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Volumn 17, Issue 5, 2009, Pages 637-650

Plant Photosystem I Design in the Light of Evolution

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; PLASTOCYANIN; PROTEIN SUBUNIT;

EID: 65149100167     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2009.03.006     Document Type: Review
Times cited : (85)

References (145)
  • 1
    • 0035651544 scopus 로고    scopus 로고
    • Molecular recognition in thylakoid structure and function
    • Allen J.F., and Forsberg J. Molecular recognition in thylakoid structure and function. Trends Plant Sci. 6 (2001) 317-326
    • (2001) Trends Plant Sci. , vol.6 , pp. 317-326
    • Allen, J.F.1    Forsberg, J.2
  • 2
    • 76149090474 scopus 로고    scopus 로고
    • Structures of proteins and cofactors: X-ray crystallography
    • 10.1007/s11120-009-9416-4 in press. Published online March 26, 2009
    • Allen J.P., Seng C., and Larson C. Structures of proteins and cofactors: X-ray crystallography. Photosynth. Res. (2009) 10.1007/s11120-009-9416-4 in press. Published online March 26, 2009
    • (2009) Photosynth. Res.
    • Allen, J.P.1    Seng, C.2    Larson, C.3
  • 3
    • 40849083514 scopus 로고    scopus 로고
    • Functional organization of a plant photosystem I: evolution of a highly efficient photochemical machine
    • Amunts A., and Nelson N. Functional organization of a plant photosystem I: evolution of a highly efficient photochemical machine. Plant Physiol. Biochem. 46 (2008) 228-237
    • (2008) Plant Physiol. Biochem. , vol.46 , pp. 228-237
    • Amunts, A.1    Nelson, N.2
  • 4
    • 29144468957 scopus 로고    scopus 로고
    • Solving the structure of plant photosystem I: biochemistry is vital
    • Amunts A., Ben-Shem A., and Nelson N. Solving the structure of plant photosystem I: biochemistry is vital. Photochem. Photobiol. Sci. 4 (2005) 1011-1015
    • (2005) Photochem. Photobiol. Sci. , vol.4 , pp. 1011-1015
    • Amunts, A.1    Ben-Shem, A.2    Nelson, N.3
  • 5
    • 34247576821 scopus 로고    scopus 로고
    • The structure of a plant photosystem I supercomplex at 3.4 Å resolution
    • Amunts A., Drory O., and Nelson N. The structure of a plant photosystem I supercomplex at 3.4 Å resolution. Nature 447 (2007) 58-63
    • (2007) Nature , vol.447 , pp. 58-63
    • Amunts, A.1    Drory, O.2    Nelson, N.3
  • 7
    • 0026722604 scopus 로고
    • The PSI-E subunit of photosystem I binds ferredoxin:NADP+ oxidoreductase
    • Andersen B., Scheller H.V., and Møller B.L. The PSI-E subunit of photosystem I binds ferredoxin:NADP+ oxidoreductase. FEBS Lett. 311 (1992) 169-173
    • (1992) FEBS Lett. , vol.311 , pp. 169-173
    • Andersen, B.1    Scheller, H.V.2    Møller, B.L.3
  • 8
    • 34247863709 scopus 로고    scopus 로고
    • Contrasting behavior of higher plant photosystem I and II antenna systems during acclimation
    • Ballottari M., Dall'Osto L., Morosinotto T., and Bassi R. Contrasting behavior of higher plant photosystem I and II antenna systems during acclimation. J. Biol. Chem. 282 (2007) 8947-8958
    • (2007) J. Biol. Chem. , vol.282 , pp. 8947-8958
    • Ballottari, M.1    Dall'Osto, L.2    Morosinotto, T.3    Bassi, R.4
  • 9
    • 66449120007 scopus 로고    scopus 로고
    • Crystallization, structure, and function of plant light-harvesting Complex II
    • 10.1016/j.bbabio.2009.03.012 in press. Published online March 25, 2009
    • Barros T., and Kühlbrandtr W. Crystallization, structure, and function of plant light-harvesting Complex II. Biochim. Biophys. Acta. (2009) 10.1016/j.bbabio.2009.03.012 in press. Published online March 25, 2009
    • (2009) Biochim. Biophys. Acta.
    • Barros, T.1    Kühlbrandtr, W.2
  • 10
    • 21244447030 scopus 로고    scopus 로고
    • Biochemical and biophysical characterization of photosystem I from phytoene desaturase and zeta-carotene desaturase deletion mutants of Synechocystis Sp. PCC 6803: evidence for PsaA- and PsaB-side electron transport in cyanobacteria
    • Bautista J.A., Rappaport F., Guergova-Kuras M., Cohen R., Golbeck J., Wang J.Y., Béal D., and Diner B. Biochemical and biophysical characterization of photosystem I from phytoene desaturase and zeta-carotene desaturase deletion mutants of Synechocystis Sp. PCC 6803: evidence for PsaA- and PsaB-side electron transport in cyanobacteria. J. Biol. Chem. 280 (2005) 20030-20041
    • (2005) J. Biol. Chem. , vol.280 , pp. 20030-20041
    • Bautista, J.A.1    Rappaport, F.2    Guergova-Kuras, M.3    Cohen, R.4    Golbeck, J.5    Wang, J.Y.6    Béal, D.7    Diner, B.8
  • 11
    • 14544282417 scopus 로고    scopus 로고
    • State transitions and light adaptation require chloroplast thylakoid protein kinase STN7
    • Bellafiore S., Barneche F., Peltier G., and Rochaix J.-D. State transitions and light adaptation require chloroplast thylakoid protein kinase STN7. Nature 433 (2005) 892-895
    • (2005) Nature , vol.433 , pp. 892-895
    • Bellafiore, S.1    Barneche, F.2    Peltier, G.3    Rochaix, J.-D.4
  • 12
    • 0348148910 scopus 로고    scopus 로고
    • Crystal structure of plant photosystem I
    • Ben-Shem A., Frolow F., and Nelson N. Crystal structure of plant photosystem I. Nature 426 (2003) 630-635
    • (2003) Nature , vol.426 , pp. 630-635
    • Ben-Shem, A.1    Frolow, F.2    Nelson, N.3
  • 13
    • 1942436332 scopus 로고    scopus 로고
    • Evolution of photosystem I-from symmetry through pseudo-symmetry to asymmetry
    • Ben-Shem A., Frolow F., and Nelson N. Evolution of photosystem I-from symmetry through pseudo-symmetry to asymmetry. FEBS Lett. 564 (2004) 274-280
    • (2004) FEBS Lett. , vol.564 , pp. 274-280
    • Ben-Shem, A.1    Frolow, F.2    Nelson, N.3
  • 14
    • 0016861451 scopus 로고
    • Purification and properties of the photosystem I reaction center from chloroplasts
    • Bengis C., and Nelson N. Purification and properties of the photosystem I reaction center from chloroplasts. J. Biol. Chem. 250 (1975) 2783-2788
    • (1975) J. Biol. Chem. , vol.250 , pp. 2783-2788
    • Bengis, C.1    Nelson, N.2
  • 15
    • 0017397279 scopus 로고
    • Subunit structure of chloroplast photosystem I reaction center
    • Bengis C., and Nelson N. Subunit structure of chloroplast photosystem I reaction center. J. Biol. Chem. 252 (1977) 4564-4569
    • (1977) J. Biol. Chem. , vol.252 , pp. 4564-4569
    • Bengis, C.1    Nelson, N.2
  • 16
    • 0035900750 scopus 로고    scopus 로고
