메뉴 건너뛰기




Volumn 52, Issue 38, 2013, Pages 6615-6626

Loss of electrostatic interactions causes increase of dynamics within the plastocyanin-cytochrome f complex

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEX FORMATIONS; ELECTRON TRANSFER; ENCOUNTER COMPLEX; HYDROPHOBIC CONTACT; HYDROPHOBIC INTERACTIONS; HYDROPHOBIC PATCH; PARAMAGNETIC RELAXATION; PROTEIN COMPLEXES;

EID: 84884862752     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400450q     Document Type: Article
Times cited : (15)

References (44)
  • 1
    • 0026607545 scopus 로고
    • Kinetics of protein-protein association explained by Brownian dynamics computer simulation
    • Northrup, S. H. and Erickson, H. P. (1992) Kinetics of protein-protein association explained by Brownian dynamics computer simulation Proc. Natl. Acad. Sci. U.S.A. 89, 3338-3342
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 3338-3342
    • Northrup, S.H.1    Erickson, H.P.2
  • 2
    • 62849090890 scopus 로고    scopus 로고
    • The courtship of proteins: Understanding the encounter complex
    • Ubbink, M. (2009) The courtship of proteins: understanding the encounter complex FEBS Lett. 583, 1060-1066
    • (2009) FEBS Lett. , vol.583 , pp. 1060-1066
    • Ubbink, M.1
  • 3
    • 0036468995 scopus 로고    scopus 로고
    • Kinetic studies of protein-protein interactions
    • Schreiber, G. (2002) Kinetic studies of protein-protein interactions Curr. Opin. Struct. Biol. 12, 41-47
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 41-47
    • Schreiber, G.1
  • 4
    • 0032981961 scopus 로고    scopus 로고
    • Free energy landscapes of encounter complexes in protein-protein association
    • Camacho, C. J., Weng, Z., Vajda, S., and DeLisi, C. (1999) Free energy landscapes of encounter complexes in protein-protein association Biophys. J. 76, 1166-1178
    • (1999) Biophys. J. , vol.76 , pp. 1166-1178
    • Camacho, C.J.1    Weng, Z.2    Vajda, S.3    Delisi, C.4
  • 5
    • 0034049350 scopus 로고    scopus 로고
    • Kinetics of desolvation-mediated protein-protein binding
    • Camacho, C. J., Kimura, S. R., DeLisi, C., and Vajda, S. (2000) Kinetics of desolvation-mediated protein-protein binding Biophys. J. 78, 1094-1105
    • (2000) Biophys. J. , vol.78 , pp. 1094-1105
    • Camacho, C.J.1    Kimura, S.R.2    Delisi, C.3    Vajda, S.4
  • 6
    • 0035845563 scopus 로고    scopus 로고
    • Protein docking along smooth association pathways
    • Camacho, C. J. and Vajda, S. (2001) Protein docking along smooth association pathways Proc. Natl. Acad. Sci. U.S.A. 98, 10636-10641
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 10636-10641
    • Camacho, C.J.1    Vajda, S.2
  • 7
    • 51349101286 scopus 로고    scopus 로고
    • Replica exchange simulations of transient encounter complexes in protein-protein association
    • Kim, Y. C., Tang, C., Clore, G. M., and Hummer, G. (2008) Replica exchange simulations of transient encounter complexes in protein-protein association Proc. Natl. Acad. Sci. U.S.A. 105, 12855-12860
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 12855-12860
    • Kim, Y.C.1    Tang, C.2    Clore, G.M.3    Hummer, G.4
  • 8
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • Sugase, K., Dyson, H. J., and Wright, P. E. (2007) Mechanism of coupled folding and binding of an intrinsically disordered protein Nature 447, 1021-1025
    • (2007) Nature , vol.447 , pp. 1021-1025
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 9
    • 84878228355 scopus 로고    scopus 로고
    • Role of hydrophobic interactions in the encounter cmplex formation of the plastocyanin and cytochrome complex revealed by paramagnetic NMR spectroscopy
    • Scanu, S., Foerster, J. M., Ullmann, G. M., and Ubbink, M. (2013) Role of hydrophobic interactions in the encounter cmplex formation of the plastocyanin and cytochrome complex revealed by paramagnetic NMR spectroscopy J. Am. Chem. Soc. 135, 7681-7692
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 7681-7692
