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Volumn 85, Issue 3, 2003, Pages 2055-2068

Brownian dynamics simulations of the interaction of Chlamydomonas cytochrome f with plastocyanin and cytochrome c6

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; CYTOCHROME C6; CYTOCHROME F; PLASTOCYANIN; UNCLASSIFIED DRUG;

EID: 0042822363     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74633-5     Document Type: Article
Times cited : (40)

References (70)
  • 3
    • 0024293340 scopus 로고
    • Structure of azurin from Alcaligenes denitrificans: Refinement at 1.8 Å resolution and comparison of the two crystallographically independent molecules
    • Baker, E. N. 1988. Structure of azurin from Alcaligenes denitrificans: refinement at 1.8 Å resolution and comparison of the two crystallographically independent molecules. J. Mol. Biol. 203:1071-1095.
    • (1988) J. Mol. Biol. , vol.203 , pp. 1071-1095
    • Baker, E.N.1
  • 4
    • 0002591183 scopus 로고    scopus 로고
    • Interprotein electron transfer
    • D. S. Bendall, editor. Bios. Scientific Publisher, Oxford, UK
    • Bendall, D. S. 1996. Interprotein electron transfer. In Protein Electron Transfer, D. S. Bendall, editor. Bios. Scientific Publisher, Oxford, UK. 43-68.
    • (1996) Protein Electron Transfer , pp. 43-68
    • Bendall, D.S.1
  • 6
    • 0034604237 scopus 로고    scopus 로고
    • X-ray structure of a truncated form of cytochrome f from chlamydomonas reinhardtii
    • Chi, Y. I., L. S. Huang, Z. Zhang, J. G. Fernandez-Velasco, and E. A. Berry. 2000. X-ray structure of a truncated form of cytochrome f from chlamydomonas reinhardtii. Biochemistry. 39:7689-7701.
    • (2000) Biochemistry , vol.39 , pp. 7689-7701
    • Chi, Y.I.1    Huang, L.S.2    Zhang, Z.3    Fernandez-Velasco, J.G.4    Berry, E.A.5
  • 8
    • 0030468363 scopus 로고    scopus 로고
    • Effect of mutations in plastocyanin on the kinetics of the protein rearrangement gating the electron-transfer reaction with zinc cytochrome c. Analysis of the rearrangement pathway
    • Crnogorac, M. M., C. Shen, S. Young, O. Hansson, and N. M. Kostic. 1996. Effect of mutations in plastocyanin on the kinetics of the protein rearrangement gating the electron-transfer reaction with zinc cytochrome c. Analysis of the rearrangement pathway. Biochemistry. 35:16465-16474.
    • (1996) Biochemistry , vol.35 , pp. 16465-16474
    • Crnogorac, M.M.1    Shen, C.2    Young, S.3    Hansson, O.4    Kostic, N.M.5
  • 9
    • 0035204346 scopus 로고    scopus 로고
    • Electrostatic analysis and Brownian dynamics simulation of the association of plastocyanin and cytochrome f
    • De Rienzo, F., R. R. Gabdoulline, M. C. Menziani, P. G. De Benedetti, and R. C. Wade. 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
  • 10
    • 0025257610 scopus 로고
    • Modeling the electrostatic potential field of plastocyanin
    • Durell, S. R., J. K. Labanowski, and E. L. Gross. 1990. Modeling 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
  • 11
    • 0039591353 scopus 로고    scopus 로고
    • Side-chain interactions in the plastocyanin-cytochrome f complex
    • Ejdeback, M., A. Bergkvist, B. G. Karlsson, and M. Ubbink. 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
  • 12
    • 0344500752 scopus 로고    scopus 로고
    • Computer simulation of protein-protein kinetics: Acetylcholinesterase-fasciculin
    • Elcock, A. H., R. R. Gabdoulline, R. C. Wade, and J. A. McCammon. 1999. Computer simulation of protein-protein kinetics: acetylcholinesterase-fasciculin. J. Mol. Biol. 291:149-162.
