메뉴 건너뛰기




Volumn 52, Issue 4, 2013, Pages 653-666

Recombinant expression, biophysical characterization, and cardiolipin-induced changes of two Caenorhabditis elegans cytochrome c proteins

Author keywords

[No Author keywords available]

Indexed keywords

BIOPHYSICAL CHARACTERIZATION; CAENORHABDITIS ELEGANS; CARDIOLIPINS; CONFORMATIONAL ENSEMBLE; CYTOCHROME C; DENATURED STATE; DISTANCE DISTRIBUTIONS; ELEGANS; HEME LIGATION; PEROXIDASE ACTIVITIES; RECOMBINANT EXPRESSION; REDOX PROPERTY; SPECTROSCOPIC TOOL; STRUCTURAL FEATURE; TIME-RESOLVED FLUORESCENCE;

EID: 84873857633     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3014938     Document Type: Article
Times cited : (10)

References (87)
  • 3
    • 0026697272 scopus 로고
    • Electron-tunneling pathways in cytochrome c
    • Wuttke, D. S., Bjerrum, M. J., Winkler, J. R., and Gray, H. B. (1992) Electron-tunneling pathways in cytochrome c Science 256, 1007-1009
    • (1992) Science , vol.256 , pp. 1007-1009
    • Wuttke, D.S.1    Bjerrum, M.J.2    Winkler, J.R.3    Gray, H.B.4
  • 4
    • 84861910382 scopus 로고    scopus 로고
    • Heme-protein vibrational couplings in cytochrome c provide a dynamic link that connects the heme-iron and the protein surface
    • Galinato, M. G., Kleingardner, J. G., Bowman, S. E., Alp, E. E., Zhao, J., Bren, K. L., and Lehnert, N. (2012) Heme-protein vibrational couplings in cytochrome c provide a dynamic link that connects the heme-iron and the protein surface Proc. Natl. Acad. Sci. U.S.A. 109, 8896-8900
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 8896-8900
    • Galinato, M.G.1    Kleingardner, J.G.2    Bowman, S.E.3    Alp, E.E.4    Zhao, J.5    Bren, K.L.6    Lehnert, N.7
  • 5
    • 0037122125 scopus 로고    scopus 로고
    • Electron-transfer dynamics of cytochrome c: A change in the reaction mechanism with distance
    • Wei, J., Liu, H., Khoshtariya, D. E., Yamamoto, H., Dick, A., and Waldeck, D. H. (2002) Electron-transfer dynamics of cytochrome c: A change in the reaction mechanism with distance Angew. Chem., Int. Ed. 41, 4700-4703
    • (2002) Angew. Chem., Int. Ed. , vol.41 , pp. 4700-4703
    • Wei, J.1    Liu, H.2    Khoshtariya, D.E.3    Yamamoto, H.4    Dick, A.5    Waldeck, D.H.6
  • 6
    • 4644359012 scopus 로고    scopus 로고
    • How cytochrome c folds, and why: Submolecular foldon units and their stepwise sequential stabilization
    • Maity, H., Maity, M., and Englander, S. W. (2004) How cytochrome c folds, and why: Submolecular foldon units and their stepwise sequential stabilization J. Mol. Biol. 343, 223-233
    • (2004) J. Mol. Biol. , vol.343 , pp. 223-233
    • Maity, H.1    Maity, M.2    Englander, S.W.3
  • 7
    • 1842531459 scopus 로고    scopus 로고
    • Cytochrome c folding dynamics
    • Winkler, J. R. (2004) Cytochrome c folding dynamics Curr. Opin. Chem. Biol. 8, 169-174
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 169-174
    • Winkler, J.R.1
  • 8
    • 0035979801 scopus 로고    scopus 로고
    • Denatured state thermodynamics: Residual structure, chain stiffness, and scaling factors
    • Hammack, B. N., Smith, C. R., and Bowler, B. E. (2001) Denatured state thermodynamics: Residual structure, chain stiffness, and scaling factors J. Mol. Biol. 311, 1091-1104
    • (2001) J. Mol. Biol. , vol.311 , pp. 1091-1104
    • Hammack, B.N.1    Smith, C.R.2    Bowler, B.E.3
  • 9
    • 0025007598 scopus 로고
    • High-resolution 3-dimensional structure of horse heart cytochrome c
