메뉴 건너뛰기




Volumn 3, Issue 6, 1996, Pages 491-497

Cytochrome c folding triggered by electron transfer

Author keywords

Cytochrome c; Electron transfer; Protein folding

Indexed keywords

EQUUS CABALLUS;

EID: 0030154861     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(96)90097-6     Document Type: Article
Times cited : (152)

References (38)
  • 2
    • 0030046906 scopus 로고    scopus 로고
    • Fast events in protein folding: Helix melting and formation in a small peptide
    • Williams, S., et al., & Dyer, R.B. (1996). Fast events in protein folding: helix melting and formation in a small peptide. Biochemistry 35, 691-697.
    • (1996) Biochemistry , vol.35 , pp. 691-697
    • Williams, S.1    Dyer, R.B.2
  • 3
    • 0027131947 scopus 로고
    • Fast events in protein folding initiated by nanosecond laser photolysis
    • Jones, C.M., et al., & Eaton, W.A. (1993). Fast events in protein folding initiated by nanosecond laser photolysis. Proc. Natl. Acad. Sci. USA 90, 11860-11864.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11860-11864
    • Jones, C.M.1    Eaton, W.A.2
  • 4
    • 0030584652 scopus 로고    scopus 로고
    • Protein folding triggered by electron transfer
    • Pascher, T., Chesick, J.P., Winkler, J.R. & Gray, H.B. (1996). Protein folding triggered by electron transfer. Science 271, 1558-1560.
    • (1996) Science , vol.271 , pp. 1558-1560
    • Pascher, T.1    Chesick, J.P.2    Winkler, J.R.3    Gray, H.B.4
  • 7
    • 0028352044 scopus 로고
    • Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands
    • Elöve, G., 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.1    Bhuyan, A.K.2    Roder, H.3
  • 9
    • 2642646038 scopus 로고
    • Electrochemical probes of protein folding
    • Bixler, J., Bakker, G. & McLendon, G. (1992). Electrochemical probes of protein folding. J. Am. Chem. Soc. 114, 6938-6939.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6938-6939
    • Bixler, J.1    Bakker, G.2    McLendon, G.3
  • 10
    • 0023044641 scopus 로고
    • Control of the redox potential of cytochrome c and microscopic dielectric effects in proteins
    • Churg, A.K. & Warshel, A. (1986). Control of the redox potential of cytochrome c and microscopic dielectric effects in proteins. Biochemistry 25, 1675-1681.
    • (1986) Biochemistry , vol.25 , pp. 1675-1681
    • Churg, A.K.1    Warshel, A.2
  • 11
    • 0028960492 scopus 로고
    • How valid are denaturant-induced free energy measurements? Level of confidence to common assumptions over an extended range of ribonuclease A stability
    • Yao, M. & Bolen, D.W. (1995). How valid are denaturant-induced free energy measurements? Level of confidence to common assumptions over an extended range of ribonuclease A stability. Biochemistry 34, 3771-3781.
    • (1995) Biochemistry , vol.34 , pp. 3771-3781
    • Yao, M.1    Bolen, D.W.2
  • 12
    • 0029039960 scopus 로고
    • Stabilizing amino acid replacements at position 52 in yeast iso-1-cytochrome c: In vivo and in vitro effects
    • Linske-O'Connell, L.I., Sherman, F. & McLendon, G. (1995). Stabilizing amino acid replacements at position 52 in yeast iso-1-cytochrome c: in vivo and in vitro effects. Biochemistry 34, 7094-7102.
    • (1995) Biochemistry , vol.34 , pp. 7094-7102
    • Linske-O'Connell, L.I.1    Sherman, F.2    McLendon, G.3
  • 13
    • 0003409056 scopus 로고
    • Measuring the conformational stability of a protein
    • (Creighton, T.F., ed.), IRL Press, Oxford
