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Volumn 86, Issue 5, 2004, Pages 3121-3130

Electrochromic Shift of Chlorophyll Absorption in Photosystem I from Synechocystis sp. PCC 6803: A Probe of Optical and Dielectric Properties around the Secondary Electron Acceptor

Author keywords

[No Author keywords available]

Indexed keywords

CHLOROPHYLL A; PIGMENT;

EID: 2142657351     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(04)74360-X     Document Type: Article
Times cited : (40)

References (65)
  • 1
    • 84961976154 scopus 로고    scopus 로고
    • Modeling electron transfer in biochemistry: A quantum chemical study of charge separation in rhodobacter sphaeroides and photosystem II
    • Blomberg, M. R. A., P. E. M. Siegbahn, and G. T. Babcock. 1998. Modeling electron transfer in biochemistry: a quantum chemical study of charge separation in rhodobacter sphaeroides and photosystem II. J. Am. Chem. Soc. 120:8812-8824.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8812-8824
    • Blomberg, M.R.A.1    Siegbahn, P.E.M.2    Babcock, G.T.3
  • 2
    • 45149142353 scopus 로고
    • Nanosecond electron transfer kinetics in photosystem I as obtained from transient EPR at room temperature
    • Bock, C. H., A. J. van der Est, K. Brettel, and D. Stehlik. 1989. Nanosecond electron transfer kinetics in photosystem I as obtained from transient EPR at room temperature. FEBS Lett. 247:91-96.
    • (1989) FEBS Lett. , vol.247 , pp. 91-96
    • Bock, C.H.1    Van Der Est, A.J.2    Brettel, K.3    Stehlik, D.4
  • 3
    • 0020490656 scopus 로고
    • Dielectric studies of the binding of water to lysozyme
    • Bone, S., and R. Pething. 1982. Dielectric studies of the binding of water to lysozyme. J. Mol. Biol. 157:571-575.
    • (1982) J. Mol. Biol. , vol.157 , pp. 571-575
    • Bone, S.1    Pething, R.2
  • 4
    • 0022429109 scopus 로고
    • Dielectric studies of protein hydration and hydration-induced flexibility
    • Bone, S., and R. Pething. 1985. Dielectric studies of protein hydration and hydration-induced flexibility. J. Mol. Biol. 181:323-326.
    • (1985) J. Mol. Biol. , vol.181 , pp. 323-326
    • Bone, S.1    Pething, R.2
  • 5
    • 0000569275 scopus 로고
    • Photosynthetic reaction center spectroscopy and electron transfer dynamics in applied electric fields
    • J. Deisenhofer and J. R. Norris, editors. Academic Press, Inc., San Diego, CA
    • Boxer, S. G. 1993. Photosynthetic reaction center spectroscopy and electron transfer dynamics in applied electric fields. In The Photosynthetic Reaction Center. J. Deisenhofer and J. R. Norris, editors. Academic Press, Inc., San Diego, CA. 179-220.
    • (1993) The Photosynthetic Reaction Center , pp. 179-220
    • Boxer, S.G.1
  • 6
    • 45449125807 scopus 로고
    • 1/2 = 200 ns at room temperature in photosystem I. Characterization by absorption spectroscopy
    • 1/2 = 200 ns at room temperature in photosystem I. Characterization by absorption spectroscopy. FEBS Lett. 239:93-98.
    • (1988) FEBS Lett. , vol.239 , pp. 93-98
    • Brettel, K.1
  • 7
    • 0031015412 scopus 로고    scopus 로고
    • Electron transfer and arrangement of the redox cofactors in photosystem I
    • Brettel, K. 1997. Electron transfer and arrangement of the redox cofactors in photosystem I. Biochim. Biophys. Acta. 1318:322-373.
