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Volumn 74, Issue 6, 1998, Pages 3226-3240

Effects of temperature and ΔG°on electron transfer from cytochrome c2 to the photosynthetic reaction center of the purple bacterium Rhodobacter sphaeroides

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C2; CYTOCHROME C;

EID: 0031595249     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)78029-4     Document Type: Article
Times cited : (40)

References (56)
  • 2
    • 0008198152 scopus 로고
    • Macroscopic and microscopic estimates of the energetics of charge separation in bacterial reaction centers
    • M.-E. Michel-Beyerle, editor. Springer-Verlag, Berlin
    • Alden, R. G., W. W. Parson, Z. T. Chu, and A. Warshel. 1995. Macroscopic and microscopic estimates of the energetics of charge separation in bacterial reaction centers. In The Reaction Center of Photosynthetic Bacteria. Structure and Dynamics. M.-E. Michel-Beyerle, editor. Springer-Verlag, Berlin. 105-116.
    • (1995) The Reaction Center of Photosynthetic Bacteria. Structure and Dynamics , pp. 105-116
    • Alden, R.G.1    Parson, W.W.2    Chu, Z.T.3    Warshel, A.4
  • 3
    • 0023408258 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: The protein subunits
    • Allen, J. P., G. Feher, T. O. Yeates, H. Komiya, and D. C. Rees. 1987. Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits. Proc. Natl. Acad. Sci. USA. 84:6162-6166.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6162-6166
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komiya, H.4    Rees, D.C.5
  • 5
    • 0026719686 scopus 로고
    • Global analysis of biochemical and biophysical data
    • Beechem, J. M. 1992. Global analysis of biochemical and biophysical data. Methods Enzymol. 210:37-54.
    • (1992) Methods Enzymol. , vol.210 , pp. 37-54
    • Beechem, J.M.1
  • 6
    • 0026434593 scopus 로고
    • Protein electron transfer rates set by the bridging secondary and tertiary structure
    • Beratan, D. N., J. N. Betts, and J. N. Onuchic. 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
  • 7
    • 0001878505 scopus 로고
    • Application of electron transfer theories to biological systems
    • Bertrand, P. 1991. Application of electron transfer theories to biological systems. Structure Bond. 75:1-47.
    • (1991) Structure Bond. , vol.75 , pp. 1-47
    • Bertrand, P.1
  • 9
    • 0025280515 scopus 로고
    • Mechanisms of long-distance electron transfer in proteins: Lessons from photosynthetic reaction centers
    • Boxer, S. G. 1990. Mechanisms of long-distance electron transfer in proteins: lessons from photosynthetic reaction centers. Annu. Rev. Biophys. Biophys. Chem. 19:267-299.
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 267-299
    • Boxer, S.G.1
  • 10
    • 0001539904 scopus 로고
    • On the action of cytochrome c: Correlating geometry changes upon oxidation with activation energies of electron transfer
    • Churg, A. K., R. M. Weiss, A. Warshel, and T. Takano. 1983. On the action of cytochrome c: correlating geometry changes upon oxidation with activation energies of electron transfer. J. Phys. Chem. 87: 1683-1694.
    • (1983) J. Phys. Chem. , vol.87 , pp. 1683-1694
    • Churg, A.K.1    Weiss, R.M.2    Warshel, A.3    Takano, T.4
  • 12
    • 0031019803 scopus 로고    scopus 로고
    • 2 and the photosynthetic reaction center of Rhodobacter sphaeroides
    • 2 and the photosynthetic reaction center of Rhodobacter sphaeroides. Biochemistry. 36:1418-1427.
    • (1997) Biochemistry , vol.36 , pp. 1418-1427
    • Drepper, F.1    Dorlet, P.2    Mathis, P.3
  • 13
    • 0031033675 scopus 로고    scopus 로고
    • 2 in electron transfer complexes with the photosynthetic reaction center of Rhodobacter sphaeroides: Optical linear dichroism and EPR
    • 2 in electron transfer complexes with the photosynthetic reaction center of Rhodobacter sphaeroides: optical linear dichroism and EPR. Biochemistry. 36:1428-1440.
    • (1997) Biochemistry , vol.36 , pp. 1428-1440
    • Drepper, F.1    Mathis, P.2
  • 15
    • 0002653186 scopus 로고
    • A in reaction centers from Rhodobacter sphaeroides R-26
    • J. Breton and A. Vermeglio, editors. Plenum, New York
    • A in reaction centers from Rhodobacter sphaeroides R-26. In The Photosynthetic Bacterial Reaction Center. J. Breton and A. Vermeglio, editors. Plenum, New York. 271-287.
