메뉴 건너뛰기




Volumn 85, Issue 3, 2003, Pages 1851-1870

Charge recombination and protein dynamics in bacterial photosynthetic reaction centers entrapped in a sol-gel matrix

Author keywords

[No Author keywords available]

Indexed keywords

SILANE DERIVATIVE; SILICON DIOXIDE;

EID: 0041821411     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74613-X     Document Type: Article
Times cited : (36)

References (99)
  • 1
    • 0023395661 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: The cofactors
    • 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 cofactors. Proc. Natl. Acad. Sci. USA. 84:5730-5734.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5730-5734
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komiya, H.4    Rees, D.C.5
  • 2
    • 0028783670 scopus 로고
    • Relationship between the oxidation potential of the bacteriochlorophyll dimer and electron transfer in photosynthetic reaction centers
    • Allen, J. P., and J. C. Williams. 1995. Relationship between the oxidation potential of the bacteriochlorophyll dimer and electron transfer in photosynthetic reaction centers. J. Bioenerg. Biomembr. 27:275-283.
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 275-283
    • Allen, J.P.1    Williams, J.C.2
  • 3
    • 0032582723 scopus 로고    scopus 로고
    • Photosynthetic reaction centers
    • Allen, J. P., and J. C. Williams. 1998. Photosynthetic reaction centers. FEBS Lett. 438:5-9.
    • (1998) FEBS Lett. , vol.438 , pp. 5-9
    • Allen, J.P.1    Williams, J.C.2
  • 4
    • 0019769585 scopus 로고
    • Delayed fluorescence from Rhodopseudomonas sphaeroides reaction centers. Enthalpy and free energy changes accompanying electron transfer from P-870 to quinones
    • Arata, H., and W. W. Parson. 1981. Delayed fluorescence from Rhodopseudomonas sphaeroides reaction centers. Enthalpy and free energy changes accompanying electron transfer from P-870 to quinones. Biochim. Biophys. Acta. 638:201-209.
    • (1981) Biochim. Biophys. Acta , vol.638 , pp. 201-209
    • Arata, H.1    Parson, W.W.2
  • 5
    • 0034613172 scopus 로고    scopus 로고
    • Dynamically controlled protein tunneling paths in photosynthetic reaction centers
    • Balabin, I. A., and J. N. Onuchic. 2000. Dynamically controlled protein tunneling paths in photosynthetic reaction centers. Science. 290:114-117.
    • (2000) Science , vol.290 , pp. 114-117
    • Balabin, I.A.1    Onuchic, J.N.2
  • 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
    • 0000895446 scopus 로고
    • Tunneling pathway and redox-state dependent electronic couplings at nearly fixed distance in electron-transfer proteins
    • Beratan, D. N., J. N. Betts, and J. N. Onuchic. 1992. Tunneling pathway and redox-state dependent electronic couplings at nearly fixed distance in electron-transfer proteins. J. Phys. Chem. 96:2852-2855.
    • (1992) J. Phys. Chem. , vol.96 , pp. 2852-2855
    • Beratan, D.N.1    Betts, J.N.2    Onuchic, J.N.3
  • 8
    • 0033621093 scopus 로고    scopus 로고
    • A in reaction centers from Rhodopseudomonas viridis revealed by Fourier transform infrared spectroscopy and site-directed mutagenesis
    • A in reaction centers from Rhodopseudomonas viridis revealed by Fourier transform infrared spectroscopy and site-directed mutagenesis. Biochemistry. 38:11541-11552.
    • (1999) Biochemistry , vol.38 , pp. 11541-11552
    • Breton, J.1    Bibikova, M.2    Oesterhelt, D.3    Nabedryk, E.4
  • 9
    • 0030612688 scopus 로고    scopus 로고
    • A demonstrated by mutations at residues Glu L104 and Trp L100 in reaction centers from Rhodobacter sphaeroides
    • A demonstrated by mutations at residues Glu L104 and Trp L100 in reaction centers from Rhodobacter sphaeroides. Biochemistry. 36:4515-4525.
    • (1997) Biochemistry , vol.36 , pp. 4515-4525
    • Breton, J.1    Nabedryk, E.2    Allen, J.P.3    Williams, J.C.4
  • 11
    • 0002097104 scopus 로고
    • Dynamics of the two-state system with ohmic dissipation
    • Chakravarty, S., and A. Leggett. 1984. Dynamics of the two-state system with ohmic dissipation. Phys. Rev. Lett. 52:5-8.