    • Bushnell, G. W., Louie, G. V., and Brayer, G. D. (1990) High-resolution 3-dimensional structure of horse heart cytochrome c J. Mol. Biol. 214, 585-595
    • (1990) J. Mol. Biol. , vol.214 , pp. 585-595
    • Bushnell, G.W.1    Louie, G.V.2    Brayer, G.D.3
  • 10
    • 0032583439 scopus 로고    scopus 로고
    • Effects of ligation and folding on reduction potentials of heme proteins
    • Tezcan, F. A., Winkler, J. R., and Gray, H. B. (1998) Effects of ligation and folding on reduction potentials of heme proteins J. Am. Chem. Soc. 120, 13383-13388
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 13383-13388
    • Tezcan, F.A.1    Winkler, J.R.2    Gray, H.B.3
  • 11
    • 0041972670 scopus 로고    scopus 로고
    • How cytochromes with different folds control heme redox potentials
    • Mao, J., Hauser, K., and Gunner, M. R. (2003) How cytochromes with different folds control heme redox potentials Biochemistry 42, 9829-9840
    • (2003) Biochemistry , vol.42 , pp. 9829-9840
    • Mao, J.1    Hauser, K.2    Gunner, M.R.3
  • 12
    • 79953745644 scopus 로고    scopus 로고
    • The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: From respiration to apoptosis
    • Hüttemann, M., Pecina, P., Rainbolt, M., Sanderson, T. H., Kagan, V. E., Samavati, L., Doan, J. W., and Lee, I. (2011) The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: From respiration to apoptosis Mitochondrion 11, 369-381
    • (2011) Mitochondrion , vol.11 , pp. 369-381
    • Hüttemann, M.1    Pecina, P.2    Rainbolt, M.3    Sanderson, T.H.4    Kagan, V.E.5    Samavati, L.6    Doan, J.W.7    Lee, I.8
  • 14
    • 0033596980 scopus 로고    scopus 로고
    • An APAF-1·cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • Zou, H., Li, Y., Liu, X., and Wang, X. (1999) An APAF-1·cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9 J. Biol. Chem. 274, 11549-11556
    • (1999) J. Biol. Chem. , vol.274 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3    Wang, X.4
  • 17
    • 33846462466 scopus 로고    scopus 로고
    • A conformational switch to β-sheet structure in cytochrome c leads to heme exposure. Implications for cardiolipin peroxidation and apoptosis
    • Balakrishnan, G., Hu, Y., Oyerinde, O. F., Su, J., Groves, J. T., and Spiro, T. G. (2007) A conformational switch to β-sheet structure in cytochrome c leads to heme exposure. Implications for cardiolipin peroxidation and apoptosis J. Am. Chem. Soc. 129, 504-505
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 504-505
    • Balakrishnan, G.1    Hu, Y.2    Oyerinde, O.F.3    Su, J.4    Groves, J.T.5    Spiro, T.G.6
  • 19
    • 84867550132 scopus 로고    scopus 로고
    • Nitric oxide binding to the cardiolipin complex of ferric cytochrome c
    • Silkstone, G., Kapetanaki, S. M., Husu, I., Vos, M. H., and Wilson, M. T. (2012) Nitric oxide binding to the cardiolipin complex of ferric cytochrome c Biochemistry 51, 6760-6766
    • (2012) Biochemistry , vol.51 , pp. 6760-6766
    • Silkstone, G.1    Kapetanaki, S.M.2    Husu, I.3    Vos, M.H.4    Wilson, M.T.5
  • 20
    • 79958122758 scopus 로고    scopus 로고
    • Single vesicle observations of the cardiolipin-cytochrome c interaction: Induction of membrane morphology changes
    • Beales, P. A., Bergstrom, C. L., Geerts, N., Groves, J. T., and Vanderlick, T. K. (2011) Single vesicle observations of the cardiolipin- cytochrome c interaction: Induction of membrane morphology changes Langmuir 27, 6107-6115
    • (2011) Langmuir , vol.27 , pp. 6107-6115
    • Beales, P.A.1    Bergstrom, C.L.2    Geerts, N.3    Groves, J.T.4    Vanderlick, T.K.5