    • (1988) The Photosynthetic Bacterial Reaction Center , pp. 271-287
    • Feher, G.1    Arno, T.R.2    Okamura, M.Y.3
  • 16
    • 0028773469 scopus 로고
    • Comparison of theory and experiment for electron transfers in proteins: Where's the beef?
    • Friesner, R. A. 1994. Comparison of theory and experiment for electron transfers in proteins: where's the beef? Structure. 2:239-343.
    • (1994) Structure , vol.2 , pp. 239-343
    • Friesner, R.A.1
  • 19
    • 0025944990 scopus 로고
    • Electrostatic control of midpoint potentials in the cytochrome subunit of the Rhodopseudomonas viridis reaction center
    • Gunner, M. R., and B. Honig. 1991. Electrostatic control of midpoint potentials in the cytochrome subunit of the Rhodopseudomonas viridis reaction center. Proc. Natl. Acad. Sci. USA. 88:9151-9155.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9151-9155
    • Gunner, M.R.1    Honig, B.2
  • 20
    • 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
  • 21
    • 0016273342 scopus 로고
    • Electron transfer between biological molecules by thermally activated tunneling
    • Hopfield, J. 1974. Electron transfer between biological molecules by thermally activated tunneling. Proc. Natl. Acad. Sci. USA. 71: 3640-3644.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 3640-3644
    • Hopfield, J.1
  • 22
    • 36749105258 scopus 로고
    • Temperature dependent activation energy for electron transfer between biological molecules
    • Jortner, J. 1976. Temperature dependent activation energy for electron transfer between biological molecules. J. Chem. Phys. 64:4860-4867.
    • (1976) J. Chem. Phys. , vol.64 , pp. 4860-4867
    • Jortner, J.1
  • 23
    • 0028773475 scopus 로고
    • Electron transfer in cytochrome c depends upon the structure of the intervening medium
    • Karpishin, T. B., M. W. Grinstaff, S. Komar-Panicucci, G. McLendon, and H. B. Gray. 1994. Electron transfer in cytochrome c depends upon the structure of the intervening medium. Structure. 2:415-422.
    • (1994) Structure , vol.2 , pp. 415-422
    • Karpishin, T.B.1    Grinstaff, M.W.2    Komar-Panicucci, S.3    McLendon, G.4    Gray, H.B.5
  • 24
    • 0023180298 scopus 로고
    • Electron tunneling paths in proteins
    • Kuki, A., and P. G. Wolynes. 1987. Electron tunneling paths in proteins. Science. 236:1647-1652.
    • (1987) Science , vol.236 , pp. 1647-1652
    • Kuki, A.1    Wolynes, P.G.2
  • 25
    • 0028000028 scopus 로고
    • Specific alteration of the oxidation potential of the electron donor in reaction centers from Rhodobacter sphaeroides
    • Lin, X., H. A. Murchison, V. Nagarajan, W. W. Parson, J. P. Allen, and J. C. Williams. 1994a. Specific alteration of the oxidation potential of the electron donor in reaction centers from Rhodobacter sphaeroides. Proc. Natl. Acad. Sci. USA. 91:10265-10269.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10265-10269
    • Lin, X.1    Murchison, H.A.2    Nagarajan, V.3    Parson, W.W.4    Allen, J.P.5    Williams, J.C.6
  • 27
    • 0024976545 scopus 로고
    • 2 to the Rhodobacter sphaeroides reaction center in optimal orientation for rapid electron transfer
    • 2 to the Rhodobacter sphaeroides reaction center in optimal orientation for rapid electron transfer. Biochemistry. 28:6970-6974.
    • (1989) Biochemistry , vol.28 , pp. 6970-6974
    • Long, J.E.1    Durham, B.2    Okamura, M.3    Millett, F.4
  • 28
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • Marcus, R. A., and N. Sutin. 1985. Electron transfers in chemistry and biology. Biochim. Biophys. Acta. 811:265-322.
    • (1985) Biochim. Biophys. Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 29
    • 0028130330 scopus 로고
    • Interaction between cytochrome c and the photosynthetic reaction center of purple bacteria: Behaviour at low temperature
    • Mathis, P., J. M. Ortega, and G. Venturoli. 1994. Interaction between cytochrome c and the photosynthetic reaction center of purple bacteria: behaviour at low temperature. Biochimie. 76:569-579.
    • (1994) Biochimie. , vol.76 , pp. 569-579
    • Mathis, P.1    Ortega, J.M.2    Venturoli, G.3
  • 30
    • 0028351917 scopus 로고
    • Changes in primary donor hydrogen-bonding interactions in mutant reaction centers from Rhodobacter sphaeroides: Identification of vibrational frequencies of all the conjugated carbonyl groups
    • Mattioli, T. A., J. C. Williams, J. P. Allen, and B. Robert. 1994. Changes in primary donor hydrogen-bonding interactions in mutant reaction centers from Rhodobacter sphaeroides: identification of vibrational frequencies of all the conjugated carbonyl groups. Biochemistry. 33: 1636-1643.