    • (1984) Phys. Rev. Lett. , vol.52 , pp. 5-8
    • Chakravarty, S.1    Leggett, A.2
  • 12
    • 0001008590 scopus 로고
    • Dissipative dynamics of a two-state system coupled to a heat bath
    • Chang, L. D., and S. Chakravarty. 1985. Dissipative dynamics of a two-state system coupled to a heat bath. Phys. Rev. B. 31:154-164.
    • (1985) Phys. Rev. B , vol.31 , pp. 154-164
    • Chang, L.D.1    Chakravarty, S.2
  • 13
    • 0022695144 scopus 로고
    • Sol-gel processing of silica: 1. The role of the starting compounds
    • Chen, K. C., T. Tsuchiya, and J. D. Mackenzie. 1986. Sol-gel processing of silica: 1. The role of the starting compounds. J. Non-Cryst. Sol. 81:227-237.
    • (1986) J. Non-Cryst. Sol. , vol.81 , pp. 227-237
    • Chen, K.C.1    Tsuchiya, T.2    Mackenzie, J.D.3
  • 16
    • 0028075936 scopus 로고
    • Quantum biomechanics of long-range electron transfer in protein: Hydrogen bonds and reorganization energies
    • Dutton, P. L., and C. C. Mosser. 1994. Quantum biomechanics of long-range electron transfer in protein: hydrogen bonds and reorganization energies. Proc. Natl. Acad. Sci. USA. 91:10247-10250.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10247-10250
    • Dutton, P.L.1    Mosser, C.C.2
  • 18
    • 0000057166 scopus 로고
    • Low-temperature dynamical simulation of spin-boson systems
    • Egger, R., and C. H. Mak. 1994a. Low-temperature dynamical simulation of spin-boson systems. Phys. Rev. B. 50:15210-15220.
    • (1994) Phys. Rev. B , vol.50 , pp. 15210-15220
    • Egger, R.1    Mak, C.H.2
  • 19
    • 36449009714 scopus 로고
    • Quantum rates for nonadiabatic electron transfer
    • Egger, R., and C. H. Mak. 1994b. Quantum rates for nonadiabatic electron transfer. J. Chem. Phys. 100:2651-2660.
    • (1994) J. Chem. Phys. , vol.100 , pp. 2651-2660
    • Egger, R.1    Mak, C.H.2
  • 20
    • 0000182049 scopus 로고    scopus 로고
    • Path-integral Monte Carlo simulations without the sign problem: Multilevel blocking approach for effective actions
    • Egger, R., L. Mühlbacher, and C. H. Mak. 2000. Path-integral Monte Carlo simulations without the sign problem: multilevel blocking approach for effective actions. Phys. Rev. E. 61:5961-5966.
    • (2000) Phys. Rev. E , vol.61 , pp. 5961-5966
    • Egger, R.1    Mühlbacher, L.2    Mak, C.H.3
  • 21
    • 0027128133 scopus 로고
    • Encapsulation of proteins in transparent porous silicate glasses prepared by the sol-gel method
    • Ellerby, L. M., C. R. Nishida, F. Nishida, S. A. Yamanaka, B. Dunn, J. S. Valentine, and J. I. Zink. 1992. Encapsulation of proteins in transparent porous silicate glasses prepared by the sol-gel method. Science. 255:1113-1115.
    • (1992) Science , vol.255 , pp. 1113-1115
    • Ellerby, L.M.1    Nishida, C.R.2    Nishida, F.3    Yamanaka, S.A.4    Dunn, B.5    Valentine, J.S.6    Zink, J.I.7
  • 22
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: Cofactors and protein-cofactor interactions
    • Ermler, U., G. Fritzsch, S. K. Buchanan, and H. Michel. 1994. Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: cofactors and protein-cofactor interactions. Structure. 2:925-936.
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.1    Fritzsch, G.2    Buchanan, S.K.3    Michel, H.4
  • 23
    • 0000058886 scopus 로고
    • Structure and function of bacterial photosynthetic reaction centers
    • Feher, G., J. P. Allen, M. Y. Okamura, and D. C. Rees. 1989. Structure and function of bacterial photosynthetic reaction centers. Nature. 339:111-116.
    • (1989) Nature , vol.339 , pp. 111-116
    • Feher, G.1    Allen, J.P.2    Okamura, M.Y.3    Rees, D.C.4
  • 24
    • 36849121368 scopus 로고
    • The relaxation distribution function of polyisobutylene in the transition from rubber-like to glass-like behavior
    • Ferry, J. D., L. D. Grandine, Jr., and E. R. Fitzgerald. 1953. The relaxation distribution function of polyisobutylene in the transition from rubber-like to glass-like behavior. J. Appl. Phys. 24:911-916.
