메뉴 건너뛰기




Volumn 94, Issue 2-3, 2007, Pages 411-422

A Brownian dynamics computational study of the interaction of spinach plastocyanin with turnip cytochrome f: The importance of plastocyanin conformational changes

Author keywords

Brownian dynamics; Cytochrome f; Electron transport; Plastocyanin; Protein protein interactions

Indexed keywords

CYTOCHROME F; PLASTOCYANIN; VEGETABLE PROTEIN;

EID: 36849032993     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-007-9192-y     Document Type: Article
Times cited : (8)

References (54)
  • 1
    • 1542321529 scopus 로고    scopus 로고
    • Cytochrome b6f structure for signaling and vectorial metabolism
    • Allen JF (2004) Cytochrome b6f structure for signaling and vectorial metabolism. Trends Plant Sci 9:130-137
    • (2004) Trends Plant Sci , vol.9 , pp. 130-137
    • Allen, J.F.1
  • 2
    • 0023658667 scopus 로고
    • The effect of ethylene diamine chemical modification of plastocyanin on the rate of cytochrome f oxidation and P-7001 reduction
    • Anderson GP, Sanderson DG, Lee CH, Durell S, Anderson LB, Gross EL (1987) The effect of ethylene diamine chemical modification of plastocyanin on the rate of cytochrome f oxidation and P-7001 reduction. Biochim Biophys Acta 894:386-398
    • (1987) Biochim Biophys Acta , vol.894 , pp. 386-398
    • Anderson, G.P.1    Sanderson, D.G.2    Lee, C.H.3    Durell, S.4    Anderson, L.B.5    Gross, E.L.6
  • 3
    • 0035869698 scopus 로고    scopus 로고
    • Concerted motions in copper plastocyanin and azurin: An essential dynamics study
    • Arcangeli C, Bizzari AR, Cannistraro S (2001) Concerted motions in copper plastocyanin and azurin: An essential dynamics study. Biophys Chem 90:45-56
    • (2001) Biophys Chem , vol.90 , pp. 45-56
    • Arcangeli, C.1    Bizzari, A.R.2    Cannistraro, S.3
  • 8
    • 0031467302 scopus 로고    scopus 로고
    • Long-term molecular dynamics simulation of copper plastocyanin in water
    • Ciocchetti A, Bizzarri AR, Cannistraro S (1997) Long-term molecular dynamics simulation of copper plastocyanin in water. Biophys Chem 69:185-198
    • (1997) Biophys Chem , vol.69 , pp. 185-198
    • Ciocchetti, A.1    Bizzarri, A.R.2    Cannistraro, S.3
  • 9
    • 0142213304 scopus 로고    scopus 로고
    • Close encounters of the transient kind: Protein interactions in the photosynthetic redox chain investigated by NMR spectroscopy
    • Crowley PB, Ubbink M (2003) Close encounters 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
  • 10
    • 1542374666 scopus 로고    scopus 로고
    • The parsley plastocyanin-turnip cytochrome f complex: A structurally distorted but kinetically functional acidic patch
    • Crowley PB, Hunter DM, Sato K, McFarlane W, Dennison K (2004) The parsley plastocyanin-turnip cytochrome f complex: a structurally distorted but kinetically functional acidic patch. Biochem J 378:45-51
    • (2004) Biochem J , vol.378 , pp. 45-51
    • Crowley, P.B.1    Hunter, D.M.2    Sato, K.3    McFarlane, W.4    Dennison, K.5
  • 11
    • 0035204346 scopus 로고    scopus 로고
    • Electrostatic analysis and Brownian dynamics simulation of the association of plastocyanin and cytochrome f
    • De Rienzo F, Gabdoulline RR, Menziani MC, De Benedetti PG, Wade RC (2001) Electrostatic analysis and Brownian dynamics simulation of the association of plastocyanin and cytochrome f. Biophys J 81:3090-3104
    • (2001) Biophys J , vol.81 , pp. 3090-3104
    • De Rienzo, F.1    Gabdoulline, R.R.2    Menziani, M.C.3    De Benedetti, P.G.4    Wade, R.C.5
  • 12
    • 0025257610 scopus 로고
    • Modeling of the electrostatic potential field of plastocyanin
    • Durell SR, Labanowski JK, Gross EL. (1990) Modeling of the electrostatic potential field of plastocyanin. Arch Biochem Biophys 277:241-254
    • (1990) Arch Biochem Biophys , vol.277 , pp. 241-254
    • Durell, S.R.1    Labanowski, J.K.2    Gross, E.L.3