    • (1994) Biochemistry , vol.33 , pp. 1636-1643
    • Mattioli, T.A.1    Williams, J.C.2    Allen, J.P.3    Robert, B.4
  • 31
    • 0345318403 scopus 로고
    • Long-distance electron transfer in proteins and model systems
    • McLendon, G. 1988. Long-distance electron transfer in proteins and model systems. Acc. Chem. Res. 21:160-167.
    • (1988) Acc. Chem. Res. , vol.21 , pp. 160-167
    • McLendon, G.1
  • 32
    • 0001594374 scopus 로고
    • Interprotein electron transfer
    • McLendon, G., and R. Hake. 1992. Interprotein electron transfer. Chem. Rev. 92:481-490.
    • (1992) Chem. Rev. , vol.92 , pp. 481-490
    • McLendon, G.1    Hake, R.2
  • 34
    • 0000614078 scopus 로고
    • Driving-force effects on the rate of long-range electron transfer in ruthenium-modified cytochrome c
    • Meade, T. J., H. B. Gray, and J. R. Winkler. 1989. Driving-force effects on the rate of long-range electron transfer in ruthenium-modified cytochrome c. J. Am. Chem. Soc. 111:4353-4356.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 4353-4356
    • Meade, T.J.1    Gray, H.B.2    Winkler, J.R.3
  • 38
    • 0004273538 scopus 로고
    • Morgan-Grampian, London
    • Newman, A. A. 1968. Glycerol. Morgan-Grampian, London.
    • (1968) Glycerol
    • Newman, A.A.1
  • 39
    • 0031025928 scopus 로고    scopus 로고
    • Very fast electron transfer from cytochrome to the bacterial photosynthetic reaction center at low temperature
    • Ortega, J. M., B. Dohse, D. Oesterhelt, and P. Mathis. 1997. Very fast electron transfer from cytochrome to the bacterial photosynthetic reaction center at low temperature. FEBS Lett. 401:153-157.
    • (1997) FEBS Lett. , vol.401 , pp. 153-157
    • Ortega, J.M.1    Dohse, B.2    Oesterhelt, D.3    Mathis, P.4
  • 40
    • 0027535989 scopus 로고
    • Electron transfer from the tetraheme cytochrome to the special pair in isolated reaction centers of Rhodopseudomonas viridis
    • Ortega, J. M., and P. Mathis. 1993. Electron transfer from the tetraheme cytochrome to the special pair in isolated reaction centers of Rhodopseudomonas viridis. Biochemistry. 32:1141-1151.
    • (1993) Biochemistry , vol.32 , pp. 1141-1151
    • Ortega, J.M.1    Mathis, P.2
  • 41
    • 0029940149 scopus 로고    scopus 로고
    • Temperature dependence of the reorganization energy for charge recombination in the reaction center from Rhodobacter sphaeroides
    • Ortega, J. M., P. Mathis, J. C. Williams, and J. P. Allen. 1996. Temperature dependence of the reorganization energy for charge recombination in the reaction center from Rhodobacter sphaeroides. Biochemistry. 35: 3354-3361.
    • (1996) Biochemistry , vol.35 , pp. 3354-3361
    • Ortega, J.M.1    Mathis, P.2    Williams, J.C.3    Allen, J.P.4
  • 42
    • 0018523407 scopus 로고
    • 2 from Rhodopseudomonas sphaeroides: In vivo and solution studies
    • 2 from Rhodopseudomonas sphaeroides: in vivo and solution studies. FEBS Lett. 105:137-142.
    • (1979) FEBS Lett. , vol.105 , pp. 137-142
    • Overfield, R.E.1    Wraight, C.A.2    DeVault, D.3
  • 43
    • 0001099869 scopus 로고
    • The electron input to cytochrome c oxidase from cytochrome c
    • Pan, L., J. T. Hazzard, J. Lin, G. Tollin, and S. I. Chan. 1991. The electron input to cytochrome c oxidase from cytochrome c. J. Am. Chem. Soc. 113:5908-5910.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5908-5910
    • Pan, L.1    Hazzard, J.T.2    Lin, J.3    Tollin, G.4    Chan, S.I.5
  • 44
    • 0001256325 scopus 로고
    • Theoretical analyses of electron transfer reactions
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer, editors. Kluwer Academic Publishers, Dordrecht, the Netherlands
    • Parson, W. W., and A. Warshel. 1995. Theoretical analyses of electron transfer reactions. In Anoxygenic Photosynthetic Bacteria. R. E. Blankenship, M. T. Madigan, and C. E. Bauer, editors. Kluwer Academic Publishers, Dordrecht, the Netherlands. 559-575.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 559-575
    • Parson, W.W.1    Warshel, A.2
  • 48
    • 0029012645 scopus 로고
    • ENDOR studies of the primary donor cation radical in mutant reaction centers of Rhodobacter sphaeroides with altered hydrogen-bond interactions
    • Rautter, J., F. Lendzian, C. Shulz, A. Fetsch, M. Kuhn, X. Lin, J. C. Williams, J. P. Allen, and W. Lubitz. 1995. ENDOR studies of the primary donor cation radical in mutant reaction centers of Rhodobacter sphaeroides with altered hydrogen-bond interactions. Biochemistry. 34: 8130-8143.
