptide unfolding
    • Apiyo, D., Jones, K., Guidry, J., and Wittung-Stafshede, P. (2001) Equilibrium unfolding of dimeric desulfoferrodoxin involves a monomeric intermediate: iron cofactors dissociate after polypeptide unfolding. Biochemistry 40, 4940-4948.
    • (2001) Biochemistry , vol.40 , pp. 4940-4948
    • Apiyo, D.1    Jones, K.2    Guidry, J.3    Wittung-Stafshede, P.4
  • 40
    • 0344519692 scopus 로고    scopus 로고
    • Equilibrium unfolding of dimeric human prostatic acid phosphatase involves an inactive monomeric intermediate
    • Wójciak, P., Mazurkiewicz, A., Bakalova, A., and Kuciel, R. (2003) Equilibrium unfolding of dimeric human prostatic acid phosphatase involves an inactive monomeric intermediate. Int. J. Biol. Macromol. 32, 43-54.
    • (2003) Int. J. Biol. Macromol , vol.32 , pp. 43-54
    • Wójciak, P.1    Mazurkiewicz, A.2    Bakalova, A.3    Kuciel, R.4
  • 41
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin, J., Miller, S., and Chothia, C. (1988) Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol. 204, 155-164.
    • (1988) J. Mol. Biol , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 42
  • 43
    • 0025109557 scopus 로고
    • Yeast cytochrome c oxidase subunit VII is essential for assembly of an active enzyme. Cloning, sequencing, and characterization of the nuclear-encoded gene
    • Aggeler, R., and Capaldi, R. A. (1990) Yeast cytochrome c oxidase subunit VII is essential for assembly of an active enzyme. Cloning, sequencing, and characterization of the nuclear-encoded gene. J. Biol. Chem. 265, 16389-16393.
    • (1990) J. Biol. Chem. 265 , pp. 16389-16393
    • Aggeler, R.1    Capaldi, R.A.2
  • 44
    • 0029894544 scopus 로고    scopus 로고
    • Crosstalk between nuclear and mitochondrial genomes
    • Poyton, R. O., and McEwen, J. E. (1996) Crosstalk between nuclear and mitochondrial genomes. Annu. Rev. Biochem. 65, 563-607.
    • (1996) Annu. Rev. Biochem , vol.65 , pp. 563-607
    • Poyton, R.O.1    McEwen, J.E.2


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