    • (1953) J. Appl. Phys. , vol.24 , pp. 911-916
    • Ferry, J.D.1    Grandine L.D., Jr.2    Fitzgerald, E.R.3
  • 25
    • 4444269588 scopus 로고
    • The theory of a general quantum system interacting with a linear dissipative system
    • Feynman, R. P., and F. L. Vernon, Jr. 1963. The theory of a general quantum system interacting with a linear dissipative system. Ann. Phys. 24:118-173.
    • (1963) Ann. Phys. , vol.24 , pp. 118-173
    • Feynman, R.P.1    Vernon F.L., Jr.2
  • 26
    • 0000204983 scopus 로고
    • Temperature dependence of the electric field modulation of electron transfer rates: Charge recombination in photosynthetic reaction centers
    • Franzen, S., and S. G. Boxer. 1993. Temperature dependence of the electric field modulation of electron transfer rates: charge recombination in photosynthetic reaction centers. J. Phys. Chem. 97:6304-6318.
    • (1993) J. Phys. Chem. , vol.97 , pp. 6304-6318
    • Franzen, S.1    Boxer, S.G.2
  • 27
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H., S. G. Sligar, and P. G. Wolynes. 1991. The energy landscapes and motions of proteins. Science. 254:1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 28
    • 0002237761 scopus 로고
    • Biomolecules: Where the physics of complexity and simplicity meet
    • Frauenfelder, H., and P. G. Wolynes. 1994. Biomolecules: where the physics of complexity and simplicity meet. Phys. Tod. 47:58-64.
    • (1994) Phys. Tod. , vol.47 , pp. 58-64
    • Frauenfelder, H.1    Wolynes, P.G.2
  • 29
    • 0025772089 scopus 로고
    • Subpicosecond dynamics of excited state of primary electron donor in reaction centers of Rhodopseudomonas viridis as revealed by hole burning at 1.7 K broad and narrow holes
    • Ganago, A. O., A. Y. Shkuropatov, and V. A. Shuvalov. 1991. Subpicosecond dynamics of excited state of primary electron donor in reaction centers of Rhodopseudomonas viridis as revealed by hole burning at 1.7 K broad and narrow holes. FEBS Lett. 284:199-202.
    • (1991) FEBS Lett. , vol.284 , pp. 199-202
    • Ganago, A.O.1    Shkuropatov, A.Y.2    Shuvalov, V.A.3
  • 30
    • 36549095460 scopus 로고
    • Effect of friction on electron transfer in biomolecules
    • Garg, A., J. N. Onuchic, and V. Ambegaokar. 1985. Effect of friction on electron transfer in biomolecules. J. Chem. Phys. 83:4491-4503.
    • (1985) J. Chem. Phys. , vol.83 , pp. 4491-4503
    • Garg, A.1    Onuchic, J.N.2    Ambegaokar, V.3
  • 31
    • 0032475402 scopus 로고    scopus 로고
    • Encapsulation of biologicals within silicate, siloxane, and hybrid sol-gel polymers: An efficient and generic approach
    • Gill, I., and A. Ballesteros. 1998. Encapsulation of biologicals within silicate, siloxane, and hybrid sol-gel polymers: an efficient and generic approach. J. Am. Chem. Soc. 120:8587-8598.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8587-8598
    • Gill, I.1    Ballesteros, A.2
  • 32
    • 0034237721 scopus 로고    scopus 로고
    • Bioencapsulation within synthetic polymers (part 1): Sol-gel encapsulated biologicals
    • Gill, I., and A. Ballesteros. 2000a. Bioencapsulation within synthetic polymers (part 1): sol-gel encapsulated biologicals. Trends Biotechnol. 18:282-296.
    • (2000) Trends Biotechnol. , vol.18 , pp. 282-296
    • Gill, I.1    Ballesteros, A.2
  • 33
    • 0034333201 scopus 로고    scopus 로고
    • Bioencapsulation within synthetic polymers (part 2): Non-sol-gel protein-polymer composites
    • Gill, I., and A. Ballesteros. 2000b. Bioencapsulation within synthetic polymers (part 2): non-sol-gel protein-polymer composites. Trends Biotechnol. 18:469-479.
