메뉴 건너뛰기




Volumn 256, Issue 1, 1996, Pages 172-186

Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c

Author keywords

Cytochrome c; Heme; Molten globule; Porphyrin cytochrome c; Protein folding

Indexed keywords

ANION; CYTOCHROME C; HEME; IRON;

EID: 0029863253     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0075     Document Type: Article
Times cited : (86)

References (55)
  • 1
    • 0025822867 scopus 로고
    • Solvent denaturation and stabilization of globular proteins
    • Alonso, D. O. V. & Dill, K. A. (1991). Solvent denaturation and stabilization of globular proteins. Biochemistry, 30, 5974-5985.
    • (1991) Biochemistry , vol.30 , pp. 5974-5985
    • Alonso, D.O.V.1    Dill, K.A.2
  • 3
    • 0027254057 scopus 로고
    • The molten globule intermediate of apomyoglobin and the process of protein folding
    • Barrick, D. & Baldwin, R. L. (1993). The molten globule intermediate of apomyoglobin and the process of protein folding. Protein Sci. 2, 869-876.
    • (1993) Protein Sci. , vol.2 , pp. 869-876
    • Barrick, D.1    Baldwin, R.L.2
  • 4
    • 0025007598 scopus 로고
    • High-resolution three-dimensional structure of horse heart cytochrome c
    • Bushnell, G. W., Louie, G. V. & Brayer, G. D. (1990). High-resolution three-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
  • 5
    • 84945799762 scopus 로고
    • Fluorescence quantum yield of tryptophan and tyrosine
    • Chen, R. F. (1967). Fluorescence quantum yield of tryptophan and tyrosine. Anal. Letters, 13, 35-42.
    • (1967) Anal. Letters , vol.13 , pp. 35-42
    • Chen, R.F.1
  • 7
    • 0025732606 scopus 로고
    • Acid denatured apo-cytochrome 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. (1991b). Acid denatured apo-cytochrome c is a random coil: evidence from small-angle X-ray scattering and dynamic light scattering. Biochim. Biophys. Acta, 1078, 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
  • 8
    • 0027155642 scopus 로고
    • Redesign of the interior hydrophilic region of mitochondrial cytochrome c by site-directed mutagenesis
    • Davies, A. M., Guillemette, J. G., Smith, M., Greenwood, C., Thurgood, A. G. P., Mauk, A. G. & Moore, G. R. (1993). Redesign of the interior hydrophilic region of mitochondrial cytochrome c by site-directed mutagenesis. Biochemistry, 32, 5431-5435.
    • (1993) Biochemistry , vol.32 , pp. 5431-5435
    • Davies, A.M.1    Guillemette, J.G.2    Smith, M.3    Greenwood, C.4    Thurgood, A.G.P.5    Mauk, A.G.6    Moore, G.R.7
  • 9
    • 0020478683 scopus 로고
    • Spin state and unfolding equilibria of ferricytochrome c in acidic solutions
    • Dyson, H. J. & Beattie, J. K. (1982). Spin state and unfolding equilibria of ferricytochrome c in acidic solutions. J. Biol. Chem. 257, 2267-2273.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2267-2273
    • Dyson, H.J.1    Beattie, J.K.2
  • 10
    • 0028352044 scopus 로고
    • Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands
    • Elöve, G. A., Bhuyan, A. K. & Roder, H. (1994). Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands. Biochemistry, 33, 6925-6935.
    • (1994) Biochemistry , vol.33 , pp. 6925-6935
    • Elöve, G.A.1    Bhuyan, A.K.2    Roder, H.3
  • 11
    • 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. (1973). On the role of heme in the formation of the structure of cytochrome c. J. Biol. Chem. 248, 3188-3195.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3188-3195
    • Fisher, W.R.1    Taniuchi, H.2    Anfinsen, C.B.3
  • 12
    • 0002413436 scopus 로고
    • Delocalized excitation and excitation transfer
    • Sinanoglu, O., ed., Academic Press, New York, US
    • Förster, T. H. (1965). Delocalized excitation and excitation transfer. In Modern Quantum Chemistry (Sinanoglu, O., ed.), pp. 93-137, Academic Press, New York, US.
    • (1965) Modern Quantum Chemistry , pp. 93-137
    • Förster, T.H.1
  • 13
    • 0028786234 scopus 로고
    • A method of directed random mutagenesis of the yeast chromosome shows that the iso-1-cytochrome c heme ligand His18 is essential
    • Fumo, G., Spitzer, J. S. & Fetrow, J. S. (1995). A method of directed random mutagenesis of the yeast chromosome shows that the iso-1-cytochrome c heme ligand His18 is essential. Gene, 164, 33-39.
