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Volumn 18, Issue 3, 2009, Pages 670-674

Fast structural dynamics in reduced and oxidized cytochrome c

Author keywords

Electron transfer; NMR relaxation; Protein dynamics; Redox state

Indexed keywords

CYTOCHROME C;

EID: 61449211125     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.72     Document Type: Article
Times cited : (14)

References (36)
  • 1
    • 0034760077 scopus 로고    scopus 로고
    • Dynamic activation of protein function: A view emerging from NMR spectroscopy
    • Wand AJ (2001) Dynamic activation of protein function: a view emerging from NMR spectroscopy. Nat Struct Biol 8:926-931.
    • (2001) Nat Struct Biol , vol.8 , pp. 926-931
    • Wand, A.J.1
  • 2
    • 1442328094 scopus 로고    scopus 로고
    • Electron tunneling through proteins
    • Gray HB, Winkler JR (2003) Electron tunneling through proteins. Q Rev Biophys 36:341-372.
    • (2003) Q Rev Biophys , vol.36 , pp. 341-372
    • Gray, H.B.1    Winkler, J.R.2
  • 3
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunneling in biological oxidation-reduction
    • Page CC, Moser CC, Chen X, Dutton PL (1999) Natural engineering principles of electron tunneling in biological oxidation-reduction. Nature 402:47-52.
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 4
    • 0019084947 scopus 로고
    • Quantum-mechanical tunnelling in biological-systems
    • Devault D (1980) Quantum-mechanical tunnelling in biological-systems. Q Rev Biophys 13:387-564.
    • (1980) Q Rev Biophys , vol.13 , pp. 387-564
    • Devault, D.1
  • 5
    • 0010884753 scopus 로고
    • Theory of oxidation-reduction reactions involving electron transfer. 1
    • Marcus RA (1956) Theory of oxidation-reduction reactions involving electron transfer. 1. J Chem Phys 24: 966-978.
    • (1956) J Chem Phys , vol.24 , pp. 966-978
    • Marcus, R.A.1
  • 6
    • 0035707451 scopus 로고    scopus 로고
    • Dynamics of biochemical and biophysical reactions: Insight from computer simulations
    • Warshel A, Parson WW (2001) Dynamics of biochemical and biophysical reactions: insight from computer simulations. Q Rev Biophys 34:563-679.
    • (2001) Q Rev Biophys , vol.34 , pp. 563-679
    • Warshel, A.1    Parson, W.W.2
  • 7
    • 0040960707 scopus 로고
    • Electrontunneling through covalent and noncovalent pathways in proteins
    • Beratan DN, Onuchic JN, Hopfield JJ (1987) Electrontunneling through covalent and noncovalent pathways in proteins. J Chem Phys 86:4488-4498.
    • (1987) J Chem Phys , vol.86 , pp. 4488-4498
    • Beratan, D.N.1    Onuchic, J.N.2    Hopfield, J.J.3
  • 8
    • 0026434593 scopus 로고
    • Protein electron-transfer rates set by the bridging secondary and tertiary structure
    • Beratan DN, Betts JN, Onuchic JN (1991) Protein electron-transfer rates set by the bridging secondary and tertiary structure. Science 252:1285-1288.
    • (1991) Science , vol.252 , pp. 1285-1288
    • Beratan, D.N.1    Betts, J.N.2    Onuchic, J.N.3
  • 9
    • 0027733719 scopus 로고
    • Effective coupling in biological electron-transfer-exponential or complex distance dependence
    • Evenson JW, Karplus M (1993) Effective coupling in biological electron-transfer-exponential or complex distance dependence. Science 262:1247-1249.
    • (1993) Science , vol.262 , pp. 1247-1249
    • Evenson, J.W.1    Karplus, M.2
  • 10
    • 0001310733 scopus 로고    scopus 로고
    • A new framework for electron-transfer calculations-beyond the pathways-like models
    • Balabin IA, Onuchic JN (1998) A new framework for electron-transfer calculations-beyond the pathways-like models. J Phys Chem B 102:7497-7505.
    • (1998) J Phys Chem B , vol.102 , pp. 7497-7505
    • Balabin, I.A.1    Onuchic, J.N.2
  • 11
    • 0034613172 scopus 로고    scopus 로고
    • Dynamically controlled protein tunneling paths in photosynthetic reaction centers
    • Balabin LA, Onuchic JN (2000) Dynamically controlled protein tunneling paths in photosynthetic reaction centers. Science 290:114-117.
    • (2000) Science , vol.290 , pp. 114-117
    • Balabin, L.A.1    Onuchic, J.N.2
  • 12
    • 0037726814 scopus 로고    scopus 로고
    • Conformational reorganisation in interfacial protein, electron transfer. Biochem. Biophys Acta