    • Scanu, S.1    Foerster, J.M.2    Ullmann, G.M.3    Ubbink, M.4
  • 10
    • 0034598395 scopus 로고    scopus 로고
    • Electron transfers amongst cytochrome f, plastocyanin and photosystem I: Kinetics and mechanisms
    • Hope, A. B. (2000) Electron transfers amongst cytochrome f, plastocyanin and photosystem I: kinetics and mechanisms Biochim. Biophys. Acta 1456, 5-26
    • (2000) Biochim. Biophys. Acta , vol.1456 , pp. 5-26
    • Hope, A.B.1
  • 12
    • 0142213304 scopus 로고    scopus 로고
    • Close encounter of the transient kind: Protein interactions in the photosynthetic redox chain investigated by NMR spectroscopy
    • Crowley, P. B. and Ubbink, M. (2003) Close encounter of the transient kind: protein interactions in the photosynthetic redox chain investigated by NMR spectroscopy Acc. Chem. Res. 36, 723-730
    • (2003) Acc. Chem. Res. , vol.36 , pp. 723-730
    • Crowley, P.B.1    Ubbink, M.2
  • 13
    • 0029873697 scopus 로고    scopus 로고
    • Rapid, electrostatically assisted association of proteins
    • Schreiber, G. and Fersht, A. R. (1996) Rapid, electrostatically assisted association of proteins Nat. Struct. Biol. 3, 427-431
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 427-431
    • Schreiber, G.1    Fersht, A.R.2
  • 14
    • 0000067495 scopus 로고    scopus 로고
    • The role of individual lysine residues in the basic patch on turnip cytochrome f for electrostatic interactions with plastocyanin in vitro
    • Gong, X. S., Wen, J. Q., Fisher, N. E., Young, S., Howe, C. J., Bendall, D. S., and Gray, J. C. (2000) The role of individual lysine residues in the basic patch on turnip cytochrome f for electrostatic interactions with plastocyanin in vitro Eur. J. Biochem. 267, 3461-3468
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3461-3468
    • Gong, X.S.1    Wen, J.Q.2    Fisher, N.E.3    Young, S.4    Howe, C.J.5    Bendall, D.S.6    Gray, J.C.7
  • 15
    • 0029995705 scopus 로고    scopus 로고
    • The role of acidic residues of plastocyanin in its interaction with cytochrome f
    • Kannt, A., Young, S., and Bendall, D. S. (1996) The role of acidic residues of plastocyanin in its interaction with cytochrome f Biochim. Biophys. Acta 1277, 115-126
    • (1996) Biochim. Biophys. Acta , vol.1277 , pp. 115-126
    • Kannt, A.1    Young, S.2    Bendall, D.S.3
  • 16
    • 0037066083 scopus 로고    scopus 로고
    • Role of electrostatics in the interaction between cytochrome f and plastocyanin of the cyanobacterium Phormidium laminosum
    • Schlarb-Ridley, B. G., Bendall, D. S., and Howe, C. J. (2002) Role of electrostatics in the interaction between cytochrome f and plastocyanin of the cyanobacterium Phormidium laminosum Biochemistry 41, 3279-3285
    • (2002) Biochemistry , vol.41 , pp. 3279-3285
    • Schlarb-Ridley, B.G.1    Bendall, D.S.2    Howe, C.J.3
  • 17
    • 0037657832 scopus 로고    scopus 로고
    • Role of charges on cytochrome f from the cyanobacterium Phormidium laminosum in its interaction with plastocyanin
    • Hart, S. E., Schlarb-Ridley, B. G., Delon, C., Bendall, D. S., and Howe, C. J. (2003) Role of charges on cytochrome f from the cyanobacterium Phormidium laminosum in its interaction with plastocyanin Biochemistry 42, 4829-4836
    • (2003) Biochemistry , vol.42 , pp. 4829-4836
    • Hart, S.E.1    Schlarb-Ridley, B.G.2    Delon, C.3    Bendall, D.S.4    Howe, C.J.5
  • 18
    • 23944504726 scopus 로고    scopus 로고
    • Laser flash-induced kinetic analysis of cytochrome f oxidation by wild-type and mutant plastocyanin from the cyanobacterium Nostoc sp. PCC 7119
    • Albarran, C., Navarro, J. A., Molina-Heredia, F. P., Murdoch, P. S., De la Rosa, M. A., and Hervas, M. (2005) Laser flash-induced kinetic analysis of cytochrome f oxidation by wild-type and mutant plastocyanin from the cyanobacterium Nostoc sp. PCC 7119 Biochemistry 44, 11601-11607
    • (2005) Biochemistry , vol.44 , pp. 11601-11607