    • Three-dimensional model and characterization of the iron stress-induced CP43′-photosystem I supercomplex isolated from the cyanobacterium Synechocystis PCC 6803
    • Bibby T.S., Nield J., and Barber J. Three-dimensional model and characterization of the iron stress-induced CP43′-photosystem I supercomplex isolated from the cyanobacterium Synechocystis PCC 6803. J. Biol. Chem. 276 (2001) 43246-43252
    • (2001) J. Biol. Chem. , vol.276 , pp. 43246-43252
    • Bibby, T.S.1    Nield, J.2    Barber, J.3
  • 17
    • 0027105895 scopus 로고
    • Origin and early evolution of photosynthesis
    • Blankenship R.E. Origin and early evolution of photosynthesis. Photosynth. Res. 33 (1992) 91-111
    • (1992) Photosynth. Res. , vol.33 , pp. 91-111
    • Blankenship, R.E.1
  • 18
    • 34247488329 scopus 로고    scopus 로고
    • Association of photosystem I and light-harvesting complex II during state transitions
    • Golbeck J. (Ed), Springer, Dordrecht
    • Boekema E., and Kouřil R. Association of photosystem I and light-harvesting complex II during state transitions. In: Golbeck J. (Ed). Photosystem I: The Light-Driven Plastocyanin:Ferredoxin Oxidoreductase (2006), Springer, Dordrecht 41-46
    • (2006) Photosystem I: The Light-Driven Plastocyanin:Ferredoxin Oxidoreductase , pp. 41-46
    • Boekema, E.1    Kouřil, R.2
  • 19
    • 0025219925 scopus 로고
    • The structure of spinach photosystem I studied by electron microscopy
    • Boekema E., Wynn R., and Malkin R. The structure of spinach photosystem I studied by electron microscopy. Biochim. Biophys. Acta 1017 (1990) 49-56
    • (1990) Biochim. Biophys. Acta , vol.1017 , pp. 49-56
    • Boekema, E.1    Wynn, R.2    Malkin, R.3
  • 22
    • 0035812833 scopus 로고    scopus 로고
    • Role of acidic amino acid residues of PsaD subunit on limiting the affinity of photosystem I for ferredoxin
    • Bottin H., Hanley J., and Lagoutte B. Role of acidic amino acid residues of PsaD subunit on limiting the affinity of photosystem I for ferredoxin. Biochem. Biophys. Res. Commun. 287 (2001) 833-836
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 833-836
    • Bottin, H.1    Hanley, J.2    Lagoutte, B.3
  • 23
    • 0035976011 scopus 로고    scopus 로고
    • Electron transfer in photosystem I
    • Brettel K., and Leibl W. Electron transfer in photosystem I. Biochim. Biophys. Acta 1507 (2001) 100-114
    • (2001) Biochim. Biophys. Acta , vol.1507 , pp. 100-114
    • Brettel, K.1    Leibl, W.2
  • 25
    • 0040313551 scopus 로고    scopus 로고
    • FTIR study of the primary electron donor of photosystem I (P700) revealing delocalization of the charge in P700+ and localization of the triplet character in 3P700
    • Breton J., Nabedryk E., and Leibl W. FTIR study of the primary electron donor of photosystem I (P700) revealing delocalization of the charge in P700+ and localization of the triplet character in 3P700. Biochemistry 38 (1999) 11585-11592
    • (1999) Biochemistry , vol.38 , pp. 11585-11592
    • Breton, J.1    Nabedryk, E.2    Leibl, W.3
  • 26
    • 0033551919 scopus 로고    scopus 로고
    • Archean molecular fossils and the early rise of eukyotes
    • Brocks J.J., Logan G.A., Buick R., and Summons R.E. Archean molecular fossils and the early rise of eukyotes. Science 285 (1999) 1033-1036
    • (1999) Science , vol.285 , pp. 1033-1036
    • Brocks, J.J.1    Logan, G.A.2    Buick, R.3    Summons, R.E.4
  • 27
    • 0026614460 scopus 로고
    • The antiquity of oxygenic photosynthesis: evidence from stromatolites in sulfate-deficient Archean lakes
    • Buick R. The antiquity of oxygenic photosynthesis: evidence from stromatolites in sulfate-deficient Archean lakes. Science 255 (1992) 74-77
    • (1992) Science , vol.255 , pp. 74-77
    • Buick, R.1
  • 29
    • 35348980719 scopus 로고    scopus 로고
    • Photovoltaic activity of photosystem I-based self-assembled monolayer
    • Carmeli I., Frolov L., Carmeli C., and Richter S. Photovoltaic activity of photosystem I-based self-assembled monolayer. J. Am. Chem. Soc. 129 (2007) 12352-12353
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 12352-12353
    • Carmeli, I.1    Frolov, L.2    Carmeli, C.3    Richter, S.4
  • 32
    • 34249308864 scopus 로고    scopus 로고
    • Amino acids in the second transmembrane helix of the Lhca4 subunit are important for formation of stable heterodimeric light-harvesting complex LHCI-730
    • Corbet D., Schweikardt T., Paulsen H., and Schmid V.H. Amino acids in the second transmembrane helix of the Lhca4 subunit are important for formation of stable heterodimeric light-harvesting complex LHCI-730. J. Mol. Biol. 370 (2007) 170-182
    • (2007) J. Mol. Biol. , vol.370 , pp. 170-182
    • Corbet, D.1    Schweikardt, T.2    Paulsen, H.3    Schmid, V.H.4
  • 33
    • 1942534616 scopus 로고    scopus 로고
    • Evidence for asymmetric electron transfer in cyanobacterial photosystem I: analysis of a methionine to leucine mutation of the ligand to the primary electron acceptor A0
    • Cohen R.O., Shen G., Golbeck J.H., Xu W., Chitnis P.R., Valieva A.I., van der Est A., Pushkar Y., and Stehlik D. Evidence for asymmetric electron transfer in cyanobacterial photosystem I: analysis of a methionine to leucine mutation of the ligand to the primary electron acceptor A0. Biochemistry 43 (2004) 4741-4754
    • (2004) Biochemistry , vol.43 , pp. 4741-4754
    • Cohen, R.O.1    Shen, G.2    Golbeck, J.H.3    Xu, W.4    Chitnis, P.R.5    Valieva, A.I.6    van der Est, A.7    Pushkar, Y.8    Stehlik, D.9
  • 34
    • 0032535215 scopus 로고    scopus 로고
    • A thermal broadening study of the antenna chlorophylls in PSI-200, LHCI, and PSI core
    • Croce R., Zucchelli G., Garlaschi F.M., and Jennings R.C. A thermal broadening study of the antenna chlorophylls in PSI-200, LHCI, and PSI core. Biochemistry 37 (1998) 17355-17360
    • (1998) Biochemistry , vol.37 , pp. 17355-17360
    • Croce, R.1    Zucchelli, G.2    Garlaschi, F.M.3    Jennings, R.C.4
  • 36
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 Å resolution
    • Deisenhofer J., Epp O., Miki K., Huber R., and Michel H. Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 Å resolution. Nature 318 (1985) 618-624
    • (1985) Nature , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 39
    • 0001269186 scopus 로고    scopus 로고
    • Banfield and Nealson, eds, Washington, DC: Mineralogical Society of America
    • De Marais, D.J. (1997). Geomicrobiology, Banfield and Nealson, eds. (Washington, DC: Mineralogical Society of America), 35, 429-445.