    • (2000) Trends Biotechnol. , vol.18 , pp. 469-479
    • Gill, I.1    Ballesteros, A.2
  • 34
    • 0020771265 scopus 로고
    • Dynamics of a small globular protein in terms of low-frequency vibrational modes
    • Go, N., T. Noguti, and T. Nishikawa. 1983. Dynamics of a small globular protein in terms of low-frequency vibrational modes. Proc. Natl. Acad. Sci. USA. 80:3696-3700.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 3696-3700
    • Go, N.1    Noguti, T.2    Nishikawa, T.3
  • 35
    • 0030607107 scopus 로고    scopus 로고
    • Rapid isolation of bacterial photosynthetic reaction centers with an engineered poly-histidine tag
    • Goldsmith, J. O., and S. G. Boxer. 1996. Rapid isolation of bacterial photosynthetic reaction centers with an engineered poly-histidine tag. Biochim. Biophys. Acta. 1276:171-175.
    • (1996) Biochim. Biophys. Acta , vol.1276 , pp. 171-175
    • Goldsmith, J.O.1    Boxer, S.G.2
  • 37
    • 0024974078 scopus 로고
    • Long-range electron transfer in multisite metalloproteins
    • Gray, H. B., and B. G. Malmström. 1989. Long-range electron transfer in multisite metalloproteins. Biochemistry. 28:7499-7505.
    • (1989) Biochemistry , vol.28 , pp. 7499-7505
    • Gray, H.B.1    Malmström, B.G.2
  • 38
    • 0029895160 scopus 로고    scopus 로고
    • Electron transfer in proteins
    • Gray, H. B., and J. R. Winkler. 1996. Electron transfer in proteins. Annu. Rev. Biochem. 65:537-561.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 537-561
    • Gray, H.B.1    Winkler, J.R.2
  • 40
    • 33845374514 scopus 로고
    • Kinetic studies on the reaction center protein from Rhodopseudomonas sphaeroides: The temperature and free energy dependence of electron transfer between various quinones in the QA site and the oxidized bacteriochlorophyll dimer
    • Gunner, M. R., D. E. Robertson, and P. L. Dutton. 1986. Kinetic studies on the reaction center protein from Rhodopseudomonas sphaeroides: the temperature and free energy dependence of electron transfer between various quinones in the QA site and the oxidized bacteriochlorophyll dimer. J. Phys. Chem. 90:3783-3795.
    • (1986) J. Phys. Chem. , vol.90 , pp. 3783-3795
    • Gunner, M.R.1    Robertson, D.E.2    Dutton, P.L.3
  • 41
    • 0031208887 scopus 로고    scopus 로고
    • Photophysics and photosynthesis. Structure and spectroscopy of reaction centers of purple bacteria
    • Hoff, A. J., and J. Deisenhofer. 1997. Photophysics and photosynthesis. Structure and spectroscopy of reaction centers of purple bacteria. Phys. Rep. 287:1-247.
    • (1997) Phys. Rep. , vol.287 , pp. 1-247
    • Hoff, A.J.1    Deisenhofer, J.2
  • 43
    • 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
  • 44
    • 0028021632 scopus 로고
    • Stabilization of reduced primary quinone by proton uptake in reaction centers of Rhodobacter sphaeroides
    • Kálmán, L., and P. Maróti. 1994. Stabilization of reduced primary quinone by proton uptake in reaction centers of Rhodobacter sphaeroides. Biochemistry. 33:9237-9244.
    • (1994) Biochemistry , vol.33 , pp. 9237-9244
    • Kálmán, L.1    Maróti, P.2
  • 46
    • 0034719114 scopus 로고    scopus 로고
    • Sol-gel trapping of functional intermediates of hemoglobin: Geminate and bimolecular recombination studies
    • Khan, I., C. F. Shannon, D. Dantsker, A. J. Friedman, J. Apodaca, and J. M. Friedman. 2000. Sol-gel trapping of functional intermediates of hemoglobin: geminate and bimolecular recombination studies. Biochemistry. 39:16099-16109.
    • (2000) Biochemistry , vol.39 , pp. 16099-16109
    • Khan, I.1    Shannon, C.F.2    Dantsker, D.3    Friedman, A.J.4    Apodaca, J.5    Friedman, J.M.6
  • 47
    • 0025363373 scopus 로고
    • Evidence that a distribution of bacterial reaction centers underlies the temperature and detection-wavelength dependence of the rates of the primary electron-transfer reactions
    • Kirmaier, C., and D. Holten. 1990. Evidence that a distribution of bacterial reaction centers underlies the temperature and detection-wavelength dependence of the rates of the primary electron-transfer reactions. Proc. Natl. Acad. Sci. USA. 87:3552-3556.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3552-3556
    • Kirmaier, C.1    Holten, D.2
  • 48
    • 0021674417 scopus 로고
    • Electron-transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state: Evidence for light-induced structural changes
    • Kleinfeld, D., M. Y. Okamura, and G. Feher. 1984. Electron-transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state: evidence for light-induced structural changes. Biochemistry. 23:5780-5786.
