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Volumn 47, Issue 36, 2008, Pages 9667-9677

The conformational manifold of ferricytochrome c explored by visible and far-UV electronic circular dichroism spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION; CELL DEATH; CELL MEMBRANES; CIRCULAR DICHROISM SPECTROSCOPY; CONCENTRATION (PROCESS); CYTOLOGY; DICHROISM; IONIC STRENGTH; OPTICAL PROPERTIES; PH; PH EFFECTS; PORPHYRINS; THERMODYNAMICS; TRANSFER FUNCTIONS;

EID: 51549102406     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800729w     Document Type: Article
Times cited : (41)

References (47)
  • 2
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu, X., Kim, C. N., Yang, J., Jemmerson, R., and Wang, X. (1996) Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86, 147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 3
    • 0033596909 scopus 로고    scopus 로고
    • A conformational change in cytochrome c of apoptotic and necrotic cells is detected by monoclonal antibody binding and mimicked by association of the native antigen with synthetic phospholipid vesicles
    • Jemmerson, R., Liu, J., Hausauer, D., Lam, K-P., Mondino, A., and Nelson, R. D. (1999) A conformational change in cytochrome c of apoptotic and necrotic cells is detected by monoclonal antibody binding and mimicked by association of the native antigen with synthetic phospholipid vesicles. Biochemistry 38, 3599-3609.
    • (1999) Biochemistry , vol.38 , pp. 3599-3609
    • Jemmerson, R.1    Liu, J.2    Hausauer, D.3    Lam, K.-P.4    Mondino, A.5    Nelson, R.D.6
  • 5
    • 0028840891 scopus 로고
    • The nature of the thermal equilibrium affecting the iron coordination of ferric cytochrome c
    • Taler, G., Schejter, A., Navon, G., Vig, I., and Margoliash, E. (1995) The nature of the thermal equilibrium affecting the iron coordination of ferric cytochrome c. Biochemistry 34, 14209-14212.
    • (1995) Biochemistry , vol.34 , pp. 14209-14212
    • Taler, G.1    Schejter, A.2    Navon, G.3    Vig, I.4    Margoliash, E.5
  • 7
    • 0020478683 scopus 로고
    • Spin state and unfolding equilibria of ferri-cytochrome c in acidic solution
    • Dyson, H. J., and Beattie, J. K. (1982) Spin state and unfolding equilibria of ferri-cytochrome c in acidic solution. J. Biol. Chem. 257, 2267-2273.
    • (1982) J. Biol. Chem , vol.257 , pp. 2267-2273
    • Dyson, H.J.1    Beattie, J.K.2
  • 8
    • 0025195499 scopus 로고
    • Mechanism of Acid-Induced Folding of Proteins
    • Goto, Y., Takahashi, N., and Fink, A. L. (1990) Mechanism of Acid-Induced Folding of Proteins. Biochemistry 29, 3480-3488.
    • (1990) Biochemistry , vol.29 , pp. 3480-3488
    • Goto, Y.1    Takahashi, N.2    Fink, A.L.3
  • 9
    • 0032508940 scopus 로고    scopus 로고
    • The alkaline conformational transitions of ferricytochrome c studied by resonance Raman spectroscopy
    • Döpner, S., Hildebrandt, P., Rosell, F. I., and Mauk, A. G. (1998) The alkaline conformational transitions of ferricytochrome c studied by resonance Raman spectroscopy. J. Am. Chem. Soc. 120, 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
  • 10
    • 0032508965 scopus 로고    scopus 로고
    • Proton-linked protein conformational switching: Definition of the alkaline conformational transition of yeast iso-1-ferricytochrome c
    • Rossel, F. I., Ferrer, J. C., and Mauk, A. G. (1998) Proton-linked protein conformational switching: definition of the alkaline conformational transition of yeast iso-1-ferricytochrome c. J. Am. Chem. Soc. 120, 11234-11245.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 11234-11245
    • Rossel, F.I.1    Ferrer, J.C.2    Mauk, A.G.3
  • 11
    • 0034805505 scopus 로고    scopus 로고
    • Resolving the individual components of a pH-induced conformational change
    • Blouin, C., Guillemette, J. G., and Wallace, C. J. A. (2001) Resolving the individual components of a pH-induced conformational change. Biophys. J. 81, 2331-2338.
    • (2001) Biophys. J , vol.81 , pp. 2331-2338
    • Blouin, C.1    Guillemette, J.G.2    Wallace, C.J.A.3
  • 12
    • 0033561331 scopus 로고    scopus 로고
    • The structural and functional role of lysine residues in the binding domain of cytochrome c for the redox process with cytochrome c oxidase
    • Döpner, S., Hildebrandt, P., Rosell, F. I., Mauk, A. G., von Walter, M., Soulimane, T., and Buse, G. (1999) The structural and functional role of lysine residues in the binding domain of cytochrome c for the redox process with cytochrome c oxidase. Eur. J. Biochem. 261, 379-391.
    • (1999) Eur. J. Biochem , vol.261 , pp. 379-391
    • Döpner, S.1    Hildebrandt, P.2    Rosell, F.I.3    Mauk, A.G.4    von Walter, M.5    Soulimane, T.6    Buse, G.7
  • 13
    • 33750828962 scopus 로고    scopus 로고
    • The alkali molten globule state of horse ferricytochrome c: Observation of cold denaturation
    • Kumar, R., Prabhu, N. P., Rao, D. K., and Bhuyan, A. K. (2006) The alkali molten globule state of horse ferricytochrome c: Observation of cold denaturation. J. Mol. Biol. 364, 483-495.
    • (2006) J. Mol. Biol , vol.364 , pp. 483-495
    • Kumar, R.1    Prabhu, N.P.2    Rao, D.K.3    Bhuyan, A.K.4
  • 14
    • 33750698968 scopus 로고    scopus 로고
    • Direct and high resolution characterization of cytochrome C equilibrium folding
    • Sagle, L. B., Zimmermann, J., Dawson, P. E., and Romesberg, F. E. (2006) Direct and high resolution characterization of cytochrome C equilibrium folding. J. Am. Chem. Soc. 128, 14232-14233.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 14232-14233
    • Sagle, L.B.1    Zimmermann, J.2    Dawson, P.E.3    Romesberg, F.E.4
  • 15
    • 0033843794 scopus 로고    scopus 로고
    • Probing local thermal stabilities of bovine, horse, and tuna ferricytochromes c at pH 7
    • Filosa, A., and English, A. M. (2000) Probing local thermal stabilities of bovine, horse, and tuna ferricytochromes c at pH 7. JBIC, J. Biol. Inorg. Chem. 4, 448-454.
    • (2000) JBIC, J. Biol. Inorg. Chem , vol.4 , pp. 448-454
    • Filosa, A.1    English, A.M.2
  • 16
    • 0001714784 scopus 로고
    • The 695 mμ band of ferricytochrome c and its relationship to protein conformation
    • Schejter, A., and George, P. (1964) The 695 mμ band of ferricytochrome c and its relationship to protein conformation. Biochemistry 3, 1045-1049.
    • (1964) Biochemistry , vol.3 , pp. 1045-1049
    • Schejter, A.1    George, P.2
  • 17
    • 0000116722 scopus 로고
    • pH-Linked conformational regulation of a metalloprotein oxidation-reduction equilibrium: Electrochemical analysis of the alkaline form of cytochrome c
    • Barker, P. D., and Mauk, A. G. (1992) pH-Linked conformational regulation of a metalloprotein oxidation-reduction equilibrium: electrochemical analysis of the alkaline form of cytochrome c. J. Am. Chem. Soc. 114, 3619-3624.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 3619-3624
    • Barker, P.D.1    Mauk, A.G.2
  • 18
    • 0032735068 scopus 로고    scopus 로고
    • Effects of nonspecific ion-protein interactions on the redox chemistry of cytochrome c
    • Battistuzzi, G., Loschi, L., Borsari, M., and Sola, M. (1999) Effects of nonspecific ion-protein interactions on the redox chemistry of cytochrome c. JBIC, J. Biol. Inorg. Chem. 4, 601-607.
    • (1999) JBIC, J. Biol. Inorg. Chem , vol.4 , pp. 601-607
    • Battistuzzi, G.1    Loschi, L.2    Borsari, M.3    Sola, M.4
  • 20
    • 34548240556 scopus 로고    scopus 로고
    • Conformational substates of horse heart cytochrome c exhibit different thermal unfolding of the heme cavity
    • Schweitzer-Stenner, R., Shah, R., Hagarman, A., and Dragomir, I. (2007) Conformational substates of horse heart cytochrome c exhibit different thermal unfolding of the heme cavity. J. Phys. Chem. B 111, 9603-9607.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 9603-9607
    • Schweitzer-Stenner, R.1    Shah, R.2    Hagarman, A.3    Dragomir, I.4
  • 21
    • 0014249253 scopus 로고
    • Conformation of cytochromes. III. Effect of urea, temperature, extrinsic ligands and pH variation on the conformation of horse heart ferricytochrome-c
    • Myer, Y. P. (1968) Conformation of cytochromes. III. Effect of urea, temperature, extrinsic ligands and pH variation on the conformation of horse heart ferricytochrome-c. Biochemistry 7, 765-776.
    • (1968) Biochemistry , vol.7 , pp. 765-776
    • Myer, Y.P.1
  • 22
    • 0014011435 scopus 로고
    • Optical rotatory dispersion of cytochrome c II. Comparative data for a heme octapeptide
    • Myer, Y. P., and Harbury, H. A. (1966) Optical rotatory dispersion of cytochrome c II. Comparative data for a heme octapeptide. J. Biol. Chem. 241, 4299-4303.
    • (1966) J. Biol. Chem , vol.241 , pp. 4299-4303
    • Myer, Y.P.1    Harbury, H.A.2
  • 24
    • 0013792676 scopus 로고
    • Protein-heme interactions in heme-proteins: Cytochrome C
    • Urry, D. W. (1965) Protein-heme interactions in heme-proteins: cytochrome C. Proc. Natl. Acad. Sci. U.S.A. 54, 640-648.
    • (1965) Proc. Natl. Acad. Sci. U.S.A , vol.54 , pp. 640-648
    • Urry, D.W.1
  • 26
    • 0015223110 scopus 로고
    • The origin of the heme cotton effects in myoglobin and hemoglobin
    • Hsu, M. C., and Woody, R. W. (1971) The origin of the heme cotton effects in myoglobin and hemoglobin. J. Am. Chem. Soc. 93, 3515-3525.
    • (1971) J. Am. Chem. Soc , vol.93 , pp. 3515-3525
    • Hsu, M.C.1    Woody, R.W.2
  • 27
    • 0037012419 scopus 로고    scopus 로고
    • Heme distortions in sperm-whale carbonmonoxy myoglobin: Correlations between rotational strengths and heme distortions in MD-generated structures
    • Kiefl, C., Sreerama, N., Haddad, R., Sun, L., Jentzen, W., Lu, Y., Qiu, Y., Shelnutt, J. A., and Woody, R. W. (2002) Heme distortions in sperm-whale carbonmonoxy myoglobin: correlations between rotational strengths and heme distortions in MD-generated structures. J. Am. Chem. Soc. 124, 3385-3394.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 3385-3394
    • Kiefl, C.1    Sreerama, N.2    Haddad, R.3    Sun, L.4    Jentzen, W.5    Lu, Y.6    Qiu, Y.7    Shelnutt, J.A.8    Woody, R.W.9
  • 28
    • 33846829579 scopus 로고    scopus 로고
    • Optical band splitting and electronic perturbations of the heme chromophore in cytochrome c at room temperature probed by visible electronic circular dichroism spectroscopy
    • Dragomir, I., Hagarman, A., Wallace, C., and Schweitzer-Stenner, R. (2007) Optical band splitting and electronic perturbations of the heme chromophore in cytochrome c at room temperature probed by visible electronic circular dichroism spectroscopy. Biophys. J. 92, 989-998.
    • (2007) Biophys. J , vol.92 , pp. 989-998
    • Dragomir, I.1    Hagarman, A.2    Wallace, C.3    Schweitzer-Stenner, R.4
  • 29
    • 34948899906 scopus 로고    scopus 로고
    • The asymmetric band profile of the soret band of deoxymyoglobin is caused by electronic and vibronic perturbations of the heme group rather than by a doming deformation
    • Schweitzer-Stenner, R., Gorden, J. P., and Hagarman, A. (2007) The asymmetric band profile of the soret band of deoxymyoglobin is caused by electronic and vibronic perturbations of the heme group rather than by a doming deformation. J. Chem. Phys. 127, 135103.
    • (2007) J. Chem. Phys , vol.127 , pp. 135103
    • Schweitzer-Stenner, R.1    Gorden, J.P.2    Hagarman, A.3
  • 30
    • 0035902439 scopus 로고    scopus 로고
    • Two-dimensional infrared correlation spectroscopy as a probe of sequential events in the thermal unfolding of cytochromes c
    • Filosa, A., Yang, Y., Ismail, A. A., and English, A. M. (2001) Two-dimensional infrared correlation spectroscopy as a probe of sequential events in the thermal unfolding of cytochromes c. Biochemistry 40, 8256-8263.
    • (2001) Biochemistry , vol.40 , pp. 8256-8263
    • Filosa, A.1    Yang, Y.2    Ismail, A.A.3    English, A.M.4
  • 31
    • 0001590073 scopus 로고    scopus 로고
    • The effects of protein environment on the low temperature electronic spectroscopy of cytochrome c and microperoxidase-11.7
    • Manas, E. S., Vaderkooi, J. M., and Sharp, K. A. (1999) The effects of protein environment on the low temperature electronic spectroscopy of cytochrome c and microperoxidase-11.7. Phys. Chem. B 103, 6334-6348.
    • (1999) Phys. Chem. B , vol.103 , pp. 6334-6348
    • Manas, E.S.1    Vaderkooi, J.M.2    Sharp, K.A.3
  • 32
    • 0032754454 scopus 로고    scopus 로고
    • FTIR-monitored thermal titration reveals different mechanisms for the alkaline isomerization of tuna compared to horse and bovine cytochromes c
    • Filosa, A., Ismail, A. A., and English, A. M. (1999) FTIR-monitored thermal titration reveals different mechanisms for the alkaline isomerization of tuna compared to horse and bovine cytochromes c. JBIC, J. Biol. Inorg. Chem. 4, 717-726.
    • (1999) JBIC, J. Biol. Inorg. Chem , vol.4 , pp. 717-726
    • Filosa, A.1    Ismail, A.A.2    English, A.M.3
  • 33
    • 33745137861 scopus 로고    scopus 로고
    • Order of steps in the cytochrome c folding pathway: Evidence for a sequential stabilization mechanism
    • Krishna, M. M. G., Maity, H., Rumbley, J. N., Lin, Y., and Englander, S. W. (2006) Order of steps in the cytochrome c folding pathway: Evidence for a sequential stabilization mechanism. J. Mol. Biol. 359, 1410-1419.
    • (2006) J. Mol. Biol , vol.359 , pp. 1410-1419
    • Krishna, M.M.G.1    Maity, H.2    Rumbley, J.N.3    Lin, Y.4    Englander, S.W.5
  • 34
    • 42949105053 scopus 로고    scopus 로고
    • Structural changes of horse heart ferricytochrome c induced by changes of ionic strength and anion binding
    • in press
    • Shah, R., and Schweitzer-Stenner, R. (2008) Structural changes of horse heart ferricytochrome c induced by changes of ionic strength and anion binding. Biochemistry, in press.
    • (2008) Biochemistry
    • Shah, R.1    Schweitzer-Stenner, R.2
  • 35
    • 4644319196 scopus 로고    scopus 로고
    • CDtool - An integrated software package for circular dichroism spectroscopic data processing, analysis and archiving
    • Lees, J. G., Smith, B., Wien, F., Miles, A., and Wallace, B. A. (2004) CDtool - An integrated software package for circular dichroism spectroscopic data processing, analysis and archiving. Anal. Biochem. 332, 285-289.
    • (2004) Anal. Biochem , vol.332 , pp. 285-289
    • Lees, J.G.1    Smith, B.2    Wien, F.3    Miles, A.4    Wallace, B.A.5
  • 36
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore, L., and Wallace, B. A. (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32, W668-W673.
    • (2004) Nucleic Acids Res , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 37
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • Lobley, A., Whitmore, L., and Wallace, B. A. (2002) DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 18, 211-212.
    • (2002) Bioinformatics , vol.18 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 38
    • 0035954963 scopus 로고    scopus 로고
    • Electronic and vibronic contributions to the band splitting in optical spectra of heme proteins
    • Schweitzer-Stenner, R., and Bigman, D. (2001) Electronic and vibronic contributions to the band splitting in optical spectra of heme proteins. J. Phys. Chem. B 105, 7064-7073.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 7064-7073
    • Schweitzer-Stenner, R.1    Bigman, D.2
  • 39
    • 23944513634 scopus 로고    scopus 로고
    • The importance of vibronic perturbations in ferrocytochrome c spectra: A reevaluation of spectral properties based on low-temperature optical absorption, resonance Raman, and molecular-dynamics simulations
    • Levantino, M., Huang, Q., Cupane, A., Laberge, M., Hagarman, A., and Schweitzer-Stenner, R. (2005) The importance of vibronic perturbations in ferrocytochrome c spectra: A reevaluation of spectral properties based on low-temperature optical absorption, resonance Raman, and molecular-dynamics simulations. J. Chem. Phys. 123, 054508.
    • (2005) J. Chem. Phys , vol.123 , pp. 054508
    • Levantino, M.1    Huang, Q.2    Cupane, A.3    Laberge, M.4    Hagarman, A.5    Schweitzer-Stenner, R.6
  • 40
    • 0034224178 scopus 로고    scopus 로고
    • The influence of protein environment on the low temperature electronic spectroscopy of Zn-substituted cytochrome c
    • Manas, E. S., Wright, W. W., Sharp, K. A., Friedrich, J., and Vanderkooi, J. M. (2000) The influence of protein environment on the low temperature electronic spectroscopy of Zn-substituted cytochrome c. J. Phys. Chem. B 104, 6932-6941.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 6932-6941
    • Manas, E.S.1    Wright, W.W.2    Sharp, K.A.3    Friedrich, J.4    Vanderkooi, J.M.5
  • 41
    • 0027199762 scopus 로고
    • Optical activity of hemoproteins in the soret region, circular dichroism of the heme undecapeptide of cytochrome c in aqueous solution
    • Blauer, G., Sreerama, N., and Woody, R. W. (1993) Optical activity of hemoproteins in the soret region, circular dichroism of the heme undecapeptide of cytochrome c in aqueous solution. Biochemistry 32, 6674-6679.
    • (1993) Biochemistry , vol.32 , pp. 6674-6679
    • Blauer, G.1    Sreerama, N.2    Woody, R.W.3
  • 42
    • 51049091874 scopus 로고    scopus 로고
    • The Internal Electric Field in Cytochrome C Explored by Visible Electronic Circular Dichroism Spectroscopy
    • Online early access, DOI: 10.1021/jp802495q. Published Online: July 30, 2008
    • Schweitzer-Stenner, R. (2008) The Internal Electric Field in Cytochrome C Explored by Visible Electronic Circular Dichroism Spectroscopy. J. Phys. Chem. B. [Online early access]. DOI: 10.1021/jp802495q. Published Online: July 30, 2008. http:// pubs.acs.org/cgi-bin/asap.cgi/jpcbfk/asap/html/jp802495q. html.
    • (2008) J. Phys. Chem. B
    • Schweitzer-Stenner, R.1
  • 43
    • 0037198831 scopus 로고    scopus 로고
    • Optical Spectra of Fe(II) Cytochrome c Interpreted Using Molecular Dynamics Simulations and Quantum mechanical Calculations
    • Prabhu, N. V., Dalosto, S. D., Sharp, K. A., Wright, W. W., and Vanderkooi, J.M. (2002) Optical Spectra of Fe(II) Cytochrome c Interpreted Using Molecular Dynamics Simulations and Quantum mechanical Calculations. J. Phys. Chem. B 106, 5561-5571.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 5561-5571
    • Prabhu, N.V.1    Dalosto, S.D.2    Sharp, K.A.3    Wright, W.W.4    Vanderkooi, J.M.5
  • 44
    • 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., and Kay, C. M. (1986) 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, 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
  • 45
    • 0034682558 scopus 로고    scopus 로고
    • Effect of pH on Axial Ligand Coordination of Cytochrome c″ from Methylophilus methylotrophus and Horse Heart Cytochrome c
    • Indiani, C., de Sanctis, G., Neri, F., Santos, H., Smulevich, G., and Coletta, M. (2000) Effect of pH on Axial Ligand Coordination of Cytochrome c″ from Methylophilus methylotrophus and Horse Heart Cytochrome c. Biochemistry 39, 8234-8242.
    • (2000) Biochemistry , vol.39 , pp. 8234-8242
    • Indiani, C.1    de Sanctis, G.2    Neri, F.3    Santos, H.4    Smulevich, G.5    Coletta, M.6
  • 46
    • 17044441821 scopus 로고    scopus 로고
    • Structural and Kinetic Description of Cytochrome c Unfolding Induced by the Interaction with Lipid Vesicles
    • Pinheiro, T. J. T., Elöve, G., Watts, A., and Roder, H. (1997) Structural and Kinetic Description of Cytochrome c Unfolding Induced by the Interaction with Lipid Vesicles. Biochemistry 36, 13122-13132.
    • (1997) Biochemistry , vol.36 , pp. 13122-13132
    • Pinheiro, T.J.T.1    Elöve, G.2    Watts, A.3    Roder, H.4
  • 47
    • 0022523277 scopus 로고
    • Nitrosyl (III) hemoglobin: Autorerduction and spectroscopy
    • Addison, A. W., and Stephanos, J. J. (1986) Nitrosyl (III) hemoglobin: autorerduction and spectroscopy. Biochemistry 25, 4104-4113.
    • (1986) Biochemistry , vol.25 , pp. 4104-4113
    • Addison, A.W.1    Stephanos, J.J.2


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