    • (1999) J. Mol. Biol. , vol.291 , pp. 149-162
    • Elcock, A.H.1    Gabdoulline, R.R.2    Wade, R.C.3    McCammon, J.A.4
  • 13
    • 0002426686 scopus 로고
    • Electron transfer in "blue" copper proteins
    • Freeman, H. C. 1981. Electron transfer in "blue" copper proteins. Coord. Chem. 21:29-52.
    • (1981) Coord. Chem. , vol.21 , pp. 29-52
    • Freeman, H.C.1
  • 14
    • 33748501925 scopus 로고    scopus 로고
    • Effective charges for macromolecules in solvent
    • Gabdoulline, R. R., and R. C. Wade. 1996. Effective charges for macromolecules in solvent. J. Phys. Chem. 100:3868-3878.
    • (1996) J. Phys. Chem. , vol.100 , pp. 3868-3878
    • Gabdoulline, R.R.1    Wade, R.C.2
  • 15
    • 0031714012 scopus 로고    scopus 로고
    • Brownian dynamics simulation of protein-protein diffusional encounter
    • Gabdoulline, R. R., and R. C. Wade. 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
  • 16
    • 0035830963 scopus 로고    scopus 로고
    • Protein-protein association: Investigation of factors influencing association rates by Brownian dynamics simulations
    • Gabdoulline, R. R., and R. C. Wade. 2001. Protein-protein association: investigation of factors influencing association rates by Brownian dynamics simulations. J. Mol. Biol. 9:1139-1155.
    • (2001) J. Mol. Biol. , vol.9 , pp. 1139-1155
    • 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, X. S., J. Q. Wen, N. E. Fisher, S. Young, C. J. Howe, D. S. Bendall, and J. C. Gray. 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. C. 1992. Cytochrome f: structure, function and biosynthesis. Photosynth. Res. 34:359-374.
    • (1992) Photosynth. Res. , vol.34 , pp. 359-374
    • Gray, J.C.1
  • 19
    • 0000303843 scopus 로고
    • Plastocyanin: Structure and function
    • Gross, E. L. 1993. Plastocyanin: structure and function. Photosynth. Res. 37:103-116.
    • (1993) Photosynth. Res. , vol.37 , pp. 103-116
    • Gross, E.L.1
  • 20
    • 0002652170 scopus 로고    scopus 로고
    • Plastocyanin: Structure, location, diffusion, and electron transfer mechanisms
    • D. Ort and C. Yocum, editors. Kluwer Academic Publishers, Dordrecht, the Netherlands
    • Gross, E. L. 1996. Plastocyanin: structure, location, diffusion, and electron transfer mechanisms. In Oxygenic Photosynthesis: The Light Reactions. D. Ort and C. Yocum, editors. Kluwer Academic Publishers, Dordrecht, the Netherlands. 413-429.
    • (1996) Oxygenic Photosynthesis: The Light Reactions , pp. 413-429
    • Gross, E.L.1
  • 22
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N., and M. C. Peitsch. 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
  • 23
    • 0000580222 scopus 로고
    • Accuracy and precision in protein structure analysis: Restrained least-squares refinement of the structure of poplar plastocyanin at 1.33 Å resolution
    • Guss, J. M., H. D. Bartunik, and H. C. Freeman. 1992. Accuracy and precision in protein structure analysis: restrained least-squares refinement of the structure of poplar plastocyanin at 1.33 Å resolution. Acta Crystallogr. B. 48:790-811.
    • (1992) Acta Crystallogr. B , vol.48 , pp. 790-811
    • Guss, J.M.1    Bartunik, H.D.2    Freeman, H.C.3
  • 24
    • 0024519351 scopus 로고
    • Treatment of electrostatic effects in macromolecular modeling
    • Harvey, S. C. 1989. Treatment of electrostatic effects in macromolecular modeling. Proteins. 5:78-92.