    • Albarran, C.1    Navarro, J.A.2    Molina-Heredia, F.P.3    Murdoch, P.S.4    De La Rosa, M.A.5    Hervas, M.6
  • 19
    • 33846607313 scopus 로고    scopus 로고
    • The specificity in the interaction between cytochrome f and plastocyanin from the cyanobacterium Nostoc sp. PCC 7119 is mainly determined by the copper protein
    • Albarran, C., Navarro, J., De la Rosa, M. A., and Hervas, M. (2007) The specificity in the interaction between cytochrome f and plastocyanin from the cyanobacterium Nostoc sp. PCC 7119 is mainly determined by the copper protein Biochemistry 46, 997-1003
    • (2007) Biochemistry , vol.46 , pp. 997-1003
    • Albarran, C.1    Navarro, J.2    De La Rosa, M.A.3    Hervas, M.4
  • 20
    • 0032520957 scopus 로고    scopus 로고
    • The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics
    • Ubbink, M., Ejdeback, M., Karlsson, B. G., and Bendall, D. S. (1998) The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics Structure 6, 323-335
    • (1998) Structure , vol.6 , pp. 323-335
    • Ubbink, M.1    Ejdeback, M.2    Karlsson, B.G.3    Bendall, D.S.4
  • 21
  • 22
    • 21444446549 scopus 로고    scopus 로고
    • Structure of the complex between plastocyanin and cytochrome f from the cyanobacterium Nostoc sp. PCC 7119 as determined by paramagnetic NMR. The balance between electrostatic and hydrophobic interactions within the transient complex determines the relative orientation of the two proteins
    • Diaz-Moreno, I., Diaz-Quintana, A., De la Rosa, M. A., and Ubbink, M. (2005) Structure of the complex between plastocyanin and cytochrome f from the cyanobacterium Nostoc sp. PCC 7119 as determined by paramagnetic NMR. The balance between electrostatic and hydrophobic interactions within the transient complex determines the relative orientation of the two proteins J. Biol. Chem. 280, 35784
    • (2005) J. Biol. Chem. , vol.280 , pp. 35784
    • Diaz-Moreno, I.1    Diaz-Quintana, A.2    De La Rosa, M.A.3    Ubbink, M.4
  • 23
    • 18044367301 scopus 로고    scopus 로고
    • The transient complex of poplar plastocyanin with cytochrome f: Effects of ionic strength and pH
    • Lange, C., Cornvik, T., Diaz-Moreno, I., and Ubbink, M. (2005) The transient complex of poplar plastocyanin with cytochrome f: effects of ionic strength and pH Biochim. Biophys. Acta 1707, 179-188
    • (2005) Biochim. Biophys. Acta , vol.1707 , pp. 179-188
    • Lange, C.1    Cornvik, T.2    Diaz-Moreno, I.3    Ubbink, M.4
  • 24
    • 39049109333 scopus 로고    scopus 로고
    • Dynamics in the transient complex of plastocyanin-cytochrome f from Prochlorothrix hollandica
    • Hulsker, R., Baranova, M. V., Bullerjahn, G. S., and Ubbink, M. (2008) Dynamics in the transient complex of plastocyanin-cytochrome f from Prochlorothrix hollandica J. Am. Chem. Soc. 130, 1985-1991
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 1985-1991
    • Hulsker, R.1    Baranova, M.V.2    Bullerjahn, G.S.3    Ubbink, M.4
  • 25
    • 14644444207 scopus 로고    scopus 로고
    • Different modes of interaction in cyanobacterial complexes of plastocyanin and cytochrome f
    • Diaz-Moreno, I., Diaz-Quintana, A., De la Rosa, M. A., Crowley, P. B., and Ubbink, M. (2005) Different modes of interaction in cyanobacterial complexes of plastocyanin and cytochrome f Biochemistry 44, 3176-3183
    • (2005) Biochemistry , vol.44 , pp. 3176-3183
    • Diaz-Moreno, I.1    Diaz-Quintana, A.2    De La Rosa, M.A.3    Crowley, P.B.4    Ubbink, M.5
  • 26
    • 0033029167 scopus 로고    scopus 로고
    • Expression of plastocyanin and cytochrome f of the cyanobacterium Phormidium laminosum in Escherichia coli and Paracoccus denitrificants and the role of leader peptides
    • Schlarb, B. G., Wagner, M. J., Vijgenboom, E., Ubbink, M., Bendall, D. S., and Howe, C. J. (1999) Expression of plastocyanin and cytochrome f of the cyanobacterium Phormidium laminosum in Escherichia coli and Paracoccus denitrificants and the role of leader peptides Gene 234, 275-283
    • (1999) Gene , vol.234 , pp. 275-283