    • (1995) Gene , vol.164 , pp. 33-39
    • Fumo, G.1    Spitzer, J.S.2    Fetrow, J.S.3
  • 15
    • 0028290594 scopus 로고
    • Acid-induced folding of heme proteins
    • Goto, Y. & Fink, A. L. (1994). Acid-induced folding of heme proteins. Methods Enzymol. 232, 3-15.
    • (1994) Methods Enzymol. , vol.232 , pp. 3-15
    • Goto, Y.1    Fink, A.L.2
  • 16
    • 0026351184 scopus 로고
    • Role of electrostatic repulsion in the acidic molten globule of cytochrome c
    • Goto Y. & Nishikiori, S. (1991). Role of electrostatic repulsion in the acidic molten globule of cytochrome c. J. Mol. Biol. 222, 679-686.
    • (1991) J. Mol. Biol. , vol.222 , pp. 679-686
    • Goto, Y.1    Nishikiori, S.2
  • 18
    • 0025195499 scopus 로고
    • Mechanism of acid-induced folding of proteins
    • Goto, Y., Takahashi, N. & Fink, A. L. (1990b). 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
  • 20
    • 0028346251 scopus 로고
    • Comparison of the conformational stability of the molten globule and native states of horse cytochrome c
    • Hagihara, Y., Tan, Y. & Goto, Y. (1994). Comparison of the conformational stability of the molten globule and native states of horse cytochrome c. J. Mol. Biol. 237, 336-348.
    • (1994) J. Mol. Biol. , vol.237 , pp. 336-348
    • Hagihara, Y.1    Tan, Y.2    Goto, Y.3
  • 21
    • 0027433511 scopus 로고
    • Intermediate conformational states of apocytochrome c
    • Hamada, D., Hoshino, M., Kataoka, M., Fink, A. L. & Goto, Y. (1993). Intermediate conformational states of apocytochrome c. Biochemistry, 32, 10351-10358.
    • (1993) Biochemistry , vol.32 , pp. 10351-10358
    • Hamada, D.1    Hoshino, M.2    Kataoka, M.3    Fink, A.L.4    Goto, Y.5
  • 22
    • 0028143596 scopus 로고
    • Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry
    • Hamada, D., Kidokoro, S., Fukada, H., Takahashi, K. & Goto, Y. (1994). Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry. Proc. Natl Acad. Sci. USA, 91, 10325-10329.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10325-10329
    • Hamada, D.1    Kidokoro, S.2    Fukada, H.3    Takahashi, K.4    Goto, Y.5
  • 23
    • 0023010358 scopus 로고
    • Amino acid replacements in yeast iso-1-cytochrome c
    • Hampsey, D. M., Das, G. & Sherman, F. (1986). Amino acid replacements in yeast iso-1-cytochrome c. J. Biol. Chem. 261, 3259-3271.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3259-3271
    • Hampsey, D.M.1    Das, G.2    Sherman, F.3
  • 25
    • 0018787274 scopus 로고
    • Kinetic studies on the effect of the heme iron(III) on the protein folding of ferricytochrome c
    • Henkens, R. W. & Turner, S. R. (1979). Kinetic studies on the effect of the heme iron(III) on the protein folding of ferricytochrome c. J. Biol. Chem. 254, 8110-8112.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8110-8112
    • Henkens, R.W.1    Turner, S.R.2
  • 26
    • 0023184951 scopus 로고
    • The spontaneous incorporation of proteins into preformed bilayers
    • Jain, M. K. & Zakim, D. (1987). The spontaneous incorporation of proteins into preformed bilayers. Biochem. Biophys. Acta. 906, 33-68.
    • (1987) Biochem. Biophys. Acta. , vol.906 , pp. 33-68
    • Jain, M.K.1    Zakim, D.2
  • 27
    • 0025203243 scopus 로고
    • Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D-NMR
    • Jeng, M.-F., Englander, S. W., Elöve, G. A., Wand, A. J. & Roder, H. (1990). Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D-NMR. Biochemistry, 29, 10433-10437.
    • (1990) Biochemistry , vol.29 , pp. 10433-10437
    • Jeng, M.-F.1    Englander, S.W.2    Elöve, G.A.3    Wand, A.J.4    Roder, H.5
  • 28
    • 0024600228 scopus 로고
    • The importance of the amino terminus of the mitochondrial precoursor protein apocytochrome c for translocation across model membranes
    • Jordi, W., Li-Xin, Z., Pilon, M., Demel, R. A. & de Kruijff, B. (1989). The importance of the amino terminus of the mitochondrial precoursor protein apocytochrome c for translocation across model membranes. J. Biol. Chem. 264, 2292-2301.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2292-2301
    • Jordi, W.1    Li-Xin, Z.2    Pilon, M.3    Demel, R.A.4    De Kruijff, B.5