    • (1997) Geomicrobiology , vol.35 , pp. 429-445
    • De Marais, D.J.1
  • 40
    • 0034623416 scopus 로고    scopus 로고
    • Evolution. When did photosynthesis emerge on Earth?
    • De Marais D.J. Evolution. When did photosynthesis emerge on Earth?. Science 289 (2000) 1703-1705
    • (2000) Science , vol.289 , pp. 1703-1705
    • De Marais, D.J.1
  • 42
    • 0002929188 scopus 로고
    • Localization and nucleotide sequence of the gene for the 8 Kda subunit of photosystem I reaction center in pea and wheat chloroplast DNA
    • Dunn P., and Gray J. Localization and nucleotide sequence of the gene for the 8 Kda subunit of photosystem I reaction center in pea and wheat chloroplast DNA. Plant Mol. Biol. 11 (1988) 311-319
    • (1988) Plant Mol. Biol. , vol.11 , pp. 311-319
    • Dunn, P.1    Gray, J.2
  • 43
    • 0029775299 scopus 로고    scopus 로고
    • Mid-ocean ridge hydrothermal fluxes and the chemical composition of the ocean
    • Elderfield H., and Schultz A. Mid-ocean ridge hydrothermal fluxes and the chemical composition of the ocean. Annu. Rev. Earth Planet. Sci. 24 (1996) 191-224
    • (1996) Annu. Rev. Earth Planet. Sci. , vol.24 , pp. 191-224
    • Elderfield, H.1    Schultz, A.2
  • 44
    • 0033612696 scopus 로고    scopus 로고
    • Characterization of ferredoxin and flavodoxin as markers of iron limitation in marine phytoplankton
    • Erdner D.L., Price N.M., Doucette G.J., Peleato M.L., and Anderson D.M. Characterization of ferredoxin and flavodoxin as markers of iron limitation in marine phytoplankton. Mar. Ecol. Prog. Ser. 184 (1999) 43-53
    • (1999) Mar. Ecol. Prog. Ser. , vol.184 , pp. 43-53
    • Erdner, D.L.1    Price, N.M.2    Doucette, G.J.3    Peleato, M.L.4    Anderson, D.M.5
  • 45
    • 0142042969 scopus 로고    scopus 로고
    • Bidirectional electron transfer in photosystem I: electron transfer on the PsaA side is not essential for phototrophic growth in Chlamydomonas
    • Fairclough W.V., Forsyth A., Evans M.C., Rigby S.E., Purton S., and Heathcote P. Bidirectional electron transfer in photosystem I: electron transfer on the PsaA side is not essential for phototrophic growth in Chlamydomonas. Biochim. Biophys. Acta 1606 (2003) 43-55
    • (2003) Biochim. Biophys. Acta , vol.1606 , pp. 43-55
    • Fairclough, W.V.1    Forsyth, A.2    Evans, M.C.3    Rigby, S.E.4    Purton, S.5    Heathcote, P.6
  • 46
    • 0032481379 scopus 로고    scopus 로고
    • The PsaC subunit of photosystem I provides an essential lysine residue for fast electron transfer to ferredoxin
    • Fischer N., Hippler M., Sétif P., Jacquot J.P., and Rochaix J.-D. The PsaC subunit of photosystem I provides an essential lysine residue for fast electron transfer to ferredoxin. EMBO J. 17 (1998) 849-858
    • (1998) EMBO J. , vol.17 , pp. 849-858
    • Fischer, N.1    Hippler, M.2    Sétif, P.3    Jacquot, J.P.4    Rochaix, J.-D.5
  • 47
    • 0039777928 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the PsaC subunit of photosystem I. F(b) is the cluster interacting with soluble ferredoxin
    • Fischer N., Sétif P., and Rochaix J.-D. Site-directed mutagenesis of the PsaC subunit of photosystem I. F(b) is the cluster interacting with soluble ferredoxin. J. Biol. Chem. 274 (1999) 23333-23340
    • (1999) J. Biol. Chem. , vol.274 , pp. 23333-23340
    • Fischer, N.1    Sétif, P.2    Rochaix, J.-D.3
  • 48
    • 84981779372 scopus 로고
    • Intermolecular energy migration and fluorescence
    • Förster T. Intermolecular energy migration and fluorescence. Ann. Phys. 2 (1948) 55-75
    • (1948) Ann. Phys. , vol.2 , pp. 55-75
    • Förster, T.1
  • 51
    • 3042801997 scopus 로고    scopus 로고
    • Unraveling the photosystem I reaction center: a history, or the sum of many efforts
    • Fromme P., and Mathis P. Unraveling the photosystem I reaction center: a history, or the sum of many efforts. Photosynth. Res. 80 (2004) 109-124
    • (2004) Photosynth. Res. , vol.80 , pp. 109-124
    • Fromme, P.1    Mathis, P.2
  • 53
    • 0242573143 scopus 로고    scopus 로고
    • Structure and function of photosystem I: interaction with its soluble electron carriers and external antenna systems
    • Fromme P., Melkozernov A., Jordan P., and Krauß N. Structure and function of photosystem I: interaction with its soluble electron carriers and external antenna systems. FEBS Lett. 555 (2003) 40-44
    • (2003) FEBS Lett. , vol.555 , pp. 40-44
    • Fromme, P.1    Melkozernov, A.2    Jordan, P.3    Krauß, N.4
  • 54
    • 65149104494 scopus 로고    scopus 로고
    • Structure of Photosystem I and its natural electron acceptor ferredoxin in co-crystals at 3.8 Å resolution. EBEC 2008 15th European Bioenergetic Conference
    • Fromme R., Yu H., Jolley C., Grotjohann I., Wang M., Sétif P., Bottin H., and Fromme P. Structure of Photosystem I and its natural electron acceptor ferredoxin in co-crystals at 3.8 Å resolution. EBEC 2008 15th European Bioenergetic Conference. Biochim. Biophys. Acta. 1777 Suppl 1 (2008) S2-11
    • (2008) Biochim. Biophys. Acta. , vol.1777 , Issue.SUPPL. 1
    • Fromme, R.1    Yu, H.2    Jolley, C.3    Grotjohann, I.4    Wang, M.5    Sétif, P.6    Bottin, H.7    Fromme, P.8
  • 55
    • 0037077690 scopus 로고    scopus 로고
    • Supramolecular organization of photosystem I and light-harvesting complex I in Chlamydomonas reinhardtii
    • Germano M., Yakushevska A.E., Keegstra W., van Gorkom H.J., Dekker J.P., and Boekema E. Supramolecular organization of photosystem I and light-harvesting complex I in Chlamydomonas reinhardtii. FEBS Lett. 525 (2002) 121-125
    • (2002) FEBS Lett. , vol.525 , pp. 121-125
    • Germano, M.1    Yakushevska, A.E.2    Keegstra, W.3    van Gorkom, H.J.4    Dekker, J.P.5    Boekema, E.6