  • 22
    • 0042469295 scopus 로고    scopus 로고
    • Worms, Life, and Death (Nobel Lecture)
    • Horvitz, H. R. (2003) Worms, Life, and Death (Nobel Lecture) ChemBioChem 4, 697-711
    • (2003) ChemBioChem , vol.4 , pp. 697-711
    • Horvitz, H.R.1
  • 23
    • 73349128117 scopus 로고    scopus 로고
    • Genetic control of programmed cell death during animal development
    • Conradt, B. (2009) Genetic control of programmed cell death during animal development Annu. Rev. Genet. 43, 493-523
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 493-523
    • Conradt, B.1
  • 24
    • 0037159784 scopus 로고    scopus 로고
    • Mechanisms of AIF-mediated apoptotic DNA degradation in Caenorhabditis elegans
    • Wang, X., Yang, C., Chai, J., Shi, Y., and Xue, D. (2002) Mechanisms of AIF-mediated apoptotic DNA degradation in Caenorhabditis elegans Science 298, 1587-1592
    • (2002) Science , vol.298 , pp. 1587-1592
    • Wang, X.1    Yang, C.2    Chai, J.3    Shi, Y.4    Xue, D.5
  • 25
    • 0035811511 scopus 로고    scopus 로고
    • Mitochondrial endonuclease G is important for apoptosis in C. elegans
    • Parrish, J., Li, L., Klotz, K., Ledwich, D., Wang, X., and Xue, D. (2001) Mitochondrial endonuclease G is important for apoptosis in C. elegans Nature 412, 90-94
    • (2001) Nature , vol.412 , pp. 90-94
    • Parrish, J.1    Li, L.2    Klotz, K.3    Ledwich, D.4    Wang, X.5    Xue, D.6
  • 26
    • 13944278072 scopus 로고    scopus 로고
    • DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans
    • Jagasia, R., Grote, P., Westermann, B., and Conradt, B. (2005) DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans Nature 433, 754-760
    • (2005) Nature , vol.433 , pp. 754-760
    • Jagasia, R.1    Grote, P.2    Westermann, B.3    Conradt, B.4
  • 27
    • 19444386896 scopus 로고    scopus 로고
    • Apoptosis in Drosophila: Neither fish nor fowl (nor man, nor worm)
    • Kornbluth, S. and White, K. (2005) Apoptosis in Drosophila: Neither fish nor fowl (nor man, nor worm) J. Cell Sci. 118, 1779-1787
    • (2005) J. Cell Sci. , vol.118 , pp. 1779-1787
    • Kornbluth, S.1    White, K.2
  • 28
    • 0037188903 scopus 로고    scopus 로고
    • Destabilizing influences in apoptosis: Sowing the seeds of IAP destruction
    • Martin, S. J. (2002) Destabilizing influences in apoptosis: Sowing the seeds of IAP destruction Cell 109, 793-796
    • (2002) Cell , vol.109 , pp. 793-796
    • Martin, S.J.1
  • 29
    • 84856839349 scopus 로고    scopus 로고
    • Deficiency of cardiolipin synthase causes abnormal mitochondrial function and morphology in germ cells of Caenorhabditis elegans
    • Sakamoto, T., Inoue, T., Otomo, Y., Yokomori, N., Ohno, M., Arai, H., and Nakagawa, Y. (2012) Deficiency of cardiolipin synthase causes abnormal mitochondrial function and morphology in germ cells of Caenorhabditis elegans J. Biol. Chem. 287, 4590-4601
    • (2012) J. Biol. Chem. , vol.287 , pp. 4590-4601
    • Sakamoto, T.1    Inoue, T.2    Otomo, Y.3    Yokomori, N.4    Ohno, M.5    Arai, H.6    Nakagawa, Y.7
  • 31
    • 0021165666 scopus 로고
    • Differential regulation of the duplicated isocytochrome c genes in yeast
    • Laz, T. M., Pietras, D. F., and Sherman, F. (1984) Differential regulation of the duplicated isocytochrome c genes in yeast Proc. Natl. Acad. Sci. U.S.A. 81, 4475-4479
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 4475-4479
    • Laz, T.M.1    Pietras, D.F.2    Sherman, F.3
  • 32
    • 0022431848 scopus 로고