  • 30
    • 0027400842 scopus 로고
    • Molten globule of cytochrome c studied by the small angle X-ray scattering
    • Kataoka, M., Hagihara, Y., Mihara, K. & Goto, Y. (1993). Molten globule of cytochrome c studied by the small angle X-ray scattering. J. Mol. Biol. 229, 591-596.
    • (1993) J. Mol. Biol. , vol.229 , pp. 591-596
    • Kataoka, M.1    Hagihara, Y.2    Mihara, K.3    Goto, Y.4
  • 31
    • 0029032691 scopus 로고
    • Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering
    • Kataoka, M., Nishii, I., Fujisawa, T., Ueki, T., Tokunaga, F. & Goto, Y. (1995). Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering. J. Mol. Biol. 249, 215-228.
    • (1995) J. Mol. Biol. , vol.249 , pp. 215-228
    • Kataoka, M.1    Nishii, I.2    Fujisawa, T.3    Ueki, T.4    Tokunaga, F.5    Goto, Y.6
  • 32
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 33
    • 0027523179 scopus 로고
    • Residual helical structure in the C-terminal fragment of cytochrome c
    • Kuroda, Y. (1993). Residual helical structure in the C-terminal fragment of cytochrome c. Biochemistry, 32, 1219-1224.
    • (1993) Biochemistry , vol.32 , pp. 1219-1224
    • Kuroda, Y.1
  • 34
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima, K. (1989). The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins: Struct. Funct. Genet. 6, 87-103.
    • (1989) Proteins: Struct. Funct. Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 35
    • 0027142050 scopus 로고
    • Structurally engineered cytochromes with unusual ligand-binding properties: Expression of Saccharomyces cerevisiae Met80 → Ala iso-1-cytochrome c
    • Lu, Y, Casimiro, D. R., Bren, K. L, Richards, J. H. & Gray, H. B. (1993). Structurally engineered cytochromes with unusual ligand-binding properties: expression of Saccharomyces cerevisiae Met80 → Ala iso-1-cytochrome c. Proc. Natl Acad. Sci. USA, 90, 11456-11459.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11456-11459
    • Lu, Y.1    Casimiro, D.R.2    Bren, K.L.3    Richards, J.H.4    Gray, H.B.5
  • 36
    • 0028926855 scopus 로고
    • A native tertiary interaction stabilizes the a state of cytochrome c
    • Marmorino, J. L. & Pielak, G. J. (1995). A native tertiary interaction stabilizes the A state of cytochrome c. Biochemistry, 34, 3140-3143.
    • (1995) Biochemistry , vol.34 , pp. 3140-3143
    • Marmorino, J.L.1    Pielak, G.J.2
  • 37
    • 0025877054 scopus 로고
    • Apocytochrome c interaction with phopholipid membranes studied by Fourier-transform infrared spectroscopy
    • Muga, A., Mantsch, H. H. & Surewicz, W. K. (1991). Apocytochrome c interaction with phopholipid membranes studied by Fourier-transform infrared spectroscopy Biochemistry, 30, 2629-2635.
    • (1991) Biochemistry , vol.30 , pp. 2629-2635
    • Muga, A.1    Mantsch, H.H.2    Surewicz, W.K.3
  • 38
    • 0025832142 scopus 로고
    • Effective concentrations of amino acid side-chains in an unfolded protein
    • Muthukrishnan, K. & Nail, B. T. (1991). Effective concentrations of amino acid side-chains in an unfolded protein. Biochemistry, 30, 4706-4710.
    • (1991) Biochemistry , vol.30 , pp. 4706-4710
    • Muthukrishnan, K.1    Nail, B.T.2
  • 39
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J. K., Pace, C. N. & Scholtz, J. M. (1995). Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4, 2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 40
    • 0028243107 scopus 로고
    • Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding
    • Nishii, I., Kataoka, M., Tokunaga, F. & Goto, Y. (1994). Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding. Biochemistry, 33, 4903-4909.
    • (1994) Biochemistry , vol.33 , pp. 4903-4909
    • Nishii, I.1    Kataoka, M.2    Tokunaga, F.3    Goto, Y.4
  • 41
    • 0021114569 scopus 로고
    • "Molten-globule state": A compact form of globular proteins with mobile side-chains
    • Ohgushi, M. & Wada, A. (1983). "Molten-globule state": a compact form of globular proteins with mobile side-chains. FEBS Letters, 164, 21-24.
    • (1983) FEBS Letters , vol.164 , pp. 21-24
    • Ohgushi, M.1    Wada, A.2
  • 42
    • 0027171026 scopus 로고
    • Leucine/isoleucine/valine binding protein contracts upon binding of ligand