    • (1984) Biochemistry , vol.23 , pp. 5780-5786
    • Kleinfeld, D.1    Okamura, M.Y.2    Feher, G.3
  • 49
    • 0000145470 scopus 로고    scopus 로고
    • Asymmetric electron transfer in reaction centers of purple bacteria strongly depends on different electron matrix elements in the active and inactive branches
    • Kolbasov, D., and A. Scherz. 2000. Asymmetric electron transfer in reaction centers of purple bacteria strongly depends on different electron matrix elements in the active and inactive branches. J. Phys. Chem. B. 104:1802-1809.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 1802-1809
    • Kolbasov, D.1    Scherz, A.2
  • 50
    • 0032578202 scopus 로고    scopus 로고
    • Direct electrochemistry of cofactor redox sites in a bacterial photosynthetic reaction center
    • Kong, J., Z. Lu, Y. M. Lvov, R. Z. B. Desamero, H. A. Frank, and J. F. Rusling. 1998. Direct electrochemistry of cofactor redox sites in a bacterial photosynthetic reaction center. J. Am. Chem. Soc. 120:7371-7372.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7371-7372
    • Kong, J.1    Lu, Z.2    Lvov, Y.M.3    Desamero, R.Z.B.4    Frank, H.A.5    Rusling, J.F.6
  • 52
    • 0001564679 scopus 로고
    • Teoriya bezizluchatelnikh electronnikh perekhodov mezhdu ionami v rastvorakh
    • Levich, V. G., and R. R. Doganadze. 1959. Teoriya bezizluchatelnikh electronnikh perekhodov mezhdu ionami v rastvorakh. Dokl. Acad. Nauk. SSSR. 124:123-126.
    • (1959) Dokl. Acad. Nauk. SSSR , vol.124 , pp. 123-126
    • Levich, V.G.1    Doganadze, R.R.2
  • 53
    • 0022419152 scopus 로고
    • Protein normal-mode dynamics: Trypsin inhibitor, crambin, ribonuclease and lysozyme
    • Levitt, M., C. Sander, and P. S. Stern. 1985. Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme. J. Mol. Biol. 181:423-447.
    • (1985) J. Mol. Biol. , vol.181 , pp. 423-447
    • Levitt, M.1    Sander, C.2    Stern, P.S.3
  • 54
    • 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. 1994. 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
  • 56
    • 0001672288 scopus 로고
    • Chemical and electrochemical electron-transfer theory
    • Marcus, R. A. 1964. Chemical and electrochemical electron-transfer theory. Annu. Rev. Phys. Chem. 15:155-196.
    • (1964) Annu. Rev. Phys. Chem. , vol.15 , pp. 155-196
    • Marcus, R.A.1
  • 57
    • 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
  • 58
    • 0039430817 scopus 로고    scopus 로고
    • - state of bacterial photosynthetic reaction centers: Rate limitation within the protein
    • - state of bacterial photosynthetic reaction centers: rate limitation within the protein. Biophys. J. 73:367-381.
    • (1997) Biophys. J. , vol.73 , pp. 367-381
    • Maróti, P.1    Wraight, C.A.2
  • 60
    • 0344193626 scopus 로고    scopus 로고
    • Electron transfer and protein dynamics in the photosynthetic reaction center
    • McMahon, B. H., J. D. Müller, C. A. Wraight, and G. U. Nienhaus. 1998. Electron transfer and protein dynamics in the photosynthetic reaction center. Biophys. J. 74:2567-2587.
    • (1998) Biophys. J. , vol.74 , pp. 2567-2587
    • McMahon, B.H.1    Müller, J.D.2    Wraight, C.A.3    Nienhaus, G.U.4
  • 64
    • 0025904874 scopus 로고
    • Electrochemical redox titration of cofactors in the reaction center from Rhodobacter sphaeroides
    • Moss, D. A., M. Leonhard, M. Bauscher, and W. Mäntele. 1991. Electrochemical redox titration of cofactors in the reaction center from Rhodobacter sphaeroides. FEBS Lett. 283:33-36.