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 322-373
    • Brettel, K.1
  • 9
    • 0000206317 scopus 로고    scopus 로고
    • 1 to the iron-sulfur cluster in photosystem I measured with a time resolution of 2 ns
    • G. Garab, editor. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • 1 to the iron-sulfur cluster in photosystem I measured with a time resolution of 2 ns. In Photosynthesis: Mechanisms and Effects. G. Garab, editor. Kluwer Academic Publishers, Dordrecht, The Netherlands. 611-614.
    • (1998) Photosynthesis: Mechanisms and Effects , pp. 611-614
    • Brettel, K.S.1
  • 10
    • 0030624708 scopus 로고    scopus 로고
    • Stark spectroscopy: Applications in chemistry, biology and materials science
    • Bublitz, G. U., and S. G. Boxer. 1997. Stark spectroscopy: applications in chemistry, biology and materials science. Annu. Rev. Phys. Chem. 48:213-242.
    • (1997) Annu. Rev. Phys. Chem. , vol.48 , pp. 213-242
    • Bublitz, G.U.1    Boxer, S.G.2
  • 11
    • 0036286172 scopus 로고    scopus 로고
    • Light harvesting in photosystem I: Modeling based on the 2.5-Å structure of photosystem I from Synechococcus elongatus
    • Byrdin, M., P. Jordan, N. Krauss, P. Fromme, D. Stehlik, and E. Schlodder. 2002. Light harvesting in photosystem I: modeling based on the 2.5-Å structure of photosystem I from Synechococcus elongatus. Biophys. J. 83:433-457.
    • (2002) Biophys. J. , vol.83 , pp. 433-457
    • Byrdin, M.1    Jordan, P.2    Krauss, N.3    Fromme, P.4    Stehlik, D.5    Schlodder, E.6
  • 13
    • 0037015749 scopus 로고    scopus 로고
    • Chlorophyll excitations in photosystem I of Synechococcus elongatus
    • Damjanovic, A., H. M. Vaswani, P. Fromme, and G. R. Fleming. 2002. Chlorophyll excitations in photosystem I of Synechococcus elongatus. J. Phys. Chem. B. 106:10251-10262.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 10251-10262
    • Damjanovic, A.1    Vaswani, H.M.2    Fromme, P.3    Fleming, G.R.4
  • 14
    • 0001250593 scopus 로고
    • Charged amino acids as spectroscopic determinants for chlorophyll in vivo
    • Eccles, J., and B. Honig. 1983. Charged amino acids as spectroscopic determinants for chlorophyll in vivo. Proc. Natl. Acad. Sci. USA. 80:4959-4962.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 4959-4962
    • Eccles, J.1    Honig, B.2
  • 15
    • 0006962146 scopus 로고
    • Suggestions for directed engineering of reaction centers: Metal, substituent and charge modifications
    • J. Brenton and A. Vermeglio, editors. Plenum Press, New York
    • Fajer, J., L. K. Hanson, M. C. Zerner, and M. A. Thompson. 1992. Suggestions for directed engineering of reaction centers: metal, substituent and charge modifications. In The Photosynthetic Bacterial Reaction Center II. J. Brenton and A. Vermeglio, editors. Plenum Press, New York. 33-42.
    • (1992) The Photosynthetic Bacterial Reaction Center II , pp. 33-42
    • Fajer, J.1    Hanson, L.K.2    Zerner, M.C.3    Thompson, M.A.4
  • 17
    • 0001099139 scopus 로고
    • Nonphotochemical hole burning of the native antenna complex of photosystem I (PSI-200)
    • Gillie, J. K., G. J. Small, and J. H. Golbeck. 1989. Nonphotochemical hole burning of the native antenna complex of photosystem I (PSI-200). J. Phys. Chem. 93:1620-1627.