  • 13
    • 0039591353 scopus 로고    scopus 로고
    • Side-chain interactions in the plastocyanin-cytochrome f complex
    • Ejdeback M, Bergkvist A, Karlsson BG, Ubbink M (2000) Side-chain interactions in the plastocyanin-cytochrome f complex. Biochemistry 39:5022-5027
    • (2000) Biochemistry , vol.39 , pp. 5022-5027
    • Ejdeback, M.1    Bergkvist, A.2    Karlsson, B.G.3    Ubbink, M.4
  • 14
    • 33750652614 scopus 로고
    • Brownian dynamics with hydrodynamic interactions
    • Ermak DL, McCammon JA (1978) Brownian dynamics with hydrodynamic interactions. J Phys Chem 69:1352-1360
    • (1978) J Phys Chem , vol.69 , pp. 1352-1360
    • Ermak, D.L.1    McCammon, J.A.2
  • 15
    • 0002426686 scopus 로고
    • Electron transfer in "blue" copper proteins
    • Freeman HC (1981). Electron transfer in "blue" copper proteins. Coord Chem 21:29-52
    • (1981) Coord Chem , vol.21 , pp. 29-52
    • Freeman, H.C.1
  • 16
    • 0031714012 scopus 로고    scopus 로고
    • Brownian dynamics simulation of protein-protein diffusional encounter
    • Gabdoulline RR, Wade RC (1998) Brownian dynamics simulation of protein-protein diffusional encounter. Methods 14:329-341
    • (1998) Methods , vol.14 , pp. 329-341
    • Gabdoulline, R.R.1    Wade, R.C.2
  • 17
    • 0000067495 scopus 로고    scopus 로고
    • The role of individual lysine residues in the basic patch on turnip cytochrome f for the electrostatic interactions with plastocyanin in vitro
    • Gong XS, Wen JQ, Fisher NE, Young S, Howe CJ, Bendall DS, Gray JC (2000) The role of individual lysine residues in the basic patch on turnip cytochrome f for the 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
  • 18
    • 0000121207 scopus 로고
    • Cytochrome f: Structure, function and biosynthesis
    • Gray J (1992) Cytochrome f: structure, function and biosynthesis. Photosynth Res 34:359-374
    • (1992) Photosynth Res , vol.34 , pp. 359-374
    • Gray, J.1
  • 19
    • 0002652170 scopus 로고    scopus 로고
    • Plastocyanin: Structure, location, diffusion, electron transfer mechanisms
    • Kluwer Academic Publishers Dordrecht, the Netherlands
    • Gross EL (1996) Plastocyanin: structure, location, diffusion, electron transfer mechanisms. In: Ort D, Yocum C (eds) Oxygenic photosynthesis: the light reactions. Advances in Photosynthesis, vol 4. Kluwer Academic Publishers, Dordrecht, the Netherlands, pp 413-429
    • (1996) Oxygenic Photosynthesis: The Light Reactions. Advances in Photosynthesis , pp. 413-429
    • Gross, E.L.1    Ort, D.2    Yocum, C.3
  • 20
    • 4444261027 scopus 로고    scopus 로고
    • A Brownian dynamics study of the interaction of Phormidium laminosum plastocyanin with Phormidium laminosum cytochrome f
    • Gross EL (2004) A Brownian dynamics study of the interaction of Phormidium laminosum plastocyanin with Phormidium laminosum cytochrome f. Biophys J 87:2043-2059
    • (2004) Biophys J , vol.87 , pp. 2043-2059
    • Gross, E.L.1
  • 21
    • 0042822363 scopus 로고    scopus 로고
    • Brownian dynamics simulations of the interaction of Chlamydomonas cytochrome f with plastocyanin and cytochrome c6
    • Gross EL, Pearson Jr DC (2003) Brownian dynamics simulations of the interaction of Chlamydomonas cytochrome f with plastocyanin and cytochrome c6. Biophys J 85:2055-2068
    • (2003) Biophys J , vol.85 , pp. 2055-2068
    • Gross, E.L.1    Pearson Jr., D.C.2
  • 22
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 24
    • 33646186478 scopus 로고    scopus 로고
    • A Brownian dynamics study of the effects of cytochrome f structure and deletion of its small domain in interactions with cytochrome c6 and plastocyanin in Chlamydomonas reinhardtii
    • Haddadian EJ, Gross EL (2006) A Brownian dynamics study of the effects of cytochrome f structure and deletion of its small domain in interactions with cytochrome c6 and plastocyanin in Chlamydomonas reinhardtii. Biophys J 90:566-577