    • Characterization of two Drosophila melanogaster cylochrome c genes and their transcripts
    • Limbach, K. J. and Wu, R. (1985) Characterization of two Drosophila melanogaster cylochrome c genes and their transcripts Nucleic Acids Res. 13, 631-644
    • (1985) Nucleic Acids Res. , vol.13 , pp. 631-644
    • Limbach, K.J.1    Wu, R.2
  • 33
    • 0032509302 scopus 로고    scopus 로고
    • Genome sequence of the nematode C. elegans: A platform for investigating biology
    • C. elegans Sequencing Consortium ()
    • C. elegans Sequencing Consortium (1998) Genome sequence of the nematode C. elegans: a platform for investigating biology Science 282, 2012-2018
    • (1998) Science , vol.282 , pp. 2012-2018
  • 34
    • 0025026424 scopus 로고
    • The primary structure of cytochrome c from the nematode Caenorhabditis elegans
    • Vanfleteren, J. R., Evers, E. A., Van de Werken, G., and Van Beeumen, J. J. (1990) The primary structure of cytochrome c from the nematode Caenorhabditis elegans Biochem. J. 271, 613-620
    • (1990) Biochem. J. , vol.271 , pp. 613-620
    • Vanfleteren, J.R.1    Evers, E.A.2    Van De Werken, G.3    Van Beeumen, J.J.4
  • 35
    • 84869442007 scopus 로고    scopus 로고
    • Origin of the conformational heterogeneity of cardiolipin-bound cytochrome c
    • Hong, Y., Muenzner, J., Grimm, S. K., and Pletneva, E. V. (2012) Origin of the conformational heterogeneity of cardiolipin-bound cytochrome c J. Am. Chem. Soc. 134, 18713-18723
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 18713-18723
    • Hong, Y.1    Muenzner, J.2    Grimm, S.K.3    Pletneva, E.V.4
  • 36
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley, L. A. and Sternberg, M. J. E. (2009) Protein structure prediction on the Web: A case study using the Phyre server Nat. Protoc. 4, 363-371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 38
    • 77954441929 scopus 로고    scopus 로고
    • 552 with its flexible linker segment, a membrane-anchored protein from Paracoccus denitrificans
    • 552 with its flexible linker segment, a membrane-anchored protein from Paracoccus denitrificans Acta Crystallogr. D66, 850-854
    • (2010) Acta Crystallogr. , vol.66 , pp. 850-854
    • Rajendran, C.1    Ermler, U.2    Ludwig, B.3    Michel, H.4
  • 40
    • 70449234614 scopus 로고
    • Spectrum of horse-heart cytochrome c
    • Margoliash, E. and Frohwirt, N. (1959) Spectrum of horse-heart cytochrome c Biochem. J. 71, 570-572
    • (1959) Biochem. J. , vol.71 , pp. 570-572
    • Margoliash, E.1    Frohwirt, N.2
  • 42
    • 0034957675 scopus 로고    scopus 로고
    • Characterization of horse cytochrome c expressed in Escherichia coli
    • Patel, C. N., Lind, M. C., and Pielak, G. J. (2001) Characterization of horse cytochrome c expressed in Escherichia coli Protein Expression Purif. 22, 220-224
    • (2001) Protein Expression Purif. , vol.22 , pp. 220-224
    • Patel, C.N.1    Lind, M.C.2    Pielak, G.J.3
  • 43
    • 0032574759 scopus 로고    scopus 로고
    • Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in yeast iso -1 cytochrome c and the alkaline conformational transition
    • Pollock, W. B. R., Rosell, F. I., Twitchett, M. B., Dumont, M. E., and Mauk, A. G. (1998) Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in yeast iso -1 cytochrome c and the alkaline conformational transition Biochemistry 37, 6124-6131
    • (1998) Biochemistry , vol.37 , pp. 6124-6131
    • Pollock, W.B.R.1    Rosell, F.I.2    Twitchett, M.B.3    Dumont, M.E.4    Mauk, A.G.5
  • 44
    • 10044269982 scopus 로고    scopus 로고