    • (1989) J. Phys. Chem. , vol.93 , pp. 1620-1627
    • Gillie, J.K.1    Small, G.J.2    Golbeck, J.H.3
  • 18
    • 0028273452 scopus 로고
    • Observation of the reduction and reoxidation of the primary electron acceptor in photosystem I
    • Hastings, G., F. A. Kleinherenbrink, S. Lin, T. J. McHugh, and R. E. Blankenship. 1994. Observation of the reduction and reoxidation of the primary electron acceptor in photosystem I. Biochemistry. 33:3193-3200.
    • (1994) Biochemistry , vol.33 , pp. 3193-3200
    • Hastings, G.1    Kleinherenbrink, F.A.2    Lin, S.3    McHugh, T.J.4    Blankenship, R.E.5
  • 19
    • 0027289393 scopus 로고
    • Energy transfer and charge separation kinetics in photosystem I. Part 1: Picosecond transient absorption and fluorescence study of cyanobacterial photosystem I particles
    • Holzwarth, A. R., G. Schatz, H. Brock, and E. Bittersmann. 1993. Energy transfer and charge separation kinetics in photosystem I. Part 1: Picosecond transient absorption and fluorescence study of cyanobacterial photosystem I particles. Biophys. J. 64:1813-1826.
    • (1993) Biophys. J. , vol.64 , pp. 1813-1826
    • Holzwarth, A.R.1    Schatz, G.2    Brock, H.3    Bittersmann, E.4
  • 21
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
    • Jordan, P., P. Fromme, H. T. Witt, O. Klukas, W. Saenger, and N. Krauss. 2001. Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature. 411:909-917.
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 22
    • 0020162159 scopus 로고
    • Theoretical studies of the electrochromic response of carotenoids in photosynthetic membranes
    • Kakitani, T., B. Honig, and A. R. Crofts. 1982. Theoretical studies of the electrochromic response of carotenoids in photosynthetic membranes. Biophys. J. 39:57-63.
    • (1982) Biophys. J. , vol.39 , pp. 57-63
    • Kakitani, T.1    Honig, B.2    Crofts, A.R.3
  • 23
    • 0035909808 scopus 로고    scopus 로고
    • A reaction induced FT-IR study of cyanobacterial photosystem I
    • Kim, S., C. A. Sacksteder, K. A. Buixby, and B. A. Barry. 2001. A reaction induced FT-IR study of cyanobacterial photosystem I. Biochemistry. 40:15384-15395.
    • (2001) Biochemistry , vol.40 , pp. 15384-15395
    • Kim, S.1    Sacksteder, C.A.2    Buixby, K.A.3    Barry, B.A.4
  • 24
    • 0000083584 scopus 로고
    • Microscopic simulations of macroscopic dielectric constants of solvated proteins
    • King, G., F. S. Lee, and A. Warshel. 1991. Microscopic simulations of macroscopic dielectric constants of solvated proteins. J. Chem. Phys. 95:4366-4377.
    • (1991) J. Chem. Phys. , vol.95 , pp. 4366-4377
    • King, G.1    Lee, F.S.2    Warshel, A.3
  • 27
    • 0029911269 scopus 로고    scopus 로고
    • Photosystem I at 4 A resolution represents the first structural model of a joint photosynthetic reaction centre and core antenna system
    • Krauss, N., W. D. Schubert, O. Klukas, P. Fromme, H. T. Witt, and W. Saenger. 1996. Photosystem I at 4 A resolution represents the first structural model of a joint photosynthetic reaction centre and core antenna system. Nat. Struct. Biol. 3:965-973.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 965-973
    • Krauss, N.1    Schubert, W.D.2    Klukas, O.3    Fromme, P.4    Witt, H.T.5    Saenger, W.6
  • 28
    • 0026008236 scopus 로고
    • Electrochromism of chlorophyll a monomer and special pair dimer
    • Krawczyk, S. 1991. Electrochromism of chlorophyll a monomer and special pair dimer. Biochim. Biophys. Acta. 1056:64-70.