    • Jeuken LJC (2003) Conformational reorganisation in interfacial protein, electron transfer. Biochem. Biophys Acta Bioenerg 1604:67-76.
    • (2003) Bioenerg , vol.1604 , pp. 67-76
    • Jeuken, L.J.C.1
  • 13
    • 33646945580 scopus 로고    scopus 로고
    • Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution
    • Igumenova TI, Frederick KK, Wand AJ (2006) Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution. Chem Rev 106: 1672-1699.
    • (2006) Chem Rev , vol.106 , pp. 1672-1699
    • Igumenova, T.I.1    Frederick, K.K.2    Wand, A.J.3
  • 14
    • 0037180383 scopus 로고    scopus 로고
    • Recombinant equine cytochrome c in Escherichia coli: High-level expression, characterization, and folding and assembly mutants
    • Rumbley JN, Hoang L, Englander SW (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
  • 15
    • 0042510863 scopus 로고    scopus 로고
    • Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c
    • Liu W, Rumbley J, Englander SW, Wand AJ (2003) Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c. Prot Sci 12:2104-2108.
    • (2003) Prot Sci , vol.12 , pp. 2104-2108
    • Liu, W.1    Rumbley, J.2    Englander, S.W.3    Wand, A.J.4
  • 16
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari G, Szabo A (1982) Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J Am Chem Soc 104:4546-4559.
    • (1982) J Am Chem Soc , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 17
    • 53849092076 scopus 로고    scopus 로고
    • Re-evaluation of the model-free analysis of fast internal motion in proteins using NMR relaxation
    • Frederick KK, Sharp KA, Warischalk N, Wand AJ (2008) Re-evaluation of the model-free analysis of fast internal motion in proteins using NMR relaxation. J Phys Chem B 112:12095-12103.
    • (2008) J Phys Chem B , vol.112 , pp. 12095-12103
    • Frederick, K.K.1    Sharp, K.A.2    Warischalk, N.3    Wand, A.J.4
  • 19
    • 33746224059 scopus 로고    scopus 로고
    • Conformational dynamics of calmodulin in complex with the calmodulin-dependent kinase kinase alpha calmodulin-binding domain
    • Marlow MS, Wand AJ (2006) Conformational dynamics of calmodulin in complex with the calmodulin-dependent kinase kinase alpha calmodulin-binding domain. Biochemistry 45:8732-8741.
    • (2006) Biochemistry , vol.45 , pp. 8732-8741
    • Marlow, M.S.1    Wand, A.J.2
  • 20
    • 0029176895 scopus 로고
    • Measurement of H-2 T-1 and T-1p relaxation-times in uniformly C-13-labeled and fractionally H-2-labeled proteins in solution
    • Muhandiram. DR, Yamazaki T, Sykes BD, Kay LE (1995) Measurement of H-2 T-1 and T-1p relaxation-times in uniformly C-13-labeled and fractionally H-2-labeled proteins in solution. J Am Chem Soc 117:11536-11544.
    • (1995) J Am Chem Soc , vol.117 , pp. 11536-11544
    • Muhandiram, D.R.1    Yamazaki, T.2    Sykes, B.D.3    Kay, L.E.4
  • 21
    • 0024402002 scopus 로고
    • Model-independent and model-dependent analysis of the global and internal dynamics of cyclosporine A
    • Dellwo MJ, Wand AJ (1989) Model-independent and model-dependent analysis of the global and internal dynamics of cyclosporine A. J Am Chem Soc 111: 4571-4578.
    • (1989) J Am Chem Soc , vol.111 , pp. 4571-4578
    • Dellwo, M.J.1    Wand, A.J.2
  • 22
    • 0025234717 scopus 로고
    • Redox-dependent structure change and hyperfine nuclear magnetic resonance shifts in cytochrome-c
    • Feng YQ, Roder H, Englander SW (1990) Redox-dependent structure change and hyperfine nuclear magnetic resonance shifts in cytochrome-c. Biochemistry 29: 3494-3504.
    • (1990) Biochemistry , vol.29 , pp. 3494-3504
    • Feng, Y.Q.1    Roder, H.2    Englander, S.W.3
  • 23
    • 33646911358 scopus 로고    scopus 로고
    • Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences
    • Jarymowycz VA, Stone MJ (2006) Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences. Chem Rev 106:1624-1671.
    • (2006) Chem Rev , vol.106 , pp. 1624-1671
    • Jarymowycz, V.A.1    Stone, M.J.2
  • 24
    • 0035810993 scopus 로고    scopus 로고
    • Main chain and side chain dynamics of a heme protein: N-15 and H-2 NMR relaxation studies of R. capsulatus ferrocytochrome c (2)
    • Flynn PF, Urbauer RJB, Zhang H, Lee AL, Wand AJ (2001) Main chain and side chain dynamics of a heme protein: N-15 and H-2 NMR relaxation studies of R. capsulatus ferrocytochrome c (2). Biochemistry 40: 6559-6569.