    • (1991) FEBS Lett. , vol.283 , pp. 33-36
    • Moss, D.A.1    Leonhard, M.2    Bauscher, M.3    Mäntele, W.4
  • 65
    • 0042368510 scopus 로고    scopus 로고
    • Two distinct conformations of the primary electron donor in reaction centers from Rhodobacter sphaeroides revealed by ENDOR/TRIPLE-spectroscopy
    • Müh, F., J. Rautter, and W. Lubitz. 1997. Two distinct conformations of the primary electron donor in reaction centers from Rhodobacter sphaeroides revealed by ENDOR/TRIPLE-spectroscopy. Biochemistry. 36:4155-4162.
    • (1997) Biochemistry , vol.36 , pp. 4155-4162
    • Müh, F.1    Rautter, J.2    Lubitz, W.3
  • 68
    • 0017411025 scopus 로고
    • Possible role of macromolecular components in the functioning of photosynthetic reaction centers of purple bacteria
    • Noks, P. P., E. P. Lukashev, A. A. Kononenko, P. S. Venediktov, and A. B. Rubin. 1977. Possible role of macromolecular components in the functioning of photosynthetic reaction centers of purple bacteria. Mol. Biol. (Mosk.). 11:1090-1099.
    • (1977) Mol. Biol. (Mosk.) , vol.11 , pp. 1090-1099
    • Noks, P.P.1    Lukashev, E.P.2    Kononenko, A.A.3    Venediktov, P.S.4    Rubin, A.B.5
  • 70
    • 0000178540 scopus 로고
    • Primary acceptor in bacterial photosynthesis: Obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas spheroides
    • Okamura, M. Y., R. A. Isaacson, and G. Feher. 1975. Primary acceptor in bacterial photosynthesis: obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas spheroides. Proc. Natl. Acad. Sci. USA. 72:3491-3495.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 3491-3495
    • Okamura, M.Y.1    Isaacson, R.A.2    Feher, G.3
  • 71
    • 36549092622 scopus 로고
    • Effect of friction on electron transfer: The two reaction coordinate case
    • Onuchic, J. N. 1987. Effect of friction on electron transfer: the two reaction coordinate case. J. Chem. Phys. 86:3925-3943.
    • (1987) J. Chem. Phys. , vol.86 , pp. 3925-3943
    • Onuchic, J.N.1
  • 72
    • 0001010258 scopus 로고
    • Some aspects of electron-transfer reaction dynamics
    • Onuchic, J. N., D. N. Beratan, and J. J. Hopfield. 1986. Some aspects of electron-transfer reaction dynamics. J. Phys. Chem. 90:3707-3721.
    • (1986) J. Phys. Chem. , vol.90 , pp. 3707-3721
    • Onuchic, J.N.1    Beratan, D.N.2    Hopfield, J.J.3
  • 73
    • 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
  • 74
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page, C. C., C. C. Moser, X. Chen, and P. L. Dutton. 1999. Natural engineering principles of electron tunnelling 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
  • 75
    • 0036156512 scopus 로고    scopus 로고
    • Electron transfer kinetics in photosynthetic reaction centers embedded in trehalose glasses: Trapping of conformational substates at room temperature
    • Palazzo, G., A. Mallardi, A. Hochkoeppler, L. Cordone, and G. Venturoli. 2002. Electron transfer kinetics in photosynthetic reaction centers embedded in trehalose glasses: trapping of conformational substates at room temperature. Biophys. J. 82:558-568.
    • (2002) Biophys. J. , vol.82 , pp. 558-568
    • Palazzo, G.1    Mallardi, A.2    Hochkoeppler, A.3    Cordone, L.4    Venturoli, G.5
  • 76
    • 0013351693 scopus 로고
    • Flash-induced absorbance changes in Rhodospirillum rubrum chromatophores
    • Parson, W. W. 1967. Flash-induced absorbance changes in Rhodospirillum rubrum chromatophores. Biochim. Biophys. Acta. 131:154-172.
    • (1967) Biochim. Biophys. Acta , vol.131 , pp. 154-172
    • Parson, W.W.1
  • 78
    • 0028287888 scopus 로고
    • Time-dependent thermodynamics during early electron transfer in reaction centers from Rhodobacter sphaeroides
    • Peloquin, J. M., J. C. Williams, X. Lin, R. G. Alden, A. K. Taguchi, J. P. Allen, and N. W. Woodbury. 1994. Time-dependent thermodynamics during early electron transfer in reaction centers from Rhodobacter sphaeroides. Biochemistry. 33:8089-8100.