    • (1991) Biochim. Biophys. Acta , vol.1056 , pp. 64-70
    • Krawczyk, S.1
  • 29
    • 0001617915 scopus 로고
    • Rates of primary electron transfer reactions in the photosystem I reaction center reconstituted with different quinones as the secondary acceptor
    • Kumazaki, S., M. Iwaki, I. Ikegami, H. Kandori, K. Yoshihara, and S. Itoh. 1994. Rates of primary electron transfer reactions in the photosystem I reaction center reconstituted with different quinones as the secondary acceptor. J. Phys. Chem. 98:11220-11225.
    • (1994) J. Phys. Chem. , vol.98 , pp. 11220-11225
    • Kumazaki, S.1    Iwaki, M.2    Ikegami, I.3    Kandori, H.4    Yoshihara, K.5    Itoh, S.6
  • 30
    • 84981796364 scopus 로고
    • Electrochromism and solvatochromism
    • Liptay, W. 1969. Electrochromism and solvatochromism. Angew. Chem. Internat. Edit. 8:177-188.
    • (1969) Angew. Chem. Internat. Edit , vol.8 , pp. 177-188
    • Liptay, W.1
  • 31
    • 0000152192 scopus 로고
    • Stark effect spectroscopy of Rhodobacter sphaeroides and Rhodopseudomonas viridis reaction centers
    • Lockhart, D. J., and S. G. Boxer. 1988. Stark effect spectroscopy of Rhodobacter sphaeroides and Rhodopseudomonas viridis reaction centers. Proc. Natl. Acad. Sci. USA. 85:107-111.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 107-111
    • Lockhart, D.J.1    Boxer, S.G.2
  • 32
    • 0027119143 scopus 로고
    • Internal Stark effect measurement of the electric field at the amino terminus of an α helix
    • Lockhart, D. J., and P. S. Kim. 1992. Internal Stark effect measurement of the electric field at the amino terminus of an α helix. Science. 257:947-951.
    • (1992) Science , vol.257 , pp. 947-951
    • Lockhart, D.J.1    Kim, P.S.2
  • 33
    • 0031577320 scopus 로고    scopus 로고
    • Calculation of the dielectric properties of a protein and its solvent: Theory and a case study
    • Löffier, G., H. Schreiber, and O. Steinhauser. 1997. Calculation of the dielectric properties of a protein and its solvent: theory and a case study. J. Mol. Biol. 270:520-534.
    • (1997) J. Mol. Biol. , vol.270 , pp. 520-534
    • Löffier, G.1    Schreiber, H.2    Steinhauser, O.3
  • 34
    • 0035720142 scopus 로고    scopus 로고
    • Excitation energy transfer in photosystem I from oxygenic organisms
    • Melkozernov, A. N. 2001. Excitation energy transfer in photosystem I from oxygenic organisms. Photosynth. Res. 70:129-153.
    • (2001) Photosynth. Res. , vol.70 , pp. 129-153
    • Melkozernov, A.N.1
  • 36
    • 0000450431 scopus 로고    scopus 로고
    • Electron-phonon coupling and vibronic fine structure of light-harvesting complex II of green plants: Temperature dependent absorption and high-resolution fluorescence spectroscopy
    • Peterman, E. J. G., T. Pullerits, R. van Grondelle, and H. van Amerongen. 1997. Electron-phonon coupling and vibronic fine structure of light-harvesting complex II of green plants: temperature dependent absorption and high-resolution fluorescence spectroscopy. J. Phys. Chem. B. 101:4448-4457.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 4448-4457
    • Peterman, E.J.G.1    Pullerits, T.2    Van Grondelle, R.3    Van Amerongen, H.4
  • 37
    • 0000018654 scopus 로고
    • Dielectric relaxation in a protein matrix
    • Pierce, D. W., and S. G. Boxer. 1992. Dielectric relaxation in a protein matrix. J. Phys. Chem. 96:5560-5566.