  • 56
    • 0035976020 scopus 로고    scopus 로고
    • Energy transfer and trapping in photosystem I
    • Gobets B., and van Grondelle R. Energy transfer and trapping in photosystem I. Biochim. Biophys. Acta 1507 (2001) 80-99
    • (2001) Biochim. Biophys. Acta , vol.1507 , pp. 80-99
    • Gobets, B.1    van Grondelle, R.2
  • 57
    • 0029967212 scopus 로고    scopus 로고
    • Reconstitution and pigment-binding properties of recombinant CP29
    • Giuffra E., Cugini D., Croce R., and Bassi R. Reconstitution and pigment-binding properties of recombinant CP29. Eur. J. Biochem. 238 (1996) 112-120
    • (1996) Eur. J. Biochem. , vol.238 , pp. 112-120
    • Giuffra, E.1    Cugini, D.2    Croce, R.3    Bassi, R.4
  • 59
    • 18844405410 scopus 로고    scopus 로고
    • Structure of cyanobacterial photosystem I
    • Grotjohann I., and Fromme P. Structure of cyanobacterial photosystem I. Photosynth. Res. 85 (2005) 51-72
    • (2005) Photosynth. Res. , vol.85 , pp. 51-72
    • Grotjohann, I.1    Fromme, P.2
  • 60
    • 0029943262 scopus 로고    scopus 로고
    • Mutagenesis of photosystem I in the region of the ferredoxin cross-linking site: modifications of positively charged amino acids
    • Hanley J., Sétif P., Bottin H., and Lagoutte B. Mutagenesis of photosystem I in the region of the ferredoxin cross-linking site: modifications of positively charged amino acids. Biochemistry 35 (1996) 8563-8571
    • (1996) Biochemistry , vol.35 , pp. 8563-8571
    • Hanley, J.1    Sétif, P.2    Bottin, H.3    Lagoutte, B.4
  • 62
    • 0030990023 scopus 로고    scopus 로고
    • Fast electron transfer from cytochrome c6 and plastocyanin to photosystem I of Chlamydomonas reinhardtii requires PsaF
    • Hippler M., Drepper F., Farah J., and Rochaix J.D. Fast electron transfer from cytochrome c6 and plastocyanin to photosystem I of Chlamydomonas reinhardtii requires PsaF. Biochemistry 36 (1997) 6343-6349
    • (1997) Biochemistry , vol.36 , pp. 6343-6349
    • Hippler, M.1    Drepper, F.2    Farah, J.3    Rochaix, J.D.4
  • 63
    • 0032560513 scopus 로고    scopus 로고
    • The N-terminal domain of PsaF: precise recognition site for binding and fast electron transfer from cytochrome c6 and plastocyanin to photosystem I of Chlamydomonas reinhardtii
    • Hippler M., Drepper F., Haehnel W., and Rochaix J.-D. The N-terminal domain of PsaF: precise recognition site for binding and fast electron transfer from cytochrome c6 and plastocyanin to photosystem I of Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA 95 (1998) 7339-7344
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7339-7344
    • Hippler, M.1    Drepper, F.2    Haehnel, W.3    Rochaix, J.-D.4
  • 64
    • 0033548179 scopus 로고    scopus 로고
    • Insertion of the N-terminal part of PsaF from Chlamydomonas reinhardtii into photosystem I from Synechococcus elongatus enables efficient binding of algal plastocyanin and cytochrome c6
    • Hippler M., Drepper F., Rochaix J.-D., and Mühlenhoff U. Insertion of the N-terminal part of PsaF from Chlamydomonas reinhardtii into photosystem I from Synechococcus elongatus enables efficient binding of algal plastocyanin and cytochrome c6. J. Biol. Chem. 274 (1999) 4180-4188
    • (1999) J. Biol. Chem. , vol.274 , pp. 4180-4188
    • Hippler, M.1    Drepper, F.2    Rochaix, J.-D.3    Mühlenhoff, U.4
  • 65
    • 84899560525 scopus 로고
    • Electron donors to P700 in cyanobacteria and algae. An instance of unusual genetic variability
    • Ho K.K., and Krogmann D.W. Electron donors to P700 in cyanobacteria and algae. An instance of unusual genetic variability. Biochim. Biophys. Acta 766 (1984) 310-316
    • (1984) Biochim. Biophys. Acta , vol.766 , pp. 310-316
    • Ho, K.K.1    Krogmann, D.W.2
  • 66
    • 0001972707 scopus 로고    scopus 로고
    • Structure-function relationship and excitation dynamics in photosystem I
    • Garab G. (Ed), Kluwer Academic Publishers, Dordrecht, the Netherlands
    • Holzwarth A.R., Dorra D., Muller M., and Karapetyan N.V. Structure-function relationship and excitation dynamics in photosystem I. In: Garab G. (Ed). Photosynthesis: Mechanisms and Effects (1998), Kluwer Academic Publishers, Dordrecht, the Netherlands 497-502
    • (1998) Photosynthesis: Mechanisms and Effects , pp. 497-502
    • Holzwarth, A.R.1    Dorra, D.2    Muller, M.3    Karapetyan, N.V.4
  • 67
    • 33646199160 scopus 로고    scopus 로고
    • Ultrafast transient absorption studies on photosystem I reaction centers from Chlamydomonas reinhardtii. 2: mutations near the P700 reaction center chlorophylls provide new insight into the nature of the primary electron donor
    • Holzwarth A., Müller M., Niklas J., and Lubitz W. Ultrafast transient absorption studies on photosystem I reaction centers from Chlamydomonas reinhardtii. 2: mutations near the P700 reaction center chlorophylls provide new insight into the nature of the primary electron donor. Biophys J. 90 (2006) 552-565
    • (2006) Biophys J. , vol.90 , pp. 552-565
    • Holzwarth, A.1    Müller, M.2    Niklas, J.3    Lubitz, W.4
  • 68
    • 0037169520 scopus 로고    scopus 로고
    • Photosystem I activity is increased in the absence of the PSI-G
    • Jensen P.E., Rosgaard L., Knoetzel J., and Scheller H.V. Photosystem I activity is increased in the absence of the PSI-G. J. Biol. Chem. 277 (2002) 2789-2803
    • (2002) J. Biol. Chem. , vol.277 , pp. 2789-2803
    • Jensen, P.E.1    Rosgaard, L.2    Knoetzel, J.3    Scheller, H.V.4
  • 70
    • 0033600564 scopus 로고    scopus 로고
    • In vivo analysis of the electron transfer within photosystem I: are the two phylloquinones involved?