    • Olah, G. A., Trakhanov, S., Trewhella, J. & Quiocho, F. A. (1993). Leucine/isoleucine/valine binding protein contracts upon binding of ligand. J. Biol. Chem. 268, 16241-16247.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16241-16247
    • Olah, G.A.1    Trakhanov, S.2    Trewhella, J.3    Quiocho, F.A.4
  • 43
    • 0002940127 scopus 로고
    • The molten globule state
    • Creighton, T. E., ed., W. H. Freeman and Company New York, US
    • Ptitsyn, O. B. (1992). The molten globule state. In Protein Folding (Creighton, T. E., ed.), pp. 243-300, W. H. Freeman and Company New York, US.
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.B.1
  • 44
    • 0029160445 scopus 로고
    • How the molten globule became
    • Ptitsyn, O. B. (1995). How the molten globule became. Trends Biochem. Sci. 237, 376-379.
    • (1995) Trends Biochem. Sci. , vol.237 , pp. 376-379
    • Ptitsyn, O.B.1
  • 45
  • 46
    • 0002775727 scopus 로고
    • Early stages of protein folding
    • Pain, R. H., ed., Oxford University Press, New York
    • Roder, H. & Elöve, G. A. (1994). Early stages of protein folding. In Mechanisms of Protein Folding (Pain, R. H., ed.), pp. 26-54, Oxford University Press, New York.
    • (1994) Mechanisms of Protein Folding , pp. 26-54
    • Roder, H.1    Elöve, G.A.2
  • 47
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR
    • Roder, H., Elöve, G. A. & Englander, S. W. (1988). Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR. Nature, 335, 700-704.
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elöve, G.A.2    Englander, S.W.3
  • 48
    • 0017802519 scopus 로고
    • Solvent denaturation
    • Schellman, J. A. (1978). Solvent denaturation. Biopolymers, 17, 1305-1322.
    • (1978) Biopolymers , vol.17 , pp. 1305-1322
    • Schellman, J.A.1
  • 49
    • 0024534401 scopus 로고
    • A novel, functional variant of cytochrome c: Replacement of the histidine ligand with arginine via site-directed mutagenesis
    • Sorrell, T., Martin, P. K. & Bowden, E. F. (1989). A novel, functional variant of cytochrome c: replacement of the histidine ligand with arginine via site-directed mutagenesis. J. Am. Chem. Soc. 111, 766-767.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 766-767
    • Sorrell, T.1    Martin, P.K.2    Bowden, E.F.3
  • 51
    • 0016717998 scopus 로고
    • Stabilization of the globular structure of ferricytochrome c by chloride in acidic solvents
    • Stellwagen, E. & Babul, J. (1975). Stabilization of the globular structure of ferricytochrome c by chloride in acidic solvents. Biochemistry, 14, 5135-5140.
    • (1975) Biochemistry , vol.14 , pp. 5135-5140
    • Stellwagen, E.1    Babul, J.2
  • 52
    • 0015524145 scopus 로고
    • The conformation of horse heart apocytochrome c
    • Stellwagen, E., Rysavy, R. J. & Babul, G. (1972). The conformation of horse heart apocytochrome c. J. Biol. Chem. 274, 8074-8077.
    • (1972) J. Biol. Chem. , vol.274 , pp. 8074-8077
    • Stellwagen, E.1    Rysavy, R.J.2    Babul, G.3
  • 53
    • 0026674590 scopus 로고
    • Functional role of heme ligation in cytochrome c
    • Wallace, C. J. A. & Clark-Lewis, I. (1992). Functional role of heme ligation in cytochrome c. J. Biol. Chem. 267, 3852-3861.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3852-3861
    • Wallace, C.J.A.1    Clark-Lewis, I.2
  • 54
    • 0027442944 scopus 로고
    • A noncovalent 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. (1993). A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c. Biochemistry, 32, 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
  • 55
    • 0026715788 scopus 로고
    • Fusion of phospholipid vesicles induced by an amphiphilic model peptide: Close correlation between fusogenicity and hydrophobicity of the peptide in an α-helix
    • Yoshimura, T., Goto, Y. & Aimoto, S. (1992). Fusion of phospholipid vesicles induced by an amphiphilic model peptide: close correlation between fusogenicity and hydrophobicity of the peptide in an α-helix. Biochemistry, 31, 6119-6126.
    • (1992) Biochemistry , vol.31 , pp. 6119-6126
    • Yoshimura, T.1    Goto, Y.2    Aimoto, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.