    • (2006) Biophys J , vol.90 , pp. 566-577
    • Haddadian, E.J.1    Gross, E.L.2
  • 25
    • 0024519351 scopus 로고
    • Treatment of electrostatic effects in macromolecular modeling
    • Harvey SC (1989) Treatment of electrostatic effects in macromolecular modeling. Proteins 5:78-92
    • (1989) Proteins , vol.5 , pp. 78-92
    • Harvey, S.C.1
  • 26
    • 0034598395 scopus 로고    scopus 로고
    • Electron transfers amongst cytochrome f, plastocyanin and photosystemI: Kinetics and mechanisms
    • Hope AB (2000) Electron transfers amongst cytochrome f, plastocyanin and photosystemI: kinetics and mechanisms. Biochim Biophys Acta 1456:5-26
    • (2000) Biochim Biophys Acta , vol.1456 , pp. 5-26
    • Hope, A.B.1
  • 27
    • 0029995705 scopus 로고    scopus 로고
    • The role of acidic residues of plastocyanin in its interaction with cytochrome f
    • Kannt A, Young S, Bendall DS (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
  • 28
    • 0242494128 scopus 로고    scopus 로고
    • Structure of the cytochrome b6f complex of oxygenic photosynthesis: Tuning the cavity
    • Kurisu G, Zhang H, Smith JL, Cramer WA (2003) Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity. Science 302:1009-1013
    • (2003) Science , vol.302 , pp. 1009-1013
    • Kurisu, G.1    Zhang, H.2    Smith, J.L.3    Cramer, W.A.4
  • 29
    • 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, 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
  • 30
    • 0029061465 scopus 로고
    • Site-directed mutagenetic study on the role of negative patches on silene plastocyanin in the interactions with cytochrome f and photosystem I
    • Lee BH, Hibino T, Takabe T, Weisbeek PJ, Takabe T (1995) Site-directed mutagenetic study on the role of negative patches on silene plastocyanin in the interactions with cytochrome f and photosystem I. J Biochem (Tokyo) 117:1209-1217
    • (1995) J Biochem (Tokyo) , vol.117 , pp. 1209-1217
    • Lee, B.H.1    Hibino, T.2    Takabe, T.3    Weisbeek, P.J.4    Takabe, T.5
  • 31
    • 0028773015 scopus 로고
    • Crystal structure of the chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation
    • Martinez SE, Huang D, Szczepaniak A, Cramer WA, Smith JL (1994) Crystal structure of the chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation. Structure 2:95-105
    • (1994) Structure , vol.2 , pp. 95-105
    • Martinez, S.E.1    Huang, D.2    Szczepaniak, A.3    Cramer, W.A.4    Smith, J.L.5
  • 32
    • 0029897140 scopus 로고    scopus 로고
    • The heme redox center of chloroplast cytochrome f is linked to a buried five-water chain
    • Martinez SE, Huang D, Ponomarev M, Cramer WA, Smith JL (1996) The heme redox center of chloroplast cytochrome f is linked to a buried five-water chain. Protein Sci 5:1081-1092
    • (1996) Protein Sci , vol.5 , pp. 1081-1092
    • Martinez, S.E.1    Huang, D.2    Ponomarev, M.3    Cramer, W.A.4    Smith, J.L.5
  • 38
    • 21444431710 scopus 로고    scopus 로고
    • Structure of the intermolecular complex between plastocycanin and cytochrome f from spinach
    • Musiani F, Dikyi A, Semenov AY, Ciurli S (2005) Structure of the intermolecular complex between plastocycanin and cytochrome f from spinach. J Biol Chem 280:18833-18841
    • (2005) J Biol Chem , vol.280 , pp. 18833-18841
    • Musiani, F.1    Dikyi, A.2    Semenov, A.Y.3    Ciurli, S.4
  • 39
    • 84986486656 scopus 로고
    • A rapid finite-difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation
    • Nicholls A, Honig B (1991) A rapid finite-difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation. J Comp Chem 12:435-445
    • (1991) J Comp Chem , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.2
  • 40
    • 0003936136 scopus 로고    scopus 로고
    • Theoretical simulation of protein-protein interactions
    • University Science Publishers Sausalito, CA
    • Northrup SH (1996) Theoretical simulation of protein-protein interactions. In: Scott RA, Mauk AG (eds) Cytochrome c: a multidiciplinary approach. University Science Publishers, Sausalito, CA, pp 543-570
    • (1996) Cytochrome C: A Multidiciplinary Approach , pp. 543-570
    • Northrup, S.H.1    Scott, R.A.2    Mauk, A.G.3
  • 42
    • 33845282908 scopus 로고
    • Electrostatic effects in the Brownian dynamics of association and orientation of heme proteins
    • Northrup SH, Boles JO, Reynolds JCL (1987). Electrostatic effects in the Brownian dynamics of association and orientation of heme proteins. J Phys Chem 91:5991-5998
    • (1987) J Phys Chem , vol.91 , pp. 5991-5998
    • Northrup, S.H.1    Boles, J.O.2    Reynolds, J.C.L.3
  • 43
    • 0024040620 scopus 로고
    • Brownian dynamics of cytochrome c and cytochrome c peroxidase association
    • Northrup SH, Boles JO, Reynolds JC (1988) Brownian dynamics of cytochrome c and cytochrome c peroxidase association. Science 241:67-70
    • (1988) Science , vol.241 , pp. 67-70
    • Northrup, S.H.1    Boles, J.O.2    Reynolds, J.C.3
  • 45
    • 0344474660 scopus 로고    scopus 로고
    • Brownian dynamics study of the interaction between plastocyanin and cytochrome f
    • Pearson DC Jr, Gross EL (1998) Brownian dynamics study of the interaction between plastocyanin and cytochrome f. Biophys J 75:2698-2711
    • (1998) Biophys J , vol.75 , pp. 2698-2711
    • Pearson Jr., D.C.1    Gross, E.L.2
  • 47
    • 0031665392 scopus 로고    scopus 로고
    • Plastocyanin, an electron-transfer protein
    • Sigfridsson K (1998) Plastocyanin, an electron-transfer protein. Photosynth Res 57:1-28
    • (1998) Photosynth Res , vol.57 , pp. 1-28
    • Sigfridsson, K.1
  • 48
    • 0030446029 scopus 로고    scopus 로고
    • Effect of the interdomain basic region of cytochrome f on its redox reactions in vivo
    • Soriano GM, Ponomarev MV, Tae GS, Cramer WA (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    Ponomarev, M.V.2    Tae, G.S.3    Cramer, W.A.4
  • 49
    • 0344497439 scopus 로고    scopus 로고
    • An atypical heme in the cytochrome b(6)f complex
    • Stroebel D, Choquet Y, Popot JL, Picot D (2003) An atypical heme in the cytochrome b(6)f complex. Nature 426:413-418
    • (2003) Nature , vol.426 , pp. 413-418
    • Stroebel, D.1    Choquet, Y.2    Popot, J.L.3    Picot, D.4
  • 50
    • 0000211392 scopus 로고
    • Plastocyanin and the blue copper proteins
    • Sykes AG (1991) Plastocyanin and the blue copper proteins. Struct Bond 75:175-224
    • (1991) Struct Bond , vol.75 , pp. 175-224
    • Sykes, A.G.1
  • 51
    • 4043055221 scopus 로고    scopus 로고
    • Complexes of photosynthetic redox proteins studied by NMR
    • Ubbink M (2004) Complexes of photosynthetic redox proteins studied by NMR. Photosynth Res 81:277-287
    • (2004) Photosynth Res , vol.81 , pp. 277-287
    • Ubbink, M.1
  • 52
    • 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, Ejdebäck M, Karlsson BG, Bendall DS (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    Ejdebäck, M.2    Karlsson, B.G.3    Bendall, D.S.4
  • 53
    • 0020475509 scopus 로고
    • Calculation of the electric potential in the active site cleft due to alpha-helix dipoles
    • Warwicker J, Watson HC (1982) Calculation of the electric potential in the active site cleft due to alpha-helix dipoles. J Mol Biol 157:671-679
    • (1982) J Mol Biol , vol.157 , pp. 671-679
    • Warwicker, J.1    Watson, H.C.2
  • 54
    • 0031732147 scopus 로고    scopus 로고
    • Crystal structure of spinach plastocyanin at 1.7 Å resolution
    • Xue Y, Okvist M, Hansson O, Young S (1998) Crystal structure of spinach plastocyanin at 1.7 Å resolution. Protein Sci 7:2099-2105
    • (1998) Protein Sci , vol.7 , pp. 2099-2105
    • Xue, Y.1    Okvist, M.2    Hansson, O.3    Young, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.