    • Joliot P., and Joliot A. In vivo analysis of the electron transfer within photosystem I: are the two phylloquinones involved?. Biochemistry 38 (1999) 11130-11136
    • (1999) Biochemistry , vol.38 , pp. 11130-11136
    • Joliot, P.1    Joliot, A.2
  • 71
    • 24144441812 scopus 로고    scopus 로고
    • Structure of plant photosystem I revealed by theoretical modeling
    • Jolley C., Ben-Shem A., Nelson N., and Fromme P. Structure of plant photosystem I revealed by theoretical modeling. J. Biol. Chem. 280 (2005) 33627-33636
    • (2005) J. Biol. Chem. , vol.280 , pp. 33627-33636
    • Jolley, C.1    Ben-Shem, A.2    Nelson, N.3    Fromme, P.4
  • 72
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 A resolution
    • Jordan P., Fromme P., Witt H.T., Klukas O., Saenger W., and Krauß N. Three-dimensional structure of cyanobacterial photosystem I at 2.5 A resolution. Nature 411 (2001) 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
  • 73
    • 4344628472 scopus 로고    scopus 로고
    • The dynamics of excitation energy in photosystem I of cyanobacteria: transfer in the antenna, capture by the reaction site, and dissipation
    • Karapetyan N.V. The dynamics of excitation energy in photosystem I of cyanobacteria: transfer in the antenna, capture by the reaction site, and dissipation. Biofizika 49 (2004) 212-226
    • (2004) Biofizika , vol.49 , pp. 212-226
    • Karapetyan, N.V.1
  • 74
    • 0032731226 scopus 로고    scopus 로고
    • The photosystem I trimer of cyanobacteria: molecular organization, excitation dynamics and physiological significance
    • Karapetyan N.V., Holzwarth A.R., and Rögner M. The photosystem I trimer of cyanobacteria: molecular organization, excitation dynamics and physiological significance. FEBS Lett. 460 (1999) 395-400
    • (1999) FEBS Lett. , vol.460 , pp. 395-400
    • Karapetyan, N.V.1    Holzwarth, A.R.2    Rögner, M.3
  • 75
    • 0033451808 scopus 로고    scopus 로고
    • Energy exchange between the chlorophyll antennae of monomeric subunits within the photosystem I trimeric complex of the cyanobacterium Spirulina
    • Karapetyan N.V., Shubin V.V., and Strasser R.J. Energy exchange between the chlorophyll antennae of monomeric subunits within the photosystem I trimeric complex of the cyanobacterium Spirulina. Photosynth. Res. 61 (1999) 291-301
    • (1999) Photosynth. Res. , vol.61 , pp. 291-301
    • Karapetyan, N.V.1    Shubin, V.V.2    Strasser, R.J.3
  • 76
    • 40349106307 scopus 로고    scopus 로고
    • Photosynthetic acclimation: structural reorganisation of light harvesting antenna - role of redox-dependent phosphorylation of major and minor chlorophyll a/b binding proteins
    • Kargul J., and Barber J. Photosynthetic acclimation: structural reorganisation of light harvesting antenna - role of redox-dependent phosphorylation of major and minor chlorophyll a/b binding proteins. FEBS J. 275 (2008) 1056-1068
    • (2008) FEBS J. , vol.275 , pp. 1056-1068
    • Kargul, J.1    Barber, J.2
  • 77
    • 0037507283 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of a light-harvesting complex I-photosystem I (LHCI-PSI) supercomplex from the green alga Chlamydomonas reinhardtii -insights into light harvesting for PSI
    • Kargul J., Nield J., and Barber J. Three-dimensional reconstruction of a light-harvesting complex I-photosystem I (LHCI-PSI) supercomplex from the green alga Chlamydomonas reinhardtii -insights into light harvesting for PSI. J. Biol. Chem. 278 (2003) 16135-16141
    • (2003) J. Biol. Chem. , vol.278 , pp. 16135-16141
    • Kargul, J.1    Nield, J.2    Barber, J.3
  • 78
    • 25444471029 scopus 로고    scopus 로고
    • Light-harvesting complex II protein CP29 binds to photosystem I of Chlamydomonas reinhardtii under State 2 conditions
    • Kargul J., Turkina M.V., Nield J., Benson S., Vener A.V., and Barber J. Light-harvesting complex II protein CP29 binds to photosystem I of Chlamydomonas reinhardtii under State 2 conditions. FEBS J. 272 (2005) 4797-4806
    • (2005) FEBS J. , vol.272 , pp. 4797-4806
    • Kargul, J.1    Turkina, M.V.2    Nield, J.3    Benson, S.4    Vener, A.V.5    Barber, J.6
  • 79
    • 0032491423 scopus 로고    scopus 로고
    • Three-dimensional structure of higher plant photosystem I determined by electron crystallography
    • Kitmitto A., Mustafa A.O., Holzenburg A., and Ford R.C. Three-dimensional structure of higher plant photosystem I determined by electron crystallography. J. Biol. Chem. 273 (1998) 29592-29599
    • (1998) J. Biol. Chem. , vol.273 , pp. 29592-29599
    • Kitmitto, A.1    Mustafa, A.O.2    Holzenburg, A.3    Ford, R.C.4
  • 80
    • 14544270322 scopus 로고    scopus 로고
    • Structure of the higher plant light harvesting complex I: in vivo characterization and structural interdependence of the Lhca proteins
    • Klimmek F., Ganeteg U., Ihalainen J.A., van Roon H., Jensen P.E., Scheller H.V., Dekker J.P., and Jansson S. Structure of the higher plant light harvesting complex I: in vivo characterization and structural interdependence of the Lhca proteins. Biochemistry 44 (2005) 3065-3073
    • (2005) Biochemistry , vol.44 , pp. 3065-3073
    • Klimmek, F.1    Ganeteg, U.2    Ihalainen, J.A.3    van Roon, H.4    Jensen, P.E.5    Scheller, H.V.6    Dekker, J.P.7    Jansson, S.8
  • 84
    • 0033548273 scopus 로고    scopus 로고
    • Localization of two phylloquinones, QK and QK′, in an improved electron density map of photosystem I at 4-Å resolution
    • Klukas O., Schubert W.D., Jordan P., Krauß N., Fromme P., Witt H.T., and Saenger W. Localization of two phylloquinones, QK and QK′, in an improved electron density map of photosystem I at 4-Å resolution. J. Biol. Chem. 274 (1999) 7361-7367
    • (1999) J. Biol. Chem. , vol.274 , pp. 7361-7367
    • Klukas, O.1    Schubert, W.D.2    Jordan, P.3    Krauß, N.4    Fromme, P.5    Witt, H.T.6    Saenger, W.7
  • 87
    • 0029911269 scopus 로고    scopus 로고
    • Photosystem I at 4Å resolution represents the first structural model of a joint photosynthetic reaction centre and core antenna system