    • Many faces of the unfolded state: Conformational heterogeneity in denatured yeast cytochrome c
    • Pletneva, E. V., Gray, H. B., and Winkler, J. R. (2005) Many faces of the unfolded state: Conformational heterogeneity in denatured yeast cytochrome c J. Mol. Biol. 345, 855-867
    • (2005) J. Mol. Biol. , vol.345 , pp. 855-867
    • Pletneva, E.V.1    Gray, H.B.2    Winkler, J.R.3
  • 45
    • 0037180383 scopus 로고    scopus 로고
    • Recombinant equine cytochrome c in Escherichia coli: High-level expression, characterization, and folding and assembly mutants
    • Rumbley, J. N., Hoang, L., and Englander, S. W. (2002) Recombinant equine cytochrome c in Escherichia coli: High-level expression, characterization, and folding and assembly mutants Biochemistry 41, 13894-13901
    • (2002) Biochemistry , vol.41 , pp. 13894-13901
    • Rumbley, J.N.1    Hoang, L.2    Englander, S.W.3
  • 46
  • 47
    • 0022760446 scopus 로고
    • Hemes and hemoproteins. 1: Preparation and analysis of the heme-containing octapeptide (microperoxidase-8) and identification of the monomeric form in aqueous solution
    • Aron, J., Baldwin, D. A., Marques, H. M., Pratt, J. M., and Adams, P. A. (1986) Hemes and hemoproteins. 1: Preparation and analysis of the heme-containing octapeptide (microperoxidase-8) and identification of the monomeric form in aqueous solution J. Inorg. Biochem. 27, 227-243
    • (1986) J. Inorg. Biochem. , vol.27 , pp. 227-243
    • Aron, J.1    Baldwin, D.A.2    Marques, H.M.3    Pratt, J.M.4    Adams, P.A.5
  • 48
    • 0013818184 scopus 로고
    • 2, and ferrocytochrome c and enzymic determination of extinction coefficients of cytochrome c
    • 2, and ferrocytochrome c and enzymic determination of extinction coefficients of cytochrome c J. Biol. Chem. 240, 4509-4514
    • (1965) J. Biol. Chem. , vol.240 , pp. 4509-4514
    • Yonetani, T.1
  • 49
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes- a, hemes- b, and hemes- c from pyridine hemochrome spectra
    • Berry, E. A. and Trumpower, B. L. (1987) Simultaneous determination of hemes- a, hemes- b, and hemes- c from pyridine hemochrome spectra Anal. Biochem. 161, 1-15
    • (1987) Anal. Biochem. , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 50
    • 0348117567 scopus 로고    scopus 로고
    • Infrared and Raman spectroscopical studies of salicylic and salicylate derivatives in aqueous solution
    • Humbert, B. (1998) Infrared and Raman spectroscopical studies of salicylic and salicylate derivatives in aqueous solution Spectrochim. Acta, Part A 54, 465-476
    • (1998) Spectrochim. Acta, Part A , vol.54 , pp. 465-476
    • Humbert, B.1
  • 51
    • 84981779372 scopus 로고
    • Zwischenmolekulare Energiewanderung und Fluoreszenz
    • Förster, T. (1948) Zwischenmolekulare Energiewanderung und Fluoreszenz Ann. Phys. (Weinheim, Ger.) 2, 55-75
    • (1948) Ann. Phys. (Weinheim, Ger.) , vol.2 , pp. 55-75
    • Förster, T.1
  • 52
    • 33748278190 scopus 로고    scopus 로고
    • Spectroscopic measurement of the redox potential of cytochrome c for the undergraduate biochemistry laboratory
    • Craig, D. B. and Nichols, E. R. (2006) Spectroscopic measurement of the redox potential of cytochrome c for the undergraduate biochemistry laboratory J. Chem. Educ. 83, 1325
    • (2006) J. Chem. Educ. , vol.83 , pp. 1325
    • Craig, D.B.1    Nichols, E.R.2
  • 54
    • 0023369081 scopus 로고
    • Hemes hemoproteins. 5: Kinetics of the peroxidatic activity of microperoxidase-8: Model for the peroxidase enzymes.