    • (1989) Proteins , vol.5 , pp. 78-92
    • Harvey, S.C.1
  • 25
    • 0021104440 scopus 로고
    • Comparative aspects of the quinol-cytochrome c/plastocyanin oxidoreductases
    • Hauska, G., E. Hurt, N. Gabellini, and W. Lockau. 1983. Comparative aspects of the quinol-cytochrome c/plastocyanin oxidoreductases. Biochim. Biophys. Acta. 726:97-133.
    • (1983) Biochim. Biophys. Acta , vol.726 , pp. 97-133
    • Hauska, G.1    Hurt, E.2    Gabellini, N.3    Lockau, W.4
  • 26
    • 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
  • 27
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin, J., and C. Chothia. 1990. The structure of protein-protein recognition sites. J. Biol. Chem. 265:16027-16030.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 28
    • 0029995705 scopus 로고    scopus 로고
    • The role of acidic residues of plastocyanin in its interaction with cytochrome f
    • Kannt, A., S. Young, and D. S. Bendall. 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
  • 29
    • 0029154240 scopus 로고
    • The structure of chloroplast cytochrome c6 at 1.9 Å resolution: Evidence for functional oligomerization
    • Kerfeld, C. A., H. P. Anwar, R. Interrante, S. Merchant, and T. O. Yeates. 1995. The structure of chloroplast cytochrome c6 at 1.9 Å resolution: evidence for functional oligomerization. J. Mol. Biol. 250:627-647.
    • (1995) J. Mol. Biol. , vol.250 , pp. 627-647
    • Kerfeld, C.A.1    Anwar, H.P.2    Interrante, R.3    Merchant, S.4    Yeates, T.O.5
  • 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, B. H., T. Hibino, T. Takabe, P. J. Weisbeek, and T. Takabe. 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
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B., and F. M. Richards. 1971. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55:379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 32
    • 0028773015 scopus 로고
    • Crystal structure of the chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation
    • Martinez, S. E., D. Huang, A. Szczepaniak, W. A. Cramer, and J. L. Smith. 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
  • 33
    • 0029897140 scopus 로고    scopus 로고
    • The heme redox center of chloroplast cytochrome f is linked to a buried five-water chain
    • Martinez, S. E., D. Huang, M. Ponomarev, W. A. Cramer, and J. L. Smith. 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
  • 36
    • 0022641081 scopus 로고
    • Regulation by copper of the expression of plastocyanin and cytochrome c552 in Chlamydomonas reinhardii
    • Merchant, S., and L. Bogorad. 1986. Regulation by copper of the expression of plastocyanin and cytochrome c552 in Chlamydomonas reinhardii. Mol. Cell. Biol. 6:462-469.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 462-469
    • Merchant, S.1    Bogorad, L.2
  • 37
    • 0027319734 scopus 로고
    • Transient kinetics of electron transfer from a variety of c-type cytochromes to plastocyanin
    • Meyer, T. E., Z. G. Zhao, M. A. Cusanovich, and G. Tollin. 1993. Transient kinetics of electron transfer from a variety of c-type cytochromes to plastocyanin. Biochemistry. 32:4552-4559.
    • (1993) Biochemistry , vol.32 , pp. 4552-4559
    • Meyer, T.E.1    Zhao, Z.G.2    Cusanovich, M.A.3    Tollin, G.4
  • 41
    • 0043134192 scopus 로고    scopus 로고
    • The interaction of plastocyanin with cytochrome f: A Brownian dynamics study
    • G. Garab, editor. Kluwer Academic Publishers, Dordrecht, the Netherlands
    • Nelson, N., D. C. Pearson, Jr., and E. L. Gross. 1999. The interaction of plastocyanin with cytochrome f: a Brownian dynamics study. In Photosynthesis: Mechanisms and Effects, Vol. 3. G. Garab, editor. Kluwer Academic Publishers, Dordrecht, the Netherlands. 1493-1498.