    • (1995) Biochemistry , vol.34 , pp. 8130-8143
    • Rautter, J.1    Lendzian, F.2    Shulz, C.3    Fetsch, A.4    Kuhn, M.5    Lin, X.6    Williams, J.C.7    Allen, J.P.8    Lubitz, W.9
  • 50
    • 0023106194 scopus 로고
    • Cytochrome c orientation in electron-transfer complexes with photosynthetic reaction centers of Rhodobacter sphaeroides and when bound to the surface of negatively charged membranes: Characterization by optical linear dichroism
    • Tiede, D. M. 1987. Cytochrome c orientation in electron-transfer complexes with photosynthetic reaction centers of Rhodobacter sphaeroides and when bound to the surface of negatively charged membranes: characterization by optical linear dichroism. Biochemistry. 26:397-410.
    • (1987) Biochemistry , vol.26 , pp. 397-410
    • Tiede, D.M.1
  • 51
    • 0343598172 scopus 로고
    • Symmetry breaking structures involved in the docking of cytochrome c and primary electron transfer in reaction centers of Rhodobacter sphaeroides
    • The Photosynthetic Bacterial Reaction Center: Structure and Dynamics J. Breton and A. Vermeglio, editors. Plenum Press, New York
    • Tiede, D. M., D. E. Budil, J. Tang, O. El-Kabbani, J. R. Norris, C. H. Chang, and M. Schiffer. 1988. Symmetry breaking structures involved in the docking of cytochrome c and primary electron transfer in reaction centers of Rhodobacter sphaeroides. In The Photosynthetic Bacterial Reaction Center: Structure and Dynamics. NATO ASI Sries A: Life Sciences, Vol. 149. J. Breton and A. Vermeglio, editors. Plenum Press, New York. 13-20.
    • (1988) NATO ASI Sries A: Life Sciences , vol.149 , pp. 13-20
    • Tiede, D.M.1    Budil, D.E.2    Tang, J.3    El-Kabbani, O.4    Norris, J.R.5    Chang, C.H.6    Schiffer, M.7
  • 52
    • 85005716828 scopus 로고
    • The cytochrome c binding surface of reaction centers from Rhodobacter sphaeroides
    • Tiede, D. M., and C. H. Chang. 1988. The cytochrome c binding surface of reaction centers from Rhodobacter sphaeroides. Isr. J. Chem. 28: 183-191.
    • (1988) Isr. J. Chem. , vol.28 , pp. 183-191
    • Tiede, D.M.1    Chang, C.H.2
  • 53
    • 0000919603 scopus 로고
    • Electron transfer between bacterial reaction centers and mobile c-type cytochromes
    • J. Deisenhofer and J. R. Norris, editors. Academic Press, New York
    • Tiede, D. M., and P. L. Dutton. 1993. Electron transfer between bacterial reaction centers and mobile c-type cytochromes. In The Photosynthetic Reaction Center. J. Deisenhofer and J. R. Norris, editors. Academic Press, New York. 257-288.
    • (1993) The Photosynthetic Reaction Center , pp. 257-288
    • Tiede, D.M.1    Dutton, P.L.2
  • 54
    • 0027243893 scopus 로고
    • Electron transfer kinetics and electrostatic properties of the Rhodobacter sphaeroides reaction center and soluble c-cytochromes
    • Tiede, D. M., A. C. Vashishta, and M. R. Gunner. 1993. Electron transfer kinetics and electrostatic properties of the Rhodobacter sphaeroides reaction center and soluble c-cytochromes. Biochemistry. 32: 4515-4531.
    • (1993) Biochemistry , vol.32 , pp. 4515-4531
    • Tiede, D.M.1    Vashishta, A.C.2    Gunner, M.R.3
  • 55
    • 0027754117 scopus 로고
    • 2 to the primary donor of Rhodobacter sphaeroides reaction center. A temperature dependence study
    • 2 to the primary donor of Rhodobacter sphaeroides reaction center. A temperature dependence study. Biochemistry. 32: 13245-13253.
    • (1993) Biochemistry , vol.32 , pp. 13245-13253
    • Venturoli, G.1    Mallardi, A.2    Mathis, P.3


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