    • Krauß N., Schubert W.D., Klukas O., Fromme P., Witt H.T., and Saenger W. Photosystem I at 4Å resolution represents the first structural model of a joint photosynthetic reaction centre and core antenna system. Nat. Struct. Biol. 3 (1996) 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
  • 88
    • 0037162418 scopus 로고    scopus 로고
    • Aggregation of LHCII leads to a redistribution of the triplets over the central xanthophylls in LHCII
    • Lampoura S.S., Barzda V., Owen G.M., Hoff A.J., and Van Amerongen H. Aggregation of LHCII leads to a redistribution of the triplets over the central xanthophylls in LHCII. Biochemistry 41 (2002) 9139-9144
    • (2002) Biochemistry , vol.41 , pp. 9139-9144
    • Lampoura, S.S.1    Barzda, V.2    Owen, G.M.3    Hoff, A.J.4    Van Amerongen, H.5
  • 89
    • 33846979420 scopus 로고    scopus 로고
    • Toward cost-effective solar energy use
    • Lewis N.S. Toward cost-effective solar energy use. Science 315 (2007) 798-801
    • (2007) Science , vol.315 , pp. 798-801
    • Lewis, N.S.1
  • 90
    • 0027186183 scopus 로고
    • Single core polypeptide in the reaction center of the photosynthetic bacterium Heliobacillus mobilis: structural implications and relations to other photosystems
    • Liebl U., Mockensturm-Wilson M., Trost J., Brune D., Blankenship R., and Vermaas W. Single core polypeptide in the reaction center of the photosynthetic bacterium Heliobacillus mobilis: structural implications and relations to other photosystems. Proc. Natl. Acad. Sci. USA 90 (1993) 7124-7128
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7124-7128
    • Liebl, U.1    Mockensturm-Wilson, M.2    Trost, J.3    Brune, D.4    Blankenship, R.5    Vermaas, W.6
  • 91
    • 0034735803 scopus 로고    scopus 로고
    • The PSI-H subunit of photosystem I is essential for state transitions in plant photosynthesis
    • Lunde C., Jensen P.E., Haldrup A., Knoetzel J., and Scheller H.V. The PSI-H subunit of photosystem I is essential for state transitions in plant photosynthesis. Nature 408 (2000) 613-615
    • (2000) Nature , vol.408 , pp. 613-615
    • Lunde, C.1    Jensen, P.E.2    Haldrup, A.3    Knoetzel, J.4    Scheller, H.V.5
  • 92
    • 36749038668 scopus 로고    scopus 로고
    • EPR studies of the primary electron donor P700 in photosystem I
    • Golbeck J. (Ed), Springer, Dordrecht
    • Lubitz W. EPR studies of the primary electron donor P700 in photosystem I. In: Golbeck J. (Ed). Photosystem I: The Light-Driven Plastocyanin:Ferredoxin Oxidoreductase (2006), Springer, Dordrecht 245-269
    • (2006) Photosystem I: The Light-Driven Plastocyanin:Ferredoxin Oxidoreductase , pp. 245-269
    • Lubitz, W.1
  • 94
    • 0022929856 scopus 로고
    • Removal of ferredoxin:NADP+ oxidoreductase from thylakoid membranes, rebinding to depleted membranes, and identification of the binding site
    • Matthijs H.C., Coughlan S.J., and Hind G. Removal of ferredoxin:NADP+ oxidoreductase from thylakoid membranes, rebinding to depleted membranes, and identification of the binding site. J. Biol. Chem. 261 (1986) 12154-12158
    • (1986) J. Biol. Chem. , vol.261 , pp. 12154-12158
    • Matthijs, H.C.1    Coughlan, S.J.2    Hind, G.3
  • 95
    • 0042565990 scopus 로고    scopus 로고
    • Expression and regulation of the crucial plant-like ferredoxin of cyanobacteria
    • Mazouni K., Domain F., Chauvat F., and Cassier-Chauvat C. Expression and regulation of the crucial plant-like ferredoxin of cyanobacteria. Mol. Microbiol. 49 (2003) 1019-1029
    • (2003) Mol. Microbiol. , vol.49 , pp. 1019-1029
    • Mazouni, K.1    Domain, F.2    Chauvat, F.3    Cassier-Chauvat, C.4
  • 96
    • 27244455478 scopus 로고    scopus 로고
    • The light reactions: a guide to recent acquisitions for the picture gallery
    • Merchant S., and Sawaya M.R. The light reactions: a guide to recent acquisitions for the picture gallery. Plant Cell 17 (2005) 648-663
    • (2005) Plant Cell , vol.17 , pp. 648-663
    • Merchant, S.1    Sawaya, M.R.2
  • 98
    • 0035839096 scopus 로고    scopus 로고
    • Evidence from time resolved studies of the radical pair for photosynthetic electron transfer on both the PsaA and PsaB branches of the photosystem I reaction centre
    • Muhiuddin I.P., Heathcote P., Carter S., Purton S., Rigby S.E.J., and Evans M.C.W. Evidence from time resolved studies of the radical pair for photosynthetic electron transfer on both the PsaA and PsaB branches of the photosystem I reaction centre. FEBS Lett. 503 (2001) 56-60
    • (2001) FEBS Lett. , vol.503 , pp. 56-60
    • Muhiuddin, I.P.1    Heathcote, P.2    Carter, S.3    Purton, S.4    Rigby, S.E.J.5    Evans, M.C.W.6
  • 99
    • 0030848989 scopus 로고    scopus 로고
    • On the origin of photosynthesis as inferred from sequence analysis: a primordial UV-protector as common ancestor of reaction centers and antenna proteins
    • Mulkidjanian A.Y., and Junge W. On the origin of photosynthesis as inferred from sequence analysis: a primordial UV-protector as common ancestor of reaction centers and antenna proteins. Photosynth. Res. 51 (1997) 27-42
    • (1997) Photosynth. Res. , vol.51 , pp. 27-42
    • Mulkidjanian, A.Y.1    Junge, W.2
  • 101
    • 0347510786 scopus 로고    scopus 로고
    • Quenching of chlorophyll a singlets and triplets by carotenoids in light-harvesting complex of photosystem II: comparison of aggregates with trimers
    • Naqvi K.R., Melo T.B., Raju B.B., Javorfi T., Simidjiev I., and Garab G. Quenching of chlorophyll a singlets and triplets by carotenoids in light-harvesting complex of photosystem II: comparison of aggregates with trimers. Spectrochim. Acta A Mol. Biomol. Spectrosc. 53 (1997) 2659-2667
    • (1997) Spectrochim. Acta A Mol. Biomol. Spectrosc. , vol.53 , pp. 2659-2667
    • Naqvi, K.R.1    Melo, T.B.2    Raju, B.B.3    Javorfi, T.4    Simidjiev, I.5    Garab, G.6
  • 102
    • 10044254637 scopus 로고    scopus 로고
    • The complex architecture of oxygenic photosynthesis