    • Schlarb, B.G.1    Wagner, M.J.2    Vijgenboom, E.3    Ubbink, M.4    Bendall, D.S.5    Howe, C.J.6
  • 27
    • 84862317298 scopus 로고    scopus 로고
    • The complex of cytochrome f and plastocyanin from Nostoc sp. PCC 7119 is highly dynamic
    • Scanu, S., Foerster, J., Finiguerra, M. G., Shabestari, M. H., Huber, M., and Ubbink, M. (2012) The complex of cytochrome f and plastocyanin from Nostoc sp. PCC 7119 is highly dynamic ChemBioChem 13, 1312-1318
    • (2012) ChemBioChem , vol.13 , pp. 1312-1318
    • Scanu, S.1    Foerster, J.2    Finiguerra, M.G.3    Shabestari, M.H.4    Huber, M.5    Ubbink, M.6
  • 28
    • 70349734868 scopus 로고    scopus 로고
    • A pulsed EPR method to determine distances between paramagnetic centers with strong spectral anisotropy and radicals: The dead-time free RIDME sequence
    • Milikisyants, S., Scarpelli, F., Finiguerra, M. G., Ubbink, M., and Huber, M. (2009) A pulsed EPR method to determine distances between paramagnetic centers with strong spectral anisotropy and radicals: the dead-time free RIDME sequence J. Magn. Reson. 201, 48-56
    • (2009) J. Magn. Reson. , vol.201 , pp. 48-56
    • Milikisyants, S.1    Scarpelli, F.2    Finiguerra, M.G.3    Ubbink, M.4    Huber, M.5
  • 29
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 31
    • 0034625121 scopus 로고    scopus 로고
    • Utilization of site-directed spin labelling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data
    • Battiste, J. L. and Wagner, G. (2000) Utilization of site-directed spin labelling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data Biochemistry 39, 5355-5365
    • (2000) Biochemistry , vol.39 , pp. 5355-5365
    • Battiste, J.L.1    Wagner, G.2
  • 32
    • 65649136908 scopus 로고    scopus 로고
    • Structure-function, stability, and chemical modification of the cyanobacterial cytochrome b6f complex from Nostoc sp. PCC 7120
    • Baniulis, D., Yamashita, E., Whitelegge, J. P., Zatsman, A. I., Hendrich, M. P., Hasan, S. S., Ryan, C. M., and Cramer, W. A. (2009) Structure-function, stability, and chemical modification of the cyanobacterial cytochrome b6f complex from Nostoc sp. PCC 7120 J. Biol. Chem. 284, 9861-9869
    • (2009) J. Biol. Chem. , vol.284 , pp. 9861-9869
    • Baniulis, D.1    Yamashita, E.2    Whitelegge, J.P.3    Zatsman, A.I.4    Hendrich, M.P.5    Hasan, S.S.6    Ryan, C.M.7    Cramer, W.A.8
  • 35
    • 0031041540 scopus 로고    scopus 로고
    • Computational simulation and analysis of dynamic association between plastocyanin and cytochrome f. Consequences for the electron-transfer reaction
    • Ullmann, G. M., Knapp, E. W., and Kostic, N. M. (1997) Computational simulation and analysis of dynamic association between plastocyanin and cytochrome f. Consequences for the electron-transfer reaction J. Am. Chem. Soc. 119, 42-52
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 42-52
    • Ullmann, G.M.1    Knapp, E.W.2    Kostic, N.M.3
  • 36
    • 74849106907 scopus 로고    scopus 로고
    • Visualization of the encounter ensemble of the transient electron transfer complex of cytochrome c and cytochrome c peroxidase
    • Bashir, Q., Volkov, A. N., Ullmann, G. M., and Ubbink, M. (2010) Visualization of the encounter ensemble of the transient electron transfer complex of cytochrome c and cytochrome c peroxidase J. Am. Chem. Soc. 132, 241-247
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 241-247
    • Bashir, Q.1    Volkov, A.N.2    Ullmann, G.M.3    Ubbink, M.4
  • 37
    • 0029658124 scopus 로고    scopus 로고
    • Analysis of the 1H-NMR chemical shifts of Cu(I)-, Cu(II)- and Cd-substituted pea plastocyanin. Metal-dependent differences in the hydrogen-bond network around the copper site
    • Ubbink, M., Lian, L. Y., Modi, S., Evans, P. A., and Bendall, D. S. (1996) Analysis of the 1H-NMR chemical shifts of Cu(I)-, Cu(II)- and Cd-substituted pea plastocyanin. Metal-dependent differences in the hydrogen-bond network around the copper site Eur. J. Biochem. 242, 132-147