    • Baldwin, D. A., Helder, M. M., and Pratt, J. M. (1987) Hemes hemoproteins. 5: Kinetics of the peroxidatic activity of microperoxidase-8: model for the peroxidase enzymes. J. Inorg. Biochem. 30, 203-217
    • (1987) J. Inorg. Biochem. , vol.30 , pp. 203-217
    • Baldwin, D.A.1    Helder, M.M.2    Pratt, J.M.3
  • 56
    • 0015438810 scopus 로고
    • The preparation of guanidine hydrochloride
    • Nozaki, Y. (1972) The preparation of guanidine hydrochloride Methods Enzymol. 26, 43-50
    • (1972) Methods Enzymol. , vol.26 , pp. 43-50
    • Nozaki, Y.1
  • 57
    • 0002343673 scopus 로고
    • Measuring the Conformational Stability of a Protein
    • In (Creighton, T. F. Ed.) pp, IRL Press, Oxford, U.K.
    • Pace, N. C., Shirley, B. A., and Thomson, J. A. (1990) Measuring the Conformational Stability of a Protein. In Protein Structure: A Practical Approach (Creighton, T. F., Ed.) pp 311-330, IRL Press, Oxford, U.K.
    • (1990) Protein Structure: A Practical Approach , pp. 311-330
    • Pace, N.C.1    Shirley, B.A.2    Thomson, J.A.3
  • 58
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • Petersen, T. N., Brunak, S., von Heijne, G., and Nielsen, H. (2011) SignalP 4.0: Discriminating signal peptides from transmembrane regions Nat. Methods 8, 785-786
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 59
    • 0030816577 scopus 로고    scopus 로고
    • Identification of the predominant non-native histidine ligand in unfolded cytochrome c
    • Colón, W., Wakem, L. P., Sherman, F., and Roder, H. (1997) Identification of the predominant non-native histidine ligand in unfolded cytochrome c Biochemistry 36, 12535-12541
    • (1997) Biochemistry , vol.36 , pp. 12535-12541
    • Colón, W.1    Wakem, L.P.2    Sherman, F.3    Roder, H.4
  • 60
    • 79953792306 scopus 로고    scopus 로고
    • Comparing substrate specificity between cytochrome c maturation and cytochrome c heme lyase systems for cytochrome c biogenesis
    • Kleingardner, J. G. and Bren, K. L. (2011) Comparing substrate specificity between cytochrome c maturation and cytochrome c heme lyase systems for cytochrome c biogenesis Metallomics 3, 396-403
    • (2011) Metallomics , vol.3 , pp. 396-403
    • Kleingardner, J.G.1    Bren, K.L.2
  • 62
    • 0020407525 scopus 로고
    • Bile pigment-protein interactions. Coupled oxidation of cytochrome c
    • Lagarias, J. C. (1982) Bile pigment-protein interactions. Coupled oxidation of cytochrome c Biochemistry 21, 5962-5967
    • (1982) Biochemistry , vol.21 , pp. 5962-5967
    • Lagarias, J.C.1
  • 63
    • 0242353383 scopus 로고    scopus 로고
    • Kinetic stability of the peroxidase activity of unfolded cytochrome c: Heme degradation and catalyst inactivation by hydrogen peroxide
    • Diederix, R. E., Fittipaldi, M., Worrall, J. A., Huber, M., Ubbink, M., and Canters, G. W. (2003) Kinetic stability of the peroxidase activity of unfolded cytochrome c: Heme degradation and catalyst inactivation by hydrogen peroxide Inorg. Chem. 42, 7249-7257
    • (2003) Inorg. Chem. , vol.42 , pp. 7249-7257
    • Diederix, R.E.1    Fittipaldi, M.2    Worrall, J.A.3    Huber, M.4    Ubbink, M.5    Canters, G.W.6
  • 64
    • 0029884694 scopus 로고    scopus 로고
    • GOR method for predicting protein secondary structure from amino acid sequence
    • Garnier, J., Gibrat, J. F., and Robson, B. (1996) GOR method for predicting protein secondary structure from amino acid sequence Methods Enzymol. 266, 540-553
    • (1996) Methods Enzymol. , vol.266 , pp. 540-553
    • Garnier, J.1    Gibrat, J.F.2    Robson, B.3
  • 66
    • 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
  • 67
    • 0000161385 scopus 로고