    • Nelson N., and Ben-Shem A. The complex architecture of oxygenic photosynthesis. Nat. Rev. Mol. Cell Biol. 5 (2004) 971-982
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 971-982
    • Nelson, N.1    Ben-Shem, A.2
  • 103
    • 26244457474 scopus 로고    scopus 로고
    • The structure of photosystem I and evolution of photosynthesis
    • Nelson N., and Ben-Shem A. The structure of photosystem I and evolution of photosynthesis. Bioessays 27 (2005) 914-922
    • (2005) Bioessays , vol.27 , pp. 914-922
    • Nelson, N.1    Ben-Shem, A.2
  • 104
    • 33745936562 scopus 로고    scopus 로고
    • Structure and function of photosystems I and II
    • Nelson N., and Yocum C. Structure and function of photosystems I and II. Annu. Rev. Plant Biol. 57 (2006) 521-565
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 521-565
    • Nelson, N.1    Yocum, C.2
  • 109
    • 55649094623 scopus 로고    scopus 로고
    • Optical measurements of secondary electron transfer in photosystem I
    • Golbeck J. (Ed), Springer, Dordrecht
    • Rappaport F. Optical measurements of secondary electron transfer in photosystem I. In: Golbeck J. (Ed). Photosystem I: The Light-Driven Plastocyanin:Ferredoxin Oxidoreductase (2006), Springer, Dordrecht 224-244
    • (2006) Photosystem I: The Light-Driven Plastocyanin:Ferredoxin Oxidoreductase , pp. 224-244
    • Rappaport, F.1
  • 110
    • 0034621829 scopus 로고    scopus 로고
    • Filamentous microfossils in a 3,235-million-year-old volcanogenic massive sulphide deposit
    • Rasmussen B. Filamentous microfossils in a 3,235-million-year-old volcanogenic massive sulphide deposit. Nature 405 (2000) 676-679
    • (2000) Nature , vol.405 , pp. 676-679
    • Rasmussen, B.1
  • 111
    • 0034680853 scopus 로고    scopus 로고
    • The location of the mobile electron carrier ferredoxin in vascular plant photosystem I
    • Ruffle S.V., Mustafa A.O., Kitmitto A., Holzenburg A., and Ford R.C. The location of the mobile electron carrier ferredoxin in vascular plant photosystem I. J. Biol. Chem. 275 (2000) 36250-36255
    • (2000) J. Biol. Chem. , vol.275 , pp. 36250-36255
    • Ruffle, S.V.1    Mustafa, A.O.2    Kitmitto, A.3    Holzenburg, A.4    Ford, R.C.5
  • 114
    • 0030740474 scopus 로고    scopus 로고
    • In vitro reconstitution of the photosystem I light-harvesting complex LHCI-730: heterodimerization is required for antenna pigment organization
    • Schmid V.H., Cammarata K.V., Bruns B.U., and Schmidt G.W. In vitro reconstitution of the photosystem I light-harvesting complex LHCI-730: heterodimerization is required for antenna pigment organization. Proc. Natl. Acad. Sci. USA 94 (1997) 7667-7672
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7667-7672
    • Schmid, V.H.1    Cammarata, K.V.2    Bruns, B.U.3    Schmidt, G.W.4
  • 115
    • 0037162395 scopus 로고    scopus 로고
    • Identification of N- and C-terminal amino acids of Lhca1 and Lhca4 required for formation of the heterodimeric peripheral photosystem I antenna LHCI-730
    • Schmid V.H., Paulsen H., and Rupprecht J. Identification of N- and C-terminal amino acids of Lhca1 and Lhca4 required for formation of the heterodimeric peripheral photosystem I antenna LHCI-730. Biochemistry 41 (2002) 9126-9131
    • (2002) Biochemistry , vol.41 , pp. 9126-9131
    • Schmid, V.H.1    Paulsen, H.2    Rupprecht, J.3
  • 116
    • 0031563799 scopus 로고    scopus 로고
    • Photosystem I of Synechococcus elongatus at 4 Å resolution: comprehensive structure analysis
    • Schubert W.D., Klukas O., Krauß N., Saenger W., Fromme P., and Witt H.T. Photosystem I of Synechococcus elongatus at 4 Å resolution: comprehensive structure analysis. J. Mol. Biol. 272 (1997) 741-769
    • (1997) J. Mol. Biol. , vol.272 , pp. 741-769
    • Schubert, W.D.1    Klukas, O.2    Krauß, N.3    Saenger, W.4    Fromme, P.5    Witt, H.T.6
  • 117
    • 24144496800 scopus 로고    scopus 로고
    • Comparison of the light-harvesting networks of plant and cyanobacterial photosystem I
    • Sener M.K., Jolley C., Ben-Shem A., Fromme P., Nelson N., Croce R., and Schulten K. Comparison of the light-harvesting networks of plant and cyanobacterial photosystem I. Biophys. J. 89 (2005) 1630-1642
    • (2005) Biophys. J. , vol.89 , pp. 1630-1642
    • Sener, M.K.1    Jolley, C.2    Ben-Shem, A.3    Fromme, P.4    Nelson, N.5    Croce, R.6    Schulten, K.7
  • 119
    • 1642506307 scopus 로고    scopus 로고
    • Microarray analysis and redox control of gene expression in the cyanobacterium Synechocystis sp. PCC 6803
    • Singh A.K., Li H., and Sherman L.A. Microarray analysis and redox control of gene expression in the cyanobacterium Synechocystis sp. PCC 6803. Physiol. Plant. 120 (2004) 27-35
    • (2004) Physiol. Plant. , vol.120 , pp. 27-35
    • Singh, A.K.1    Li, H.2    Sherman, L.A.3
  • 120
    • 43649104636 scopus 로고    scopus 로고
    • Trap-limited charge separation kinetics in higher plant photosystem I complexes
    • Slavov C., Ballottari M., Morosinotto T., Bassi R., and Holzwarth A. Trap-limited charge separation kinetics in higher plant photosystem I complexes. Biophys J. 94 (2008) 3601-3612
    • (2008) Biophys J. , vol.94 , pp. 3601-3612
    • Slavov, C.1    Ballottari, M.2    Morosinotto, T.3    Bassi, R.4    Holzwarth, A.5
  • 121
    • 33845920682 scopus 로고    scopus 로고
    • Identification of precise electrostatic recognition sites between cytochrome c6 and the photosystem I subunit PsaF using mass spectrometry
    • Sommer F., Drepper F., Haehnel W., and Hippler M. Identification of precise electrostatic recognition sites between cytochrome c6 and the photosystem I subunit PsaF using mass spectrometry. J. Biol. Chem. 281 (2006) 35097-35103
    • (2006) J. Biol. Chem. , vol.281 , pp. 35097-35103
    • Sommer, F.1    Drepper, F.2    Haehnel, W.3    Hippler, M.4
  • 122
    • 16344363252 scopus 로고    scopus 로고
    • Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 Å resolution
    • Standfuss J., Terwisscha van Scheltinga A.C., Lamborghini M., and Kühlbrandt W. Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 Å resolution. EMBO J. 24 (2005) 919-928