    • Pace, N.C., Shirley, BA & Thomson, JA (1990). Measuring the conformational stability of a protein. In Protein Structure: A Practical Approach. (Creighton, T.F., ed.), pp. 311-330, IRL Press, Oxford.
    • (1990) Protein Structure: A Practical Approach , pp. 311-330
    • Pace, N.C.1    Shirley, B.A.2    Thomson, J.A.3
  • 15
    • 0015526732 scopus 로고
    • Participation of the protein ligands in the folding of cytochrome c
    • Babul, J. & Stellwagen, E. (1972). Participation of the protein ligands in the folding of cytochrome c. Biochemistry 11, 1195-1200.
    • (1972) Biochemistry , vol.11 , pp. 1195-1200
    • Babul, J.1    Stellwagen, E.2
  • 16
    • 0018265664 scopus 로고
    • The unfolding of cytochromes c in methanol and acid
    • Drew, H.R. & Dickerson, R.E. (1978). The unfolding of cytochromes c in methanol and acid. J. Mol. Biol. 253, 8420-8427.
    • (1978) J. Mol. Biol. , vol.253 , pp. 8420-8427
    • Drew, H.R.1    Dickerson, R.E.2
  • 18
    • 33845278074 scopus 로고
    • Direct electrochemistry of the undecapeptide from cytochrome c (microperoxidase) at a glassy carbon electrode
    • Santucci, R., Reinhard, H. & Brunori, M. (1988). Direct electrochemistry of the undecapeptide from cytochrome c (microperoxidase) at a glassy carbon electrode. J. Am. Chem. Soc. 110, 8536-8537.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 8536-8537
    • Santucci, R.1    Reinhard, H.2    Brunori, M.3
  • 20
    • 0025007598 scopus 로고
    • High-resolution 3-dimensional structure of horse heart cytochrome c
    • Bushnell, G.W., Louie, G.V. & 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
  • 21
    • 0026608669 scopus 로고
    • Oxidation-state dependent conformational changes in cytochrome c
    • Berghuis, A.M. & Brayer, G.D. (1992). Oxidation-state dependent conformational changes in cytochrome c. J. Mol. Biol. 223, 959-976.
    • (1992) J. Mol. Biol. , vol.223 , pp. 959-976
    • Berghuis, A.M.1    Brayer, G.D.2
  • 22
    • 0017027586 scopus 로고
    • Ferricytochrome c chain folding measured by the energy transfer of tryptophan to the heme group
    • Tsong, T.Y. (1976). Ferricytochrome c chain folding measured by the energy transfer of tryptophan to the heme group. Biochemistry 15, 5467-5473.
    • (1976) Biochemistry , vol.15 , pp. 5467-5473
    • Tsong, T.Y.1
  • 23
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai, Y., Sosnick, T.R., Mayne, L & Englander, S.W. (1995). Protein folding intermediates: native-state hydrogen exchange. Science 269, 192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 24
    • 0028947257 scopus 로고
    • Funnels, pathways and the energy landscape of protein folding - A synthesis
    • Bryngelson, J.D., Onuchic, J.N. & Wolynes, P.G. (1995). Funnels, pathways and the energy landscape of protein folding - a synthesis. Proteins: Struct. Func. Gen. 21, 167-195.
    • (1995) Proteins: Struct. Func. Gen. , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 26
    • 5244245983 scopus 로고
    • A correlation of reaction rates
    • Hammond, G.S. (1955). A correlation of reaction rates. J. Am. Chem. Soc. 77, 334-338.
    • (1955) J. Am. Chem. Soc. , vol.77 , pp. 334-338
    • Hammond, G.S.1
  • 27
    • 0029940033 scopus 로고    scopus 로고
    • Molecular collapse: The rate-limiting step in two-state cytochrome c folding
    • Sosnick, T.R., Mayne, L & Englander, S.W. (1996). Molecular collapse: the rate-limiting step in two-state cytochrome c folding. Proteins: Struct. Func. Gen. 24, 413-426.