    • (1996) Eur. J. Biochem. , vol.242 , pp. 132-147
    • Ubbink, M.1    Lian, L.Y.2    Modi, S.3    Evans, P.A.4    Bendall, D.S.5
  • 38
    • 0033609516 scopus 로고    scopus 로고
    • Structure of the soluble domain of cytochrome f from the cyanobacterium Phormidium laminosum
    • Carrell, C. J., Schlarb, B. G., Bendall, D. S., Howe, C. J., Cramer, W. A., and Smith, J. L. (1999) Structure of the soluble domain of cytochrome f from the cyanobacterium Phormidium laminosum Biochemistry 38, 9590-9599
    • (1999) Biochemistry , vol.38 , pp. 9590-9599
    • Carrell, C.J.1    Schlarb, B.G.2    Bendall, D.S.3    Howe, C.J.4    Cramer, W.A.5    Smith, J.L.6
  • 39
    • 70349093561 scopus 로고    scopus 로고
    • Theory, practice and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes
    • Clore, G. M. and Iwahara, J. (2009) Theory, practice and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes Chem. Rev. 109, 4108-4139
    • (2009) Chem. Rev. , vol.109 , pp. 4108-4139
    • Clore, G.M.1    Iwahara, J.2
  • 40
    • 0036771785 scopus 로고    scopus 로고
    • Myoglobin and cytochrome b5: A nuclear magnetic resonance study of a highly dynamic protein complex
    • Worrall, J. A. R., Liu, Y. J., Crowley, P. B., Nocek, J. M., Hoffman, B. M., and Ubbink, M. (2002) Myoglobin and cytochrome b5: a nuclear magnetic resonance study of a highly dynamic protein complex Biochemistry 41, 11721-11730
    • (2002) Biochemistry , vol.41 , pp. 11721-11730
    • Worrall, J.A.R.1    Liu, Y.J.2    Crowley, P.B.3    Nocek, J.M.4    Hoffman, B.M.5    Ubbink, M.6
  • 41
    • 43949086199 scopus 로고    scopus 로고
    • Dynamics in a pure encounter complex of two proteins studied by solution scattering and paramagnetic NMR spectroscopy
    • Xu, X. F., Reinle, W. G., Hannemann, F., Konarev, P. V., Svergun, D. I., Bernhardt, R., and Ubbink, M. (2008) Dynamics in a pure encounter complex of two proteins studied by solution scattering and paramagnetic NMR spectroscopy J. Am. Chem. Soc. 130, 6395-6403
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 6395-6403
    • Xu, X.F.1    Reinle, W.G.2    Hannemann, F.3    Konarev, P.V.4    Svergun, D.I.5    Bernhardt, R.6    Ubbink, M.7
  • 42
    • 77955787224 scopus 로고    scopus 로고
    • Shifting the equilibrium between the encounter state and the specific form of a protein complex by interfacial point mutations
    • Volkov, A. N., Bashir, Q., Worrall, J. A. R., Ullmann, G. M., and Ubbink, M. (2010) Shifting the equilibrium between the encounter state and the specific form of a protein complex by interfacial point mutations J. Am. Chem. Soc. 132, 11487-11495
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 11487-11495
    • Volkov, A.N.1    Bashir, Q.2    Worrall, J.A.R.3    Ullmann, G.M.4    Ubbink, M.5
  • 43
    • 0030446029 scopus 로고    scopus 로고
    • Effect of the interdomain basic region of cytochrome f on its redox reactions in vivo
    • Soriano, G. M., Ponamarev, M. V., Tae, G. -S., and Cramer, W. A. (1996) Effect of the interdomain basic region of cytochrome f on its redox reactions in vivo Biochemistry 35, 14590-14598
    • (1996) Biochemistry , vol.35 , pp. 14590-14598
    • Soriano, G.M.1    Ponamarev, M.V.2    Tae, G.-S.3    Cramer, W.A.4
  • 44
    • 0032573033 scopus 로고    scopus 로고
    • Identification of the basic residues of cytochrome f responsible for electrostatic docking interactions with plastocyanin in vitro: Relevance to the electron transfer reaction in vivo
    • Soriano, G. M., Ponamarev, M. V., Piskorowski, R. A., and Cramer, W. A. (1998) Identification of the basic residues of cytochrome f responsible for electrostatic docking interactions with plastocyanin in vitro: relevance to the electron transfer reaction in vivo Biochemistry 37, 15120-15128
    • (1998) Biochemistry , vol.37 , pp. 15120-15128
    • Soriano, G.M.1    Ponamarev, M.V.2    Piskorowski, R.A.3    Cramer, W.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.