    • Surface-enhanced resonance Raman spectroscopy of cytochrome c at room and low temperatures
    • Hildebrandt, P. and Stockburger, M. (1986) Surface-enhanced resonance Raman spectroscopy of cytochrome c at room and low temperatures J. Phys. Chem. 90, 6017-6024
    • (1986) J. Phys. Chem. , vol.90 , pp. 6017-6024
    • Hildebrandt, P.1    Stockburger, M.2
  • 68
    • 0016400375 scopus 로고
    • Resonance Raman spectra of heme proteins. Effects of oxidation and spin state
    • Spiro, T. G. and Strekas, T. C. (1974) Resonance Raman spectra of heme proteins. Effects of oxidation and spin state J. Am. Chem. Soc. 96, 338-345
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 338-345
    • Spiro, T.G.1    Strekas, T.C.2
  • 70
    • 0025226189 scopus 로고
    • Changing the invariant proline-30 of rat and Drosophila melanogaster cytochromes c to alanine or valine destabilizes the heme crevice more than the overall conformation
    • Koshy, T. I., Luntz, T. L., Schejter, A., and Margoliash, E. (1990) Changing the invariant proline-30 of rat and Drosophila melanogaster cytochromes c to alanine or valine destabilizes the heme crevice more than the overall conformation Proc. Natl. Acad. Sci. U.S.A. 87, 8697-8701
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 8697-8701
    • Koshy, T.I.1    Luntz, T.L.2    Schejter, A.3    Margoliash, E.4
  • 72
    • 0037195257 scopus 로고    scopus 로고
    • Peroxidase activity as a tool for studying the folding of c -type cytochromes
    • Diederix, R. E., Ubbink, M., and Canters, G. W. (2002) Peroxidase activity as a tool for studying the folding of c -type cytochromes Biochemistry 41, 13067-13077
    • (2002) Biochemistry , vol.41 , pp. 13067-13077
    • Diederix, R.E.1    Ubbink, M.2    Canters, G.W.3
  • 73
    • 0030800574 scopus 로고    scopus 로고
    • Protein engineering using molecular assembly: Functional conversion of cytochrome c via noncovalent interactions
    • Hamachi, I., Fujita, A., and Kunitake, T. (1997) Protein engineering using molecular assembly: Functional conversion of cytochrome c via noncovalent interactions J. Am. Chem. Soc. 119, 9096-9102
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 9096-9102
    • Hamachi, I.1    Fujita, A.2    Kunitake, T.3
  • 74
    • 68149136523 scopus 로고    scopus 로고
    • Tyrosine-67 in cytochrome c is a possible apoptotic trigger controlled by hydrogen bonds via a conformational transition
    • Ying, T., Wang, Z. H., Lin, Y. W., Xie, J., Tan, X., and Huang, Z. X. (2009) Tyrosine-67 in cytochrome c is a possible apoptotic trigger controlled by hydrogen bonds via a conformational transition Chem. Commun. 4512-4514
    • (2009) Chem. Commun. , pp. 4512-4514
    • Ying, T.1    Wang, Z.H.2    Lin, Y.W.3    Xie, J.4    Tan, X.5    Huang, Z.X.6
  • 75
    • 0037465522 scopus 로고    scopus 로고
    • Effect of pH on the iso-1 cytochrome c denatured state: Changing constraints due to heme ligation
    • Smith, C. R., Wandschneider, E., and Bowler, B. E. (2003) Effect of pH on the iso-1 cytochrome c denatured state: Changing constraints due to heme ligation Biochemistry 42, 2174-2184
    • (2003) Biochemistry , vol.42 , pp. 2174-2184
    • Smith, C.R.1    Wandschneider, E.2    Bowler, B.E.3
  • 78
    • 0038645365 scopus 로고    scopus 로고
    • The role of mitochondria in the life of the nematode, Caenorhabditis elegans
    • Tsang, W. Y. and Lemire, B. D. (2003) The role of mitochondria in the life of the nematode, Caenorhabditis elegans Biochim. Biophys. Acta 1638, 91-105
    • (2003) Biochim. Biophys. Acta , vol.1638 , pp. 91-105
    • Tsang, W.Y.1    Lemire, B.D.2
  • 79
    • 0019332553 scopus 로고
    • Comparison of the binding sites on cytochrome c for cytochrome c oxidase, cytochrome bc 1, and cytochrome c 1