    • (1992) J. Phys. Chem. , vol.96 , pp. 5560-5566
    • Pierce, D.W.1    Boxer, S.G.2
  • 38
    • 0035011330 scopus 로고    scopus 로고
    • Dielectric properties of proteins from simulations: The effect of solvent, ligands, pH, and temperature
    • Pitera, J. W., M. Falta, and W. F. van Gunsteren. 2001. Dielectric properties of proteins from simulations: the effect of solvent, ligands, pH, and temperature. Biophys. J. 80:2546-2555.
    • (2001) Biophys. J. , vol.80 , pp. 2546-2555
    • Pitera, J.W.1    Falta, M.2    Van Gunsteren, W.F.3
  • 39
    • 0035822184 scopus 로고    scopus 로고
    • New insights on persistent nonphotochemical hole burning and its application to photosynthetic complexes
    • Reinot, T., V. Zazubovich, J. M. Hayes, and G. J. Small. 2001. New insights on persistent nonphotochemical hole burning and its application to photosynthetic complexes. J. Phys. Chem. B. 105:5083-5098.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 5083-5098
    • Reinot, T.1    Zazubovich, V.2    Hayes, J.M.3    Small, G.J.4
  • 40
    • 0005829624 scopus 로고
    • Dielectric properties of protein powders with adsorbed water
    • Rosen, D. 1963. Dielectric properties of protein powders with adsorbed water. Trans. Faraday. Soc. 59:2178-2191.
    • (1963) Trans. Faraday. Soc. , vol.59 , pp. 2178-2191
    • Rosen, D.1
  • 41
    • 0023646665 scopus 로고
    • Rational modification of enzyme catalysis by engineering surface charge
    • Russell, A. J., and A. R. Fersht. 1987. Rational modification of enzyme catalysis by engineering surface charge. Nature. 328:496-500.
    • (1987) Nature , vol.328 , pp. 496-500
    • Russell, A.J.1    Fersht, A.R.2
  • 42
    • 0347164867 scopus 로고    scopus 로고
    • The red-absorbing chlorophyll a antenna states of photosystem I: A hole-burning study of Synechocystis sp. PCC 6803 and its mutants
    • Rätsep, M., T. W. Johnson, P. R. Chitnis, and G. J. Small. 2000. The red-absorbing chlorophyll a antenna states of photosystem I: a hole-burning study of Synechocystis sp. PCC 6803 and its mutants. J. Phys. Chem. B. 104:836-847.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 836-847
    • Rätsep, M.1    Johnson, T.W.2    Chitnis, P.R.3    Small, G.J.4
  • 47
    • 0000849231 scopus 로고
    • Electrostatic forces and dielectric polarizability of multiply protonated gas-phase cytochrome c ions probed by ion/molecule chemistry
    • Schnier, P. D., D. S. Gross, and E. R. Williams. 1995. Electrostatic forces and dielectric polarizability of multiply protonated gas-phase cytochrome c ions probed by ion/molecule chemistry. J. Am. Chem. Soc. 117:6747-6757.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6747-6757
    • Schnier, P.D.1    Gross, D.S.2    Williams, E.R.3
  • 48
    • 0037104747 scopus 로고    scopus 로고
    • Robustness and optimality of light harvesting in cyanobacterial photosystem I
    • Sener, M. K., D. Lu, T. Ritz, S. Park, P. Fomme, and K. Schulten. 2002. Robustness and optimality of light harvesting in cyanobacterial photosystem I. J. Phys. Chem. B. 106:7948-7960.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 7948-7960
    • Sener, M.K.1    Lu, D.2    Ritz, T.3    Park, S.4    Fomme, P.5    Schulten, K.6
  • 49
    • 0027249198 scopus 로고
    • 1 to iron-sulfur centers in spinach photosystem I
    • 1 to iron-sulfur centers in spinach photosystem I. Biochemistry. 32:7846-7854.