    • (1996) Proteins: Struct. Func. Gen. , vol.24 , pp. 413-426
    • Sosnick, T.R.1    Mayne, L.2    Englander, S.W.3
  • 28
    • 0027171034 scopus 로고
    • Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding
    • Matouschek, A. & Fersht, A.R. (1993). Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding. Proc. Natl. Acad. Sci. USA 90, 7814-7818.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7814-7818
    • Matouschek, A.1    Fersht, A.R.2
  • 29
    • 0027948175 scopus 로고
    • Structure of the transition state for the foldingfunfolding of the barley chymostrypsin inhibitor 2 and its implications for mechanisms of protein folding
    • Otzen, D.E., Itzhaki, LS., El Masry, N.F, Jackson, S.E. & Fersht A.R. (1994). Structure of the transition state for the foldingfunfolding of the barley chymostrypsin inhibitor 2 and its implications for mechanisms of protein folding. Proc. Natl. Acad. Sci. USA 91, 10422-10425.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10422-10425
    • Otzen, D.E.1    Itzhaki, L.S.2    El Masry, N.F.3    Jackson, S.E.4    Fersht, A.R.5
  • 30
    • 0028037217 scopus 로고
    • Single versus parallel pathways of protein folding and fractional formation of structure in the transition state
    • Fersht, A.R., Itzhaki, L.S., El Masry, N.F., Matthews, J.M. & Otzen D.E. (1994). Single versus parallel pathways of protein folding and fractional formation of structure in the transition state. Proc. Natl. Acad. Sd. USA 91, 10426-10429.
    • (1994) Proc. Natl. Acad. Sd. USA , vol.91 , pp. 10426-10429
    • Fersht, A.R.1    Itzhaki, L.S.2    El Masry, N.F.3    Matthews, J.M.4    Otzen, D.E.5
  • 32
    • 0029967474 scopus 로고    scopus 로고
    • Side-chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding
    • Colón, W., Elöve, G.A., Wakem, L.P., Sherman, F. & Roder, H. (1996). Side-chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding. Biochemistry 35, 5538-5549.
    • (1996) Biochemistry , vol.35 , pp. 5538-5549
    • Colón, W.1    Elöve, G.A.2    Wakem, L.P.3    Sherman, F.4    Roder, H.5
  • 33
    • 0000710672 scopus 로고    scopus 로고
    • Diffusive dynamics of the reaction coordinate for protein folding funnels
    • Socci, N.D., Onuchic, J.N. & Wolynes, P.G. (1996). Diffusive dynamics of the reaction coordinate for protein folding funnels. J. Chem. Phys. 104, 5860-5868.
    • (1996) J. Chem. Phys. , vol.104 , pp. 5860-5868
    • Socci, N.D.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 36
    • 0004629518 scopus 로고
    • Transient electron-transfer studies on the two-subunit cytochrome c oxidase from Paracoccus denitrificans
    • Stowell, M.H.B, Larsen, R.W., Winkler, J.R., Rees, D.C. & Chan, S.I. (1993). Transient electron-transfer studies on the two-subunit cytochrome c oxidase from Paracoccus denitrificans. J. Phys. Chem. 97, 3054-3057.
    • (1993) J. Phys. Chem. , vol.97 , pp. 3054-3057
    • Stowell, M.H.B.1    Larsen, R.W.2    Winkler, J.R.3    Rees, D.C.4    Chan, S.I.5
  • 37
    • 0000699151 scopus 로고
    • Evidence for lifetime distributions in cyclodextrin inclusion complexes
    • Bright, F.V., Catena, G.C. & Huang, J. (1990). Evidence for lifetime distributions in cyclodextrin inclusion complexes. J. Am. Chem. Soc. 112, 1343-1346.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 1343-1346
    • Bright, F.V.1    Catena, G.C.2    Huang, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.