    • Reider, R. and Bosshard, H. (1980) Comparison of the binding sites on cytochrome c for cytochrome c oxidase, cytochrome bc 1, and cytochrome c 1 J. Biol. Chem. 255, 4732-4739
    • (1980) J. Biol. Chem. , vol.255 , pp. 4732-4739
    • Reider, R.1    Bosshard, H.2
  • 80
    • 0032488914 scopus 로고    scopus 로고
    • Cytochrome c folding traps are not due solely to histidine-heme ligation: Direct demonstration of a role for N-terminal amino group-heme ligation
    • Hammack, B. N., Godbole, S., and Bowler, B. E. (1998) Cytochrome c folding traps are not due solely to histidine-heme ligation: Direct demonstration of a role for N-terminal amino group-heme ligation J. Mol. Biol. 275, 719-724
    • (1998) J. Mol. Biol. , vol.275 , pp. 719-724
    • Hammack, B.N.1    Godbole, S.2    Bowler, B.E.3
  • 81
    • 0028950245 scopus 로고
    • Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome c
    • Lo, T. P., Murphy, M. E. P., Guillemette, J. G., Smith, M., and Brayer, G. D. (1995) Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome c Protein Sci. 4, 198-208
    • (1995) Protein Sci. , vol.4 , pp. 198-208
    • Lo, T.P.1    Murphy, M.E.P.2    Guillemette, J.G.3    Smith, M.4    Brayer, G.D.5
  • 82
    • 0028057721 scopus 로고
    • Evidence for two distinct acidic phospholipid-binding sites in cytochrome c
    • Rytömaa, M. and Kinnunen, P. K. (1994) Evidence for two distinct acidic phospholipid-binding sites in cytochrome c J. Biol. Chem. 269, 1770-1774
    • (1994) J. Biol. Chem. , vol.269 , pp. 1770-1774
    • Rytömaa, M.1    Kinnunen, P.K.2
  • 83
    • 0039178090 scopus 로고    scopus 로고
    • Membrane location of spin-labeled cytochrome c determined by paramagnetic relaxation agents
    • Kostrzewa, A., Pali, T., Froncisz, W., and Marsh, D. (2000) Membrane location of spin-labeled cytochrome c determined by paramagnetic relaxation agents Biochemistry 39, 6066-6074
    • (2000) Biochemistry , vol.39 , pp. 6066-6074
    • Kostrzewa, A.1    Pali, T.2    Froncisz, W.3    Marsh, D.4
  • 84
    • 30444448684 scopus 로고    scopus 로고
    • The two Drosophila cytochrome c proteins can function in both respiration and caspase activation
    • Arama, E., Bader, M., Srivastava, M., Bergmann, A., and Steller, H. (2006) The two Drosophila cytochrome c proteins can function in both respiration and caspase activation EMBO J. 25, 232-243
    • (2006) EMBO J. , vol.25 , pp. 232-243
    • Arama, E.1    Bader, M.2    Srivastava, M.3    Bergmann, A.4    Steller, H.5
  • 85
    • 0017394346 scopus 로고
    • Cytochrome c: Immunofluorescent localization of the testis-specific form
    • Goldberg, E., Sberna, D., Wheat, T. E., Urbanski, G. J., and Margoliash, E. (1977) Cytochrome c: Immunofluorescent localization of the testis-specific form Science 196, 1010-1012
    • (1977) Science , vol.196 , pp. 1010-1012
    • Goldberg, E.1    Sberna, D.2    Wheat, T.E.3    Urbanski, G.J.4    Margoliash, E.5
  • 86
    • 33745119432 scopus 로고    scopus 로고
    • Remarkably high activities of testicular cytochrome c in destroying reactive oxygen species and in triggering apoptosis
    • Liu, Z., Lin, H., Ye, S., Liu, Q. Y., Meng, Z., Zhang, C. M., Xia, Y., Margoliash, E., Rao, Z., and Liu, X. J. (2006) Remarkably high activities of testicular cytochrome c in destroying reactive oxygen species and in triggering apoptosis Proc. Natl. Acad. Sci. U.S.A. 103, 8965-8970
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 8965-8970
    • Liu, Z.1    Lin, H.2    Ye, S.3    Liu, Q.Y.4    Meng, Z.5    Zhang, C.M.6    Xia, Y.7    Margoliash, E.8    Rao, Z.9    Liu, X.J.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.