    • (2001) Biochemistry , vol.40 , pp. 6559-6569
    • Flynn, P.F.1    Urbauer, R.J.B.2    Zhang, H.3    Lee, A.L.4    Wand, A.J.5
  • 25
    • 0035846624 scopus 로고    scopus 로고
    • Main chain and side chain dynamics of oxidized flavodoxin from Cyanobacterium anabaena
    • Liu WX, Flynn PF, Fuentes EJ, Kranz JK, McCormick M, Wand AJ (2001) Main chain and side chain dynamics of oxidized flavodoxin from Cyanobacterium anabaena. Biochemistry 40:14744-14753.
    • (2001) Biochemistry , vol.40 , pp. 14744-14753
    • Liu, W.X.1    Flynn, P.F.2    Fuentes, E.J.3    Kranz, J.K.4    McCormick, M.5    Wand, A.J.6
  • 26
    • 0033528556 scopus 로고    scopus 로고
    • Assignment of N-15 chemical shifts and N-15 relaxation measurements for oxidized and reduced iso-1-cytochrome c
    • Fetrow JS, Baxter SM (1999) Assignment of N-15 chemical shifts and N-15 relaxation measurements for oxidized and reduced iso-1-cytochrome c. Biochemistry 38: 4480-4492.
    • (1999) Biochemistry , vol.38 , pp. 4480-4492
    • Fetrow, J.S.1    Baxter, S.M.2
  • 27
    • 0037028941 scopus 로고    scopus 로고
    • Protein dynamics and cytochrome c: Correlations between ligand vibrations and redox activity
    • Chin JK, Jimenez R, Romesberg FE (2002) Protein dynamics and cytochrome c: correlations between ligand vibrations and redox activity. J Am Chem. Soc 124: 1846-1847.
    • (2002) J Am Chem. Soc , vol.124 , pp. 1846-1847
    • Chin, J.K.1    Jimenez, R.2    Romesberg, F.E.3
  • 29
    • 0031912073 scopus 로고    scopus 로고
    • Determinants of protein hydrogen exchange studied in equine cytochrome c
    • Milne JS, Mayne L, Roder H, Wand AJ, Englander SW (1998) Determinants of protein hydrogen exchange studied in equine cytochrome c. Prot Sci 7:739-745.
    • (1998) Prot Sci , vol.7 , pp. 739-745
    • Milne, J.S.1    Mayne, L.2    Roder, H.3    Wand, A.J.4    Englander, S.W.5
  • 30
    • 0034823714 scopus 로고    scopus 로고
    • A further clue to understanding the mobility of mitochondrial yeast cytochrome c-a N-15 T-1 rho investigation of the oxidized and reduced species
    • Barker PD, Bertini I, Del Conte R, Ferguson SJ, Hajieva P, Tomlinson E, Turano P, Viezzoli MS (2001) A further clue to understanding the mobility of mitochondrial yeast cytochrome c-a N-15 T-1 rho investigation of the oxidized and reduced species. Eur J Biochem. 268: 4468-4476.
    • (2001) Eur J Biochem , vol.268 , pp. 4468-4476
    • Barker, P.D.1    Bertini, I.2    Del Conte, R.3    Ferguson, S.J.4    Hajieva, P.5    Tomlinson, E.6    Turano, P.7    Viezzoli, M.S.8
  • 31
    • 0001174286 scopus 로고    scopus 로고
    • Contribution of backbone dynamics to entropy changes occurring on oxidation of cytochrome b (5). Can redox linked changes in hydrogen bond networks modulate reduction potentials?
    • Dangi B, Blankman JI, Miller CJ, Volkman BF, Guiles RD (1998) Contribution of backbone dynamics to entropy changes occurring on oxidation of cytochrome b (5). Can redox linked changes in hydrogen bond networks modulate reduction potentials? J Phys Chem B 102: 8201-8208.
    • (1998) J Phys Chem B , vol.102 , pp. 8201-8208
    • Dangi, B.1    Blankman, J.I.2    Miller, C.J.3    Volkman, B.F.4    Guiles, R.D.5
  • 32
    • 0019888571 scopus 로고
    • Conformation change of cytochrome c. 2. Ferricytochrome c refinement at 1.8 Å and comparison with the ferrocytochrome structure
    • Takano T, Dickerson RE (1981) Conformation change of cytochrome c. 2. Ferricytochrome c refinement at 1.8 Å and comparison with the ferrocytochrome structure. J Mol Biol 153:95-115.
    • (1981) J Mol Biol , vol.153 , pp. 95-115
    • Takano, T.1    Dickerson, R.E.2
  • 33
    • 0026608669 scopus 로고
    • Oxidation state-dependent conformational changes in cytochrome c
    • Berghuis AM, Brayer GD (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
  • 36
    • 34447503697 scopus 로고    scopus 로고
    • Conformational entropy in molecular recognition by proteins
    • Frederick KK, Marlow MS, Valentine KG, Wand AJ (2007) Conformational entropy in molecular recognition by proteins. Nature 448:325-329.
    • (2007) Nature , vol.448 , pp. 325-329
    • Frederick, K.K.1    Marlow, M.S.2    Valentine, K.G.3    Wand, A.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.