    • (1993) Biochemistry , vol.32 , pp. 7846-7854
    • Setif, P.1    Brettel, K.2
  • 50
    • 80053073402 scopus 로고    scopus 로고
    • Dielectric constant of cytochrome c from simulations in a water droplet including all electrostatic interactions
    • Simonson, T. 1998. Dielectric constant of cytochrome c from simulations in a water droplet including all electrostatic interactions. J. Am. Chem. Soc. 120:4875-4876.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4875-4876
    • Simonson, T.1
  • 51
    • 0029833446 scopus 로고    scopus 로고
    • Charge screening and the dielectric constant of proteins: Insights from molecular dynamics
    • Simonson, T., and C. L. Brooks, III. 1996. Charge screening and the dielectric constant of proteins: insights from molecular dynamics. J. Am. Chem. Soc. 118:8452-8458.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8452-8458
    • Simonson, T.1    Brooks III, C.L.2
  • 52
    • 0028876827 scopus 로고
    • Internal and interfacial dielectric properties of cytochrome c from molecular dynamics in aqueous solution
    • Simonson, T., and D. Perahia. 1995. Internal and interfacial dielectric properties of cytochrome c from molecular dynamics in aqueous solution. Proc. Natl. Acad. Sci. USA. 92:1082-1086.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1082-1086
    • Simonson, T.1    Perahia, D.2
  • 53
    • 0001008706 scopus 로고
    • Dielectric properties of trypsin inhibitor and lysozyme calculated from molecular dynamics simulations
    • Smith, P. E., R. M. Brunne, A. E. Mark, and W. F. van Gunsteren. 1993. Dielectric properties of trypsin inhibitor and lysozyme calculated from molecular dynamics simulations. J. Phys. Chem. 97:2009-2014.
    • (1993) J. Phys. Chem. , vol.97 , pp. 2009-2014
    • Smith, P.E.1    Brunne, R.M.2    Mark, A.E.3    Van Gunsteren, W.F.4
  • 54
    • 0028238239 scopus 로고
    • Dielectric asymmetry in the photosynthetic reaction center
    • Steffen, M. A., K. Lao, and S. G. Boxer. 1994. Dielectric asymmetry in the photosynthetic reaction center. Science. 264:810-816.
    • (1994) Science , vol.264 , pp. 810-816
    • Steffen, M.A.1    Lao, K.2    Boxer, S.G.3
  • 55
    • 0031753569 scopus 로고    scopus 로고
    • Isolation and functional study of photosystem I subunits in the cyanobacterium Synechocystis sp. PCC 6803
    • Sun, J., A. Ke, P. Jin, V. P. Chitnis, and P. R. Chitnis. 1998. Isolation and functional study of photosystem I subunits in the cyanobacterium Synechocystis sp. PCC 6803. Methods Enzymol. 297:124-139.
    • (1998) Methods Enzymol. , vol.297 , pp. 124-139
    • Sun, J.1    Ke, A.2    Jin, P.3    Chitnis, V.P.4    Chitnis, P.R.5
  • 56
    • 0026527492 scopus 로고
    • Chromophore-protein interactions and the function of the photosynthetic reaction center: A molecular dynamics study
    • Treutlein, H., K. Schulten, A. T. Brünger, M. Karplus, J. Deisenhofer, and H. Michel. 1992. Chromophore-protein interactions and the function of the photosynthetic reaction center: a molecular dynamics study. Proc. Natl. Acad. Sci. USA. 89:75-79.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 75-79
    • Treutlein, H.1    Schulten, K.2    Brünger, A.T.3    Karplus, M.4    Deisenhofer, J.5    Michel, H.6
  • 58
    • 0028861388 scopus 로고
    • The orientation of the transition dipole moments of chlorophyll a and pheophytin a in their molecular frame
    • van Zanvoort, M. A. M. J., D. Wróbel, P. Lettinga, G. van Ginkel, and Y. K. Levine. 1995. The orientation of the transition dipole moments of chlorophyll a and pheophytin a in their molecular frame. Photochem. Photobiol. 62:299-308.