    • (2005) EMBO J. , vol.24 , pp. 919-928
    • Standfuss, J.1    Terwisscha van Scheltinga, A.C.2    Lamborghini, M.3    Kühlbrandt, W.4
  • 123
    • 34648859918 scopus 로고    scopus 로고
    • Transient EPR spectroscopy as applied to light-induced functional intermediates along the electron transfer pathway in photosystem I
    • Golbeck J. (Ed), Springer, Dordrecht
    • Stehlik D. Transient EPR spectroscopy as applied to light-induced functional intermediates along the electron transfer pathway in photosystem I. In: Golbeck J. (Ed). Photosystem I: The Light-Driven Plastocyanin:Ferredoxin Oxidoreductase (2006), Springer, Dordrecht 361-386
    • (2006) Photosystem I: The Light-Driven Plastocyanin:Ferredoxin Oxidoreductase , pp. 361-386
    • Stehlik, D.1
  • 124
    • 0033527055 scopus 로고    scopus 로고
    • 2-Methylhopanoids as biomarkers for cyanobacterial oxygenic photosynthesis
    • Summons R.E., Jahnke L.L., Hope J.M., and Logan G.A. 2-Methylhopanoids as biomarkers for cyanobacterial oxygenic photosynthesis. Nature 400 (1999) 554-557
    • (1999) Nature , vol.400 , pp. 554-557
    • Summons, R.E.1    Jahnke, L.L.2    Hope, J.M.3    Logan, G.A.4
  • 125
    • 31044439022 scopus 로고    scopus 로고
    • Identification of the mobile light-harvesting complex II polypeptides for state transitions in Chlamydomonas reinhardtii
    • Takahashi H., Iwai M., Takahashi Y., and Minagawa J. Identification of the mobile light-harvesting complex II polypeptides for state transitions in Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA 103 (2006) 477-482
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 477-482
    • Takahashi, H.1    Iwai, M.2    Takahashi, Y.3    Minagawa, J.4
  • 129
    • 33747488135 scopus 로고    scopus 로고
    • Functional replacement of ferredoxin by a cyanobacterial flavodoxin in tobacco confers broad-range stress tolerance
    • Tognetti V.B., Palatnik J.F., Fillat M.F., Melzer M., Hajirezaei M.R., Valle E.M., and Carrillo N. Functional replacement of ferredoxin by a cyanobacterial flavodoxin in tobacco confers broad-range stress tolerance. Plant Cell 18 (2006) 2035-2050
    • (2006) Plant Cell , vol.18 , pp. 2035-2050
    • Tognetti, V.B.1    Palatnik, J.F.2    Fillat, M.F.3    Melzer, M.4    Hajirezaei, M.R.5    Valle, E.M.6    Carrillo, N.7
  • 131
    • 23144435792 scopus 로고    scopus 로고
    • Microscopy and single molecule detection in photosynthesis
    • Vacha F., Bumba L., Kaftan D., and Vacha M. Microscopy and single molecule detection in photosynthesis. Micron 36 (2005) 483-502
    • (2005) Micron , vol.36 , pp. 483-502
    • Vacha, F.1    Bumba, L.2    Kaftan, D.3    Vacha, M.4
  • 132
    • 0029139611 scopus 로고
    • Description of energy migration and trapping in photosystem I by a model with two distance scaling parameters
    • Valkunas L., Liuolia V., Dekker J.P., and van Grondelle R. Description of energy migration and trapping in photosystem I by a model with two distance scaling parameters. Photosynth. Res. 43 (1995) 149-154
    • (1995) Photosynth. Res. , vol.43 , pp. 149-154
    • Valkunas, L.1    Liuolia, V.2    Dekker, J.P.3    van Grondelle, R.4
  • 133
    • 0021759550 scopus 로고
    • Evidence for the existence of a thylakoid intrinsic protein that binds ferredoxin-NADP+ oxidoreductase
    • Vallejos R.H., Ceccarelli E., and Chan R. Evidence for the existence of a thylakoid intrinsic protein that binds ferredoxin-NADP+ oxidoreductase. J. Biol. Chem. 259 (1984) 8048-8051
    • (1984) J. Biol. Chem. , vol.259 , pp. 8048-8051
    • Vallejos, R.H.1    Ceccarelli, E.2    Chan, R.3
  • 134
    • 57649143641 scopus 로고    scopus 로고
    • Genetic analysis of the photosystem I subunits from the red alga, Galdieria sulphuraria
    • Vanselow C., Weber A., Krause K., and Fromme P. Genetic analysis of the photosystem I subunits from the red alga, Galdieria sulphuraria. Biochim. Biophys. Acta 1787 (2009) 46-59
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 46-59
    • Vanselow, C.1    Weber, A.2    Krause, K.3    Fromme, P.4
  • 135
    • 0035983637 scopus 로고    scopus 로고
    • Single and double knock-outs of the genes for photosystem I subunits G, K and H of Arabidopsis. Effects on photosystem I composition, photosynthetic electron flow and state transitions
    • Varotto C., Pesaresi P., Jahns P., Lessnick A., Tizzano M., Schiavon F., Salamini F., and Leister D. Single and double knock-outs of the genes for photosystem I subunits G, K and H of Arabidopsis. Effects on photosystem I composition, photosynthetic electron flow and state transitions. Plant Physiol. 129 (2002) 616-624
    • (2002) Plant Physiol. , vol.129 , pp. 616-624
    • Varotto, C.1    Pesaresi, P.2    Jahns, P.3    Lessnick, A.4    Tizzano, M.5    Schiavon, F.6    Salamini, F.7    Leister, D.8
  • 136
    • 65149088367 scopus 로고    scopus 로고
    • The role of LHCA complexes in the supramolecular organization of higher plant photosystem I
    • Wientjes E., Oostergetel G.T., Jansson S., Boekema E.J., and Croce R. The role of LHCA complexes in the supramolecular organization of higher plant photosystem I. J. Biol. Chem. 284 (2009) 7803-7810
    • (2009) J. Biol. Chem. , vol.284 , pp. 7803-7810
    • Wientjes, E.1    Oostergetel, G.T.2    Jansson, S.3    Boekema, E.J.4    Croce, R.5
  • 138
    • 1342287541 scopus 로고    scopus 로고
    • Phosphatized multicellular algae in the Neoproterozoic Doushantuo Formation, China, and the early evolution of florideophyte red algae
    • Xiao S., Knoll A.H., Yuan X., and Pueschel C. Phosphatized multicellular algae in the Neoproterozoic Doushantuo Formation, China, and the early evolution of florideophyte red algae. Am. J. Bot. 91 (2004) 214-227
    • (2004) Am. J. Bot. , vol.91 , pp. 214-227
    • Xiao, S.1    Knoll, A.H.2    Yuan, X.3    Pueschel, C.4
  • 143
    • 34248581202 scopus 로고    scopus 로고
    • Stress-inducible flavodoxin from photosynthetic microorganisms. The mystery of flavodoxin loss from the plant genome
    • Zurbