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Volumn 285, Issue 2, 1999, Pages 463-468

Structural organization in peptide fragments of cytochrome c by heme binding

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; HEME; LYASE; PEPTIDE FRAGMENT; SULFIDE;

EID: 0033555241     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2341     Document Type: Article
Times cited : (11)

References (33)
  • 1
    • 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
  • 2
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai Y., Sosnick T. R., Mayne L., Englander S. W. Protein folding intermediates: native-state hydrogen exchange. Science. 269:1995;192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 3
    • 0029129996 scopus 로고
    • Control of the redox potential in c -type cytochromes: Importance of the entropic contribution
    • Bertrand P., Mbarki O., Asso M., Blanchard L., Guerlesquin F., Tegoni M. Control of the redox potential in c -type cytochromes: importance of the entropic contribution. Biochemistry. 34:1995;11071-11079.
    • (1995) Biochemistry , vol.34 , pp. 11071-11079
    • Bertrand, P.1    Mbarki, O.2    Asso, M.3    Blanchard, L.4    Guerlesquin, F.5    Tegoni, M.6
  • 4
    • 0025007598 scopus 로고
    • High-resolution three-dimensional structure of horse heart
    • Bushnell G. W., Louie G. V., Brayer G. D. High-resolution three-dimensional structure of horse heart. 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
  • 5
    • 0025732606 scopus 로고
    • Acid denatured apo-ctychrome c is a random coil: Evidence from small-angle X-ray scattering and dynamic light scattering
    • Damaschun G., Damaschun H., Gast K., Gernat C., Zirwer D. Acid denatured apo-ctychrome c is a random coil: evidence from small-angle X-ray scattering and dynamic light scattering. Biochim. Biophys. Acta. 1078:1991;289-295.
    • (1991) Biochim. Biophys. Acta , vol.1078 , pp. 289-295
    • Damaschun, G.1    Damaschun, H.2    Gast, K.3    Gernat, C.4    Zirwer, D.5
  • 6
    • 0028244331 scopus 로고
    • Noncovalent binding of heme induces a compact apocytochrome c structure
    • Dumont M. E., Corin A. F., Campbell G. A. Noncovalent binding of heme induces a compact apocytochrome c structure. Biochemistry. 33:1994;7368-7378.
    • (1994) Biochemistry , vol.33 , pp. 7368-7378
    • Dumont, M.E.1    Corin, A.F.2    Campbell, G.A.3
  • 7
    • 0030575785 scopus 로고    scopus 로고
    • Is apomyoglobin a molten globule? Structural characterization by NMR
    • Eliezer D., Wright P. E. Is apomyoglobin a molten globule? Structural characterization by NMR. J. Mol. Biol. 263:1996;531-538.
    • (1996) J. Mol. Biol. , vol.263 , pp. 531-538
    • Eliezer, D.1    Wright, P.E.2
  • 8
    • 0026781019 scopus 로고
    • Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy
    • Elöve G. A., Chaffotte A. F., Roder H., Goldberg M. E. Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy. Biochemistry. 31:1992;6876-6883.
    • (1992) Biochemistry , vol.31 , pp. 6876-6883
    • Elöve, G.A.1    Chaffotte, A.F.2    Roder, H.3    Goldberg, M.E.4
  • 9
    • 0028352044 scopus 로고
    • Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands
    • Elöve G. A., Bhuyan A. K., Roder H. Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands. Biochemistry. 33:1994;6925-6935.
    • (1994) Biochemistry , vol.33 , pp. 6925-6935
    • Elöve, G.A.1    Bhuyan, A.K.2    Roder, H.3
  • 12
    • 0015919686 scopus 로고
    • On the role of heme in the formation of the structure of cytochrome c
    • Fisher W. R., Taniuchi H., Anfinsen C. B. On the role of heme in the formation of the structure of cytochrome c. J. Biol. Chem. 248:1973;3188-3195.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3188-3195
    • Fisher, W.R.1    Taniuchi, H.2    Anfinsen, C.B.3
  • 13
    • 0025633802 scopus 로고
    • Biogenesis of mitochondrial c -type cytochromes
    • Gonzales D. H., Neupert W. Biogenesis of mitochondrial c -type cytochromes. J. Bioenerget. Biomembr. 22:1990;753-768.
    • (1990) J. Bioenerget. Biomembr. , vol.22 , pp. 753-768
    • Gonzales, D.H.1    Neupert, W.2
  • 14
  • 15
    • 0029863253 scopus 로고    scopus 로고
    • Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochromec
    • Hamada D., Kuroda Y., Kataoka M., Aimoto S., Yoshimura T., Goto Y. Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochromec. J. Mol. Biol. 256:1996;172-186.
    • (1996) J. Mol. Biol. , vol.256 , pp. 172-186
    • Hamada, D.1    Kuroda, Y.2    Kataoka, M.3    Aimoto, S.4    Yoshimura, T.5    Goto, Y.6
  • 16
    • 0023677077 scopus 로고
    • Study of the specific heme orientation in reconstituted hemoglobins
    • Ishimori K., Morishima I. Study of the specific heme orientation in reconstituted hemoglobins. Biochemistry. 27:1988;4747-4753.
    • (1988) Biochemistry , vol.27 , pp. 4747-4753
    • Ishimori, K.1    Morishima, I.2
  • 17
    • 0019320701 scopus 로고
    • A biologically active, three-fragment complex of horse heart cytochrome c
    • Juillerat M., Parr G. R., Taniuchi H. A biologically active, three-fragment complex of horse heart cytochrome c. J. Biol. Chem. 255:1980;845-853.
    • (1980) J. Biol. Chem. , vol.255 , pp. 845-853
    • Juillerat, M.1    Parr, G.R.2    Taniuchi, H.3
  • 18
    • 0015928945 scopus 로고
    • A theoretical model for the effects of local nonpolar heme environment on the redox potentials in cytochromes
    • Kassner R. J. A theoretical model for the effects of local nonpolar heme environment on the redox potentials in cytochromes. J. Am. Chem. Soc. 95:1973;2674-2677.
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 2674-2677
    • Kassner, R.J.1
  • 19
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 20
    • 0027523179 scopus 로고
    • Residual helical structure in the C-terminal fragment of cytochrome c
    • Kuroda Y. Residual helical structure in the C-terminal fragment of cytochrome c. Biochemistry. 32:1993;1219-1224.
    • (1993) Biochemistry , vol.32 , pp. 1219-1224
    • Kuroda, Y.1
  • 21
    • 0028988453 scopus 로고    scopus 로고
    • Stability of helices in a molten globule state of cytochrome c by hydrogen-deuterium exchange and two-dimensional NMR spectroscopy
    • Kuroda Y., Endo S., Nagayama K., Wada A. Stability of helices in a molten globule state of cytochrome c by hydrogen-deuterium exchange and two-dimensional NMR spectroscopy. J. Mol. Biol. 247:1996;682-688.
    • (1996) J. Mol. Biol. , vol.247 , pp. 682-688
    • Kuroda, Y.1    Endo, S.2    Nagayama, K.3    Wada, A.4
  • 22
    • 45149140617 scopus 로고
    • 1H n.m.r. study of equine heart apocytochrome c
    • 1H n.m.r. study of equine heart apocytochrome c. Biofizika. 35:1990;407-409.
    • (1990) Biofizika , vol.35 , pp. 407-409
    • Kutyshenko, V.P.1
  • 23
    • 0021112460 scopus 로고
    • Heme orientational disorder in reconstituted and native sperm whale myoglobin
    • La Mar G. N., Davis N. L., Parish D. W., Smith K. M. Heme orientational disorder in reconstituted and native sperm whale myoglobin. J. Mol. Biol. 168:1983;887-896.
    • (1983) J. Mol. Biol. , vol.168 , pp. 887-896
    • La Mar, G.N.1    Davis, N.L.2    Parish, D.W.3    Smith, K.M.4
  • 24
    • 0015222647 scopus 로고
    • The interpretation of protein structure: Estimation of static accessibility
    • Lee B., Richards F. M. The interpretation of protein structure: estimation of static accessibility. J. Mol. Biol. 55:1971;379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 27
    • 0017814312 scopus 로고
    • Formation of two alternative complementing structures from a cytochrome c heme fragment (residues 1 to 38) and the apoprotein
    • Parr G. R., Hantgan R. R., Taniuchi H. Formation of two alternative complementing structures from a cytochrome c heme fragment (residues 1 to 38) and the apoprotein. J. Biol. Chem. 253:1978;5381-5388.
    • (1978) J. Biol. Chem. , vol.253 , pp. 5381-5388
    • Parr, G.R.1    Hantgan, R.R.2    Taniuchi, H.3
  • 29
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR
    • Roder H., Elöve G. A., Englander S. W. Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. Nature. 225:1988;700-704.
    • (1988) Nature , vol.225 , pp. 700-704
    • Roder, H.1    Elöve, G.A.2    Englander, S.W.3
  • 30
    • 0018129356 scopus 로고
    • Haem exposure as the determinate of oxidation-reduction potential of haem proteins
    • Stellwagen E. Haem exposure as the determinate of oxidation-reduction potential of haem proteins. Nature. 275:1978;73-74.
    • (1978) Nature , vol.275 , pp. 73-74
    • Stellwagen, E.1
  • 31
    • 0015524145 scopus 로고
    • The conformation of horse heart apocytochrome c
    • Stellwagen E., Rysavy R., Babul G. The conformation of horse heart apocytochrome c. J. Biol. Chem. 247:1972;8074-8077.
    • (1972) J. Biol. Chem. , vol.247 , pp. 8074-8077
    • Stellwagen, E.1    Rysavy, R.2    Babul, G.3
  • 32
    • 0013800421 scopus 로고
    • The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites
    • Stryer L. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J. Mol. Biol. 13:1965;482-495.
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 33
    • 0027442944 scopus 로고
    • A noncovanlent peptide complex as a model for an early folding intermediate of cytochrome c
    • Wu L. C., Laub P. B., Elöve G. A., Carey J., Roder H. A noncovanlent peptide complex as a model for an early folding intermediate of cytochrome c. Biochemistry. 32:1993;10271-10276.
    • (1993) Biochemistry , vol.32 , pp. 10271-10276
    • Wu, L.C.1    Laub, P.B.2    Elöve, G.A.3    Carey, J.4    Roder, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.