    • (1994) Biochemistry , vol.33 , pp. 8089-8100
    • Peloquin, J.M.1    Williams, J.C.2    Lin, X.3    Alden, R.G.4    Taguchi, A.K.5    Allen, J.P.6    Woodbury, N.W.7
  • 79
    • 0000260455 scopus 로고
    • Application of spectral hole burning spectroscopies to antenna and reaction center complexes
    • Reddy, N. R. S., P. A. Lyle, and G. J. Small. 1992. Application of spectral hole burning spectroscopies to antenna and reaction center complexes. Photosyn. Res. 31:167-194.
    • (1992) Photosyn. Res. , vol.31 , pp. 167-194
    • Reddy, N.R.S.1    Lyle, P.A.2    Small, G.J.3
  • 80
    • 8444227547 scopus 로고
    • Dynamics of supercooled melts treated in terms of the random-walk concept
    • Richert, R., and H. Bässler. 1990. Dynamics of supercooled melts treated in terms of the random-walk concept. J. Phys. Condens. Matter. 2:2273-2288.
    • (1990) J. Phys. Condens. Matter , vol.2 , pp. 2273-2288
    • Richert, R.1    Bässler, H.2
  • 81
    • 0013610799 scopus 로고
    • Dynamic solvent effects on outer-sphere electron transfer
    • Rips, I., and J. Jortner. 1987. Dynamic solvent effects on outer-sphere electron transfer. J. Chem. Phys. 87:2090-2104.
    • (1987) J. Chem. Phys. , vol.87 , pp. 2090-2104
    • Rips, I.1    Jortner, J.2
  • 84
    • 0001385236 scopus 로고    scopus 로고
    • Temperature and free energy dependence of the direct charge recombination rate from the secondary quinone in bacterial reaction centers from Rhodobacter sphaeroides
    • Schmid, R., and A. Labahn. 2000. Temperature and free energy dependence of the direct charge recombination rate from the secondary quinone in bacterial reaction centers from Rhodobacter sphaeroides. J. Phys. Chem. 104:2928-2936.
    • (2000) J. Phys. Chem. , vol.104 , pp. 2928-2936
    • Schmid, R.1    Labahn, A.2
  • 85
    • 0000764744 scopus 로고
    • Coupling of protein motions to electron transfer: Molecular dynamics and stochastic quantum mechanics study of photosynthetic reaction centers
    • Schulten, K., and M. Tesch. 1991. Coupling of protein motions to electron transfer: molecular dynamics and stochastic quantum mechanics study of photosynthetic reaction centers. Chem. Phys. 158:421-446.
    • (1991) Chem. Phys. , vol.158 , pp. 421-446
    • Schulten, K.1    Tesch, M.2
  • 86
    • 0031886681 scopus 로고    scopus 로고
    • Calculation of electron transfer reorganization energies using the finite difference Poisson-Boltzmann model
    • Sharp, K. A. 1998. Calculation of electron transfer reorganization energies using the finite difference Poisson-Boltzmann model. Biophys. J. 74:1241-1250.
    • (1998) Biophys. J. , vol.74 , pp. 1241-1250
    • Sharp, K.A.1
  • 87
    • 0029163340 scopus 로고
    • Fixation of the quaternary structures of human adult haemoglobin by encapsulation in transparent porous silica gels
    • Shibayama, N., and S. Saigo. 1995. Fixation of the quaternary structures of human adult haemoglobin by encapsulation in transparent porous silica gels. J. Mol. Biol. 251:203-209.
    • (1995) J. Mol. Biol. , vol.251 , pp. 203-209
    • Shibayama, N.1    Saigo, S.2
  • 88
    • 0025938315 scopus 로고
    • Protein dynamics: Comparison of simulations with inelastic neutron scattering experiments
    • Smith, J. C. 1991. Protein dynamics: comparison of simulations with inelastic neutron scattering experiments. Q. Rev. Biophys. 24:227-291.
    • (1991) Q. Rev. Biophys. , vol.24 , pp. 227-291
    • Smith, J.C.1
  • 90
    • 0032898345 scopus 로고    scopus 로고
    • Chemical and biochemical sensors based on advances in materials chemistry
    • Tess, M. E., and J. A. Cox. 1999. Chemical and biochemical sensors based on advances in materials chemistry, J. Pharm. Biomed. Anal. 19:55-68.