    • (1999) Photosynthesis: Mechanisms and Effects , vol.3 , pp. 1493-1498
    • Nelson, N.1    Pearson D.C., Jr.2    Gross, E.L.3
  • 42
    • 84986486656 scopus 로고
    • A rapid finite-difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation
    • Nicholls, A., and B. Honig. 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
  • 43
    • 33845282908 scopus 로고
    • Electrostatic effects in the Brownian dynamics of association and orientation of heme proteins
    • Northrup, S. H., J. O. Boles, and J. C. L. Reynolds. 1987a. 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
  • 45
    • 0024040620 scopus 로고
    • Brownian dynamics of cytochrome c and cytochrome c peroxidase association
    • Northrup, S. H., J. O. Boles, and J. C. Reynolds. 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
  • 47
    • 0003936136 scopus 로고    scopus 로고
    • Theoretical simulation of protein-protein interactions
    • R. A. Scott and A. G. Mauk, editors. University Science Publishers, Sausalito, CA
    • Northrup, S. H. 1996. Theoretical simulation of protein-protein interactions. In Cytochrome c: A Multidiciplinary Approach. R. A. Scott and A. G. Mauk, editors. University Science Publishers, Sausalito, CA. 543-570.
    • (1996) Cytochrome c: A Multidiciplinary Approach , pp. 543-570
    • Northrup, S.H.1
  • 49
    • 8944236999 scopus 로고    scopus 로고
    • The electrostatic properties of cytochrome f: Implications for docking with plastocyanin
    • Pearson, D. C., Jr., E. L. Gross, and E. S. David. 1996. The electrostatic properties of cytochrome f: implications for docking with plastocyanin. Biophys. J. 71:64-76.
    • (1996) Biophys. J. , vol.71 , pp. 64-76
    • Pearson D.C., Jr.1    Gross, E.L.2    David, E.S.3
  • 50
    • 0344474660 scopus 로고    scopus 로고
    • Brownian dynamics study of the interaction between plastocyanin and cytochrome f
    • Pearson, D. C., Jr., and E. L. Gross. 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 D.C., Jr.1    Gross, E.L.2
  • 52
    • 0026628159 scopus 로고
    • Electron-transfer reactions of cytochrome f with flavin semiquinones and with plastocyanin. Importance of protein-protein electrostatic interactions and of donor-acceptor coupling
    • Qin, L., and N. M. Kostic. 1992. Electron-transfer reactions of cytochrome f with flavin semiquinones and with plastocyanin. Importance of protein-protein electrostatic interactions and of donor-acceptor coupling. Biochemistry. 31:5145-5150.
    • (1992) Biochemistry , vol.31 , pp. 5145-5150
    • Qin, L.1    Kostic, N.M.2
  • 53
    • 0027263613 scopus 로고
    • Importance of protein rearrangements in the electron-transfer reaction between the physiological partners cytochrome f and plastocyanin
    • Qin, L., and N. M. Kostic. 1993. Importance of protein rearrangements in the electron-transfer reaction between the physiological partners cytochrome f and plastocyanin. Biochemistry. 32:6073-6080.
    • (1993) Biochemistry , vol.32 , pp. 6073-6080
    • Qin, L.1    Kostic, N.M.2
  • 54
    • 0027340169 scopus 로고
    • The 1.5-Å crystal structure of plastocyanin from the green alga Chlamydomonas reinhardtii
    • Redinbo, M. R., D. Cascio, M. K. Choukair, D. Rice, S. Merchant, and T. O. Yeates. 1993. The 1.5-Å crystal structure of plastocyanin from the green alga Chlamydomonas reinhardtii. Biochemistry. 32:10560-10567.
    • (1993) Biochemistry , vol.32 , pp. 10560-10567
    • Redinbo, M.R.1    Cascio, D.2    Choukair, M.K.3    Rice, D.4    Merchant, S.5    Yeates, T.O.6
  • 56
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • Richards, F. M. 1977. Areas, volumes, packing and protein structure. Annu. Rev. Biophys. Bioeng. 6:151-176.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 57
    • 0027256739 scopus 로고
    • Hydrogen bonding, hydrophobicity, packing and protein folding
    • Rose, G. D., and R. Wolfenden. 1993. Hydrogen bonding, hydrophobicity, packing and protein folding. Annu. Rev. Biophys. Biomol. Struct. 22: 381-415.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 381-415
    • Rose, G.D.1    Wolfenden, R.2
  • 58
    • 0026416668 scopus 로고
    • Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects
    • Sharp, K. A., A. Nicholls, R. F. Fine, and B. Honig. 1991. Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects. Science. 252:106-109.
    • (1991) Science , vol.252 , pp. 106-109
    • Sharp, K.A.1    Nicholls, A.2    Fine, R.F.3    Honig, B.4
  • 59
    • 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
  • 60
    • 0030446029 scopus 로고    scopus 로고
    • Effect of the interdomain basic region of cytochrome f on its redox reactions in vivo
    • Soriano, G. M., M. V. Ponomarev, G. S. Tae, and W. A. Cramer. 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
  • 61
    • 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., M. V. Pomamarev, R. A. Piskorowski, and W. A. Cramer. 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    Pomamarev, M.V.2    Piskorowski, R.A.3    Cramer, W.A.4
  • 62
    • 0000211392 scopus 로고
    • Plastocyanin and the blue copper proteins
    • Sykes, A. G. 1991. Plastocyanin and the blue copper proteins. Struct. Bond. 75:175-224.
    • (1991) Struct. Bond. , vol.75 , pp. 175-224
    • Sykes, A.G.1
  • 63
    • 0022685115 scopus 로고
    • Charges on proteins and distances of electron transfer in metalloprotein redox reactions
    • Takabe, T., K. Takenaka, H. Kawamura, and Y. Beppu. 1986. Charges on proteins and distances of electron transfer in metalloprotein redox reactions. J. Biochem. (Tokyo). 99:833-840.
    • (1986) J. Biochem. (Tokyo) , vol.99 , pp. 833-840
    • Takabe, T.1    Takenaka, K.2    Kawamura, H.3    Beppu, Y.4
  • 64
    • 0021738121 scopus 로고
    • Importance of local positive charges on cytochrome f for electron transfer to plastocyanin and potassium ferricyanide
    • Takenaka, K., and T. Takabe. 1984. Importance of local positive charges on cytochrome f for electron transfer to plastocyanin and potassium ferricyanide. J. Biochem. (Tokyo). 96:1813-1821.
    • (1984) J. Biochem. (Tokyo) , vol.96 , pp. 1813-1821
    • Takenaka, K.1    Takabe, T.2
  • 65
    • 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., M. Ejdebäck, B. G. Karlsson, and D. S. Bendall. 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
  • 67
    • 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., E.-W. Knapp, and N. M. Kostic. 1997b. 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
  • 68
    • 0031732147 scopus 로고    scopus 로고
    • Crystal structure of spinach plastocyanin at 1.7 Å resolution
    • Xue, Y., M. Okvist, O. Hansson, and S. Young. 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
  • 69
    • 0020475509 scopus 로고
    • Calculation of the electric potential in the active site cleft due to alpha-helix dipoles
    • Warwicker, J., and H. C. Watson. 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
  • 70
    • 0029928149 scopus 로고    scopus 로고
    • N-terminal mutants of chloroplast cytochrome f: Effect on redox reactions and growth in Chlamydomonas reinhardtii
    • Zhou, J., J. G. Fernandez-Velasco, and R. Malkin. 1996. N-terminal mutants of chloroplast cytochrome f: effect on redox reactions and growth in Chlamydomonas reinhardtii. J. Biol. Chem. 271:6225-6232.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6225-6232
    • Zhou, J.1    Fernandez-Velasco, J.G.2    Malkin, R.3


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