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Volumn 110, Issue 3, 2004, Pages 203-211

pH-dependent conformational changes of ferricytochrome c induced by electrode surface microstructure

Author keywords

Alkaline conformational changes of ferricytochrome c; CD spectra; Electrode surface microstructure; SWNTs modified electrode

Indexed keywords

CARBON NANOTUBE; CYTOCHROME C; GLASS; NANOTUBE;

EID: 3042604801     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2004.02.004     Document Type: Article
Times cited : (11)

References (37)
  • 3
    • 0019888623 scopus 로고
    • Conformation change of cytochrome c: I. Ferrocytochrome c structure refined at 1.5 Å resolution
    • Takano T., Dickerson R.E. Conformation change of cytochrome c: I. Ferrocytochrome c structure refined at 1.5 Å resolution. J. Mol. Biol. 153:1981;79-94
    • (1981) J. Mol. Biol. , vol.153 , pp. 79-94
    • Takano, T.1    Dickerson, R.E.2
  • 4
    • 0025146477 scopus 로고
    • High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochrome c
    • Louie G.V., Brayer G.D. High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochrome c. J. Mol. Biol. 214:1990;527-555
    • (1990) J. Mol. Biol. , vol.214 , pp. 527-555
    • Louie, G.V.1    Brayer, G.D.2
  • 5
    • 0025007598 scopus 로고
    • High resolution three-dimensional structure of horse heart cytochrome c
    • Bushnell G.W., Louie G.V., Brayer G.D. High resolution three-dimensional structure of horse heart cytochrome c. J. Mol. Biol. 214:1990;585-595
    • (1990) J. Mol. Biol. , vol.214 , pp. 585-595
    • Bushnell, G.W.1    Louie, G.V.2    Brayer, G.D.3
  • 6
    • 0026608669 scopus 로고
    • Oxidation state-dependent conformational changes in cytochrome c
    • Berghuis A.M., Brayer G.D. Oxidation state-dependent conformational changes in cytochrome c. J. Mol. Biol. 223:1992;959-976
    • (1992) J. Mol. Biol. , vol.223 , pp. 959-976
    • Berghuis, A.M.1    Brayer, G.D.2
  • 7
    • 0025101781 scopus 로고
    • Conformational changes in cytochrome c and cytochrome oxidase upon complex formation: A resonance Raman study
    • Hildebrandt P., Heimburg T., Marsh D., Powell G.L. Conformational changes in cytochrome c and cytochrome oxidase upon complex formation: a resonance Raman study. Biochemistry. 29:1990;1661-1668
    • (1990) Biochemistry , vol.29 , pp. 1661-1668
    • Hildebrandt, P.1    Heimburg, T.2    Marsh, D.3    Powell, G.L.4
  • 8
    • 0023260274 scopus 로고
    • Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c
    • Gadsby P.M.A., Peterson J., Foote N., Greenwood C., Thomson A.J. Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c. Biochem. J. 246:1987;43-54
    • (1987) Biochem. J. , vol.246 , pp. 43-54
    • Gadsby, P.M.A.1    Peterson, J.2    Foote, N.3    Greenwood, C.4    Thomson, A.J.5
  • 9
    • 0024596945 scopus 로고
    • NMR study of the alkaline isomerization of ferricytochrome c
    • Hong X., Dixon D.W. NMR study of the alkaline isomerization of ferricytochrome c. FEBS. 246:1989;105-108
    • (1989) FEBS , vol.246 , pp. 105-108
    • Hong, X.1    Dixon, D.W.2
  • 10
    • 0001370438 scopus 로고
    • Identification of Lys79 as an iron ligand in one form of alkaline yeast iso-1-ferricytochrome c
    • Ferrer J.C., Guillemette J.G., Bogumil R., Inglis S.C., Smith M., Mauk A.G. Identification of Lys79 as an iron ligand in one form of alkaline yeast iso-1-ferricytochrome c. J. Am. Chem. Soc. 115:1993;7507-7508