    • (1995) Photochem. Photobiol. , vol.62 , pp. 299-308
    • Van Zanvoort, M.A.M.J.1    Wróbel, D.2    Lettinga, P.3    Van Ginkel, G.4    Levine, Y.K.5
  • 59
    • 0024495355 scopus 로고
    • Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobin
    • Varadarajan, R., T. E. Zewert, H. B. Gray, and S. G. Boxer. 1989. Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobin. Science. 243:69-72.
    • (1989) Science , vol.243 , pp. 69-72
    • Varadarajan, R.1    Zewert, T.E.2    Gray, H.B.3    Boxer, S.G.4
  • 60
    • 0002184931 scopus 로고
    • The pi electron structure and absorption spectra of chlorophylls in solution
    • Weiss, C. J. 1972. The pi electron structure and absorption spectra of chlorophylls in solution. J. Mol. Spectrosc. 44:37-80.
    • (1972) J. Mol. Spectrosc. , vol.44 , pp. 37-80
    • Weiss, C.J.1
  • 61
    • 0030197675 scopus 로고    scopus 로고
    • Primary charge separation and energy transfer in the photosystem I reaction center of higher plants
    • White, N. T. H., G. S. Beddard, R. G. Thome, T. M. Feehan, T. E. Keyes, and P. Heathcote. 1996. Primary charge separation and energy transfer in the photosystem I reaction center of higher plants. J. Phys. Chem. 100:12086-12099.
    • (1996) J. Phys. Chem , vol.100 , pp. 12086-12099
    • White, N.T.H.1    Beddard, G.S.2    Thome, R.G.3    Feehan, T.M.4    Keyes, T.E.5    Heathcote, P.6
  • 63
    • 0001337010 scopus 로고
    • The pathway, kinetics and thermodynamics of electron transfer in wild type and mutant reaction centers of purple nonsulfur bacteria
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer, editors. Kluwer, Dordrecht, The Netherlands
    • Woodbury, N., and J. P. Allen, 1995. The pathway, kinetics and thermodynamics of electron transfer in wild type and mutant reaction centers of purple nonsulfur bacteria. In Anoxygenic Photosynthetic Bacteria. R. E. Blankenship, M. T. Madigan, and C. E. Bauer, editors. Kluwer, Dordrecht, The Netherlands. 527-557.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 527-557
    • Woodbury, N.1    Allen, J.P.2
  • 64
    • 0036142282 scopus 로고    scopus 로고
    • Red antenna states of photosystem I from cyanobacterium Synechococcus elongatus: A spectral hole burning study
    • Zazubovich, V., S. Matsuzaki, T. W. Johnson, J. M. Hayes, P. R. Chitnis, and G. J. Small. 2002. Red antenna states of photosystem I from cyanobacterium Synechococcus elongatus: a spectral hole burning study. Chem. Phys. 275:47-59.
    • (2002) Chem. Phys. , vol.275 , pp. 47-59
    • Zazubovich, V.1    Matsuzaki, S.2    Johnson, T.W.3    Hayes, J.M.4    Chitnis, P.R.5    Small, G.J.6
  • 65
    • 0002276579 scopus 로고
    • Time-resolved spectroscopy of the primary electron transfer in reaction centers of Rhodobacter sphaeroides and Rhodopseudomonas viridis
    • J. Deisenhofer and J. Norris, editors. Academic Press, London, UK
    • Zinth, W., and W. Kaiser. 1993. Time-resolved spectroscopy of the primary electron transfer in reaction centers of Rhodobacter sphaeroides and Rhodopseudomonas viridis. In The Photosynthetic Reaction Center. J. Deisenhofer and J. Norris, editors. Academic Press, London, UK. 71.
    • (1993) The Photosynthetic Reaction Center , pp. 71
    • Zinth, W.1    Kaiser, W.2


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