    • (1999) J. Pharm. Biomed. Anal. , vol.19 , pp. 55-68
    • Tess, M.E.1    Cox, J.A.2
  • 92
    • 0028199789 scopus 로고
    • Temperature-dependent electron spin polarization of the triplet state of the primary donor in Rhodopseudomonas viridis
    • van den Brink, J. S., H. Manikowski, P. Gast, and A. J. Hoff. 1994. Temperature-dependent electron spin polarization of the triplet state of the primary donor in Rhodopseudomonas viridis. Biochim. Biophys. Acta. 1185:177-187.
    • (1994) Biochim. Biophys. Acta , vol.1185 , pp. 177-187
    • Van den Brink, J.S.1    Manikowski, H.2    Gast, P.3    Hoff, A.J.4
  • 93
    • 0001266147 scopus 로고
    • - in external and magnetic fields
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer, editors. Kluwer Academic Publishers, Dordrecht
    • - in external and magnetic fields. In Anoxygenic Bacteria, R. E. Blankenship, M. T. Madigan, and C. E. Bauer, editors. Kluwer Academic Publishers, Dordrecht. 595-626.
    • (1995) Anoxygenic Bacteria , pp. 595-626
    • Volk, M.1    Ogrodnik, A.2    Michel-Beyerle, M.E.3
  • 94
    • 0024445808 scopus 로고
    • Dispersed polaron simulations of electron transfer in photosynthetic reaction centers
    • Warshel, A., Z. T. Chu, and W. W. Parson. 1989. Dispersed polaron simulations of electron transfer in photosynthetic reaction centers. Science. 246:112-116.
    • (1989) Science , vol.246 , pp. 112-116
    • Warshel, A.1    Chu, Z.T.2    Parson, W.W.3
  • 95
    • 1542382717 scopus 로고
    • Simulation of the dynamics of electron transfer reactions in polar solvents: Semiclassical trajectories and dispersed polaron approaches
    • Warshel, A., and J.-H. Hwang. 1986. Simulation of the dynamics of electron transfer reactions in polar solvents: semiclassical trajectories and dispersed polaron approaches. J. Chem. Phys. 84:4938-4957.
    • (1986) J. Chem. Phys. , vol.84 , pp. 4938-4957
    • Warshel, A.1    Hwang, J.-H.2
  • 96
    • 0023040257 scopus 로고
    • Nanosecond fluorescence from chromatophores of Rhodopseudomonas sphaeroides and Rhodospirillum rubrum
    • Woodbury, N. W., and W. W. Parson. 1986. Nanosecond fluorescence from chromatophores of Rhodopseudomonas sphaeroides and Rhodospirillum rubrum. Biochim. Biophys. Acta. 850:197-210.
    • (1986) Biochim. Biophys. Acta , vol.850 , pp. 197-210
    • Woodbury, N.W.1    Parson, W.W.2
  • 97
    • 0043134863 scopus 로고
    • Multi-mode coupling of protein motions to electron-transfer in the photosynthetic reaction center: Spin-boson theory based on a classical molecular dynamics simulation
    • J. Breton, and A. Verméglio, editors. Plenum Press, New York
    • Xu, D., and K. Schulten. 1992. Multi-mode coupling of protein motions to electron-transfer in the photosynthetic reaction center: spin-boson theory based on a classical molecular dynamics simulation. In The Photosynthetic Reaction Center II. J. Breton, and A. Verméglio, editors. Plenum Press, New York. 301-312.
    • (1992) The Photosynthetic Reaction Center II , pp. 301-312
    • Xu, D.1    Schulten, K.2
  • 98
    • 21744452904 scopus 로고
    • Coupling of protein motion to electron transfer in a photosynthetic reaction center: Investigating the low temperature behavior in the framework of the spin-boson model
    • Xu, D., and K. Schulten. 1994. Coupling of protein motion to electron transfer in a photosynthetic reaction center: investigating the low temperature behavior in the framework of the spin-boson model. Chem. Phys. 182:91-117.
    • (1994) Chem. Phys. , vol.182 , pp. 91-117
    • Xu, D.1    Schulten, K.2
  • 99
    • 0034710423 scopus 로고    scopus 로고
    • -charge recombination in Rhodobacter sphaeroides R-26 reaction centers
    • -charge recombination in Rhodobacter sphaeroides R-26 reaction centers. J. Phys. Chem. 104:8035-8043.
    • (2000) J. Phys. Chem. , vol.104 , pp. 8035-8043
    • Xu, Q.1    Gunner, M.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.