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 7507-7508
    • Ferrer, J.C.1    Guillemette, J.G.2    Bogumil, R.3    Inglis, S.C.4    Smith, M.5    Mauk, A.G.6
  • 11
    • 0015209749 scopus 로고
    • Some aspects of pH and temperature dependence of the NMR spectra of cytochrome c
    • Gupta R.K., Koenig S.H. Some aspects of pH and temperature dependence of the NMR spectra of cytochrome c. Biochem. Biophys. Res. Commun. 45:1971;1134-1143
    • (1971) Biochem. Biophys. Res. Commun. , vol.45 , pp. 1134-1143
    • Gupta, R.K.1    Koenig, S.H.2
  • 12
    • 0017697819 scopus 로고
    • Nuclear magnetic resonance studies of hemoproteins: IX. pH dependent features of horse heart ferric cytochrome c
    • Morishima I., Ogawa S., Yonezawa T., Iizuka T. Nuclear magnetic resonance studies of hemoproteins: IX. pH dependent features of horse heart ferric cytochrome c. Biochim. Biophys. Acta. 495:1977;287-298
    • (1977) Biochim. Biophys. Acta , vol.495 , pp. 287-298
    • Morishima, I.1    Ogawa, S.2    Yonezawa, T.3    Iizuka, T.4
  • 13
    • 33947437177 scopus 로고
    • Studies on cytochrome c: II. the optical properties of pure cytochrome c and some of its derivatives
    • Theorell H., Åkesson Å. Studies on cytochrome c: II. The optical properties of pure cytochrome c and some of its derivatives. J. Am. Chem. Soc. 63:1941;1812-1818
    • (1941) J. Am. Chem. Soc. , vol.63 , pp. 1812-1818
    • Theorell, H.1    Åkesson, Å.2
  • 14
    • 0024537169 scopus 로고
    • Fourier-transform infra-red studies of the alkaline isomerization of mitochondria cytochrome c and the ionization of carboxylic acids
    • Tonge P., Moore G.R., Wharton C.W. Fourier-transform infra-red studies of the alkaline isomerization of mitochondria cytochrome c and the ionization of carboxylic acids. Biochem. J. 258:1989;599-605
    • (1989) Biochem. J. , vol.258 , pp. 599-605
    • Tonge, P.1    Moore, G.R.2    Wharton, C.W.3
  • 16
    • 0036558165 scopus 로고    scopus 로고
    • Direct electrochemistry of cytochrome c at a glassy carbon electrode modified with single-wall carbon nanotubes
    • Wang J., Li M., Shi Z., Li N., Gu Z. Direct electrochemistry of cytochrome c at a glassy carbon electrode modified with single-wall carbon nanotubes. Anal. Chem. 74:2002;1993-1997
    • (2002) Anal. Chem. , vol.74 , pp. 1993-1997
    • Wang, J.1    Li, M.2    Shi, Z.3    Li, N.4    Gu, Z.5
  • 17
    • 0031384224 scopus 로고    scopus 로고
    • Protein electrochemistry at carbon nanotube electrodes
    • Davis J.J., Coles R.J., Hill H.A.O. Protein electrochemistry at carbon nanotube electrodes. J. Electroanal. Chem. 440:1997;279-282
    • (1997) J. Electroanal. Chem. , vol.440 , pp. 279-282
    • Davis, J.J.1    Coles, R.J.2    Hill, H.A.O.3
  • 18
    • 0031004544 scopus 로고    scopus 로고
    • The application of circular dichroism to studies of protein folding and unfolding
    • Kelly S.M., Price N.C. The application of circular dichroism to studies of protein folding and unfolding. Biochim. Biophys. Acta. 1338:1997;161-185
    • (1997) Biochim. Biophys. Acta , vol.1338 , pp. 161-185
    • Kelly, S.M.1    Price, N.C.2
  • 19
    • 0015526732 scopus 로고
    • Participation of the protein ligands in the folding of cytochrome c
    • Babul J., Stellwagen E. Participation of the protein ligands in the folding of cytochrome c. Biochemistry. 11:1972;1195-1200
    • (1972) Biochemistry , vol.11 , pp. 1195-1200
    • Babul, J.1    Stellwagen, E.2
  • 21
    • 0034735702 scopus 로고    scopus 로고
    • Conformational transition of DNA in electroreduction studied by in situ UV and CD thin layer spectroelectrochemistry
    • Zhu Y., Cheng G., Dong S. Conformational transition of DNA in electroreduction studied by in situ UV and CD thin layer spectroelectrochemistry. Biophys. Chem. 87:2000;103-110
    • (2000) Biophys. Chem. , vol.87 , pp. 103-110
    • Zhu, Y.1    Cheng, G.2    Dong, S.3
  • 22
    • 0035869686 scopus 로고    scopus 로고
    • The electrochemically induced conformational transition of disulfides in bovine serum albumin studied by thin layer circular dichroism spectroelectrochemistry
    • Zhu Y., Cheng G., Dong S. The electrochemically induced conformational transition of disulfides in bovine serum albumin studied by thin layer circular dichroism spectroelectrochemistry. Biophy. Chem. 90:2001;1-8
    • (2001) Biophy. Chem. , vol.90 , pp. 1-8
    • Zhu, Y.1    Cheng, G.2    Dong, S.3
  • 23
    • 0032508940 scopus 로고    scopus 로고
    • Alkaline conformational transitions of ferricytochrome c studied by Resonance Raman spectroscopy
    • Döpner S., Hildebrandt P., Rosell F.I., Mauk A.G. Alkaline conformational transitions of ferricytochrome c studied by Resonance Raman spectroscopy. J. Am. Chem. Soc. 120:1998;11246-11255
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11246-11255
    • Döpner, S.1    Hildebrandt, P.2    Rosell, F.I.3    Mauk, A.G.4
  • 24
    • 0035401143 scopus 로고    scopus 로고
    • Conformational stability of ferricytochrome c near the heme in its complex with heparin in alkaline pH
    • Bàgel'ová J., Gazová Z., Valušová E., Antalik M. Conformational stability of ferricytochrome c near the heme in its complex with heparin in alkaline pH. Carbohydr. Polym. 45:2001;227-232
    • (2001) Carbohydr. Polym. , vol.45 , pp. 227-232
    • Bàgel'Ová, J.1    Gazová, Z.2    Valušová, E.3    Antalik, M.4
  • 25
    • 0032508965 scopus 로고    scopus 로고
    • Proton-linked protein conformational switching: Definition of the alkaline conformational transition of yeast iso-1-ferricytochrome c
    • Rosell F.I., Ferrer J.C., Mauk A.G. Proton-linked protein conformational switching: definition of the alkaline conformational transition of yeast iso-1-ferricytochrome c. J. Am. Chem. Soc. 120:1998;11234-11245
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11234-11245
    • Rosell, F.I.1    Ferrer, J.C.2    Mauk, A.G.3
  • 26
    • 0027062939 scopus 로고
    • Spectrophotometric detection of the interaction between cytochrome c and heparin
    • Antalìk M., Bona M., Bágel'ová J. Spectrophotometric detection of the interaction between cytochrome c and heparin. Biochem. Int. 28:1992;675-682
    • (1992) Biochem. Int. , vol.28 , pp. 675-682
    • Antalìk, M.1    Bona, M.2    Bágel'Ová, J.3
  • 27
    • 0042622662 scopus 로고    scopus 로고
    • Effect of varying polyglutamate chain length on the structure and stability of ferricytochrome c
    • Antalìk M., Bágel'ová J., Gazová Z., Musatov A., Fedunová D. Effect of varying polyglutamate chain length on the structure and stability of ferricytochrome c. Biochim. Biophys. Acta. 1646:2003;11-20
    • (2003) Biochim. Biophys. Acta , vol.1646 , pp. 11-20
    • Antalìk, M.1    Bágel'Ová, J.2    Gazová, Z.3    Musatov, A.4    Fedunová, D.5
  • 28
    • 0035242492 scopus 로고    scopus 로고
    • Effects of specific anion-protein binding on the alkaline transition of cytochrome c
    • Battistuzzi G., Borsari M., Ranieri A., Sola M. Effects of specific anion-protein binding on the alkaline transition of cytochrome c. Arch. Biochem. Biophys. 386:2001;117-122
    • (2001) Arch. Biochem. Biophys. , vol.386 , pp. 117-122
    • Battistuzzi, G.1    Borsari, M.2    Ranieri, A.3    Sola, M.4
  • 30
    • 0026254055 scopus 로고
    • Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water
    • Scholtz J.M., Qian H., York E.J., Stewart J.M., Baldwin R.L. Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water. Biopolymers. 31:1991;1463-1470
    • (1991) Biopolymers , vol.31 , pp. 1463-1470
    • Scholtz, J.M.1    Qian, H.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 31
    • 0027482684 scopus 로고
    • Protein secondary structure from Fourier Transform Infrared and/or Circular Dichroism Spectra
    • Pribić R., Vanstokkum I.H.M., Chapman D., Haris P.I., Bloemendal M. Protein secondary structure from Fourier Transform Infrared and/or Circular Dichroism Spectra. Anal. Biochem. 214:1993;366-378
    • (1993) Anal. Biochem. , vol.214 , pp. 366-378
    • Pribić, R.1    Vanstokkum, I.H.M.2    Chapman, D.3    Haris, P.I.4    Bloemendal, M.5
  • 32
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Å resolution
    • Deisenhofer J., Epp O., Miki K., Huber R., Michel H. Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Å resolution. Nature. 318:1985;618-624
    • (1985) Nature , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 33
    • 33751385611 scopus 로고
    • Electrochemically induced conformational changes in cytochrome c monitored by Fourier Transform Infrared Difference Spectroscopy: Influence of temperature, pH, and electrode surfaces
    • Schlereth D.D., Maentele W. Electrochemically induced conformational changes in cytochrome c monitored by Fourier Transform Infrared Difference Spectroscopy: influence of temperature, pH, and electrode surfaces. Biochemistry. 32:1993;1118-1126
    • (1993) Biochemistry , vol.32 , pp. 1118-1126
    • Schlereth, D.D.1    Maentele, W.2
  • 34
    • 0024316314 scopus 로고
    • Ionic strength dependence of cytochrome c structure and Trp-59 H/D exchange from Ultraviolet Resonance Raman spectroscopy
    • Liu G., Grygon C.A., Spiro T.G. Ionic strength dependence of cytochrome c structure and Trp-59 H/D exchange from Ultraviolet Resonance Raman spectroscopy. Biochemistry. 28:1989;5046-5050
    • (1989) Biochemistry , vol.28 , pp. 5046-5050
    • Liu, G.1    Grygon, C.A.2    Spiro, T.G.3
  • 36
    • 0000402746 scopus 로고
    • Elimination of the negative Soret cotton effect of cytochrome c by replacement of the invariant Phenylalanine using site-directed mutagenesis
    • Pielak G.J., Oikawa K., Mauk A.G., Smith M., Kay C.M. Elimination of the negative Soret cotton effect of cytochrome c by replacement of the invariant Phenylalanine using site-directed mutagenesis. J. Am. Chem. Soc. 108:1986;2724-2727
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 2724-2727
    • Pielak, G.J.1    Oikawa, K.2    Mauk, A.G.3    Smith, M.4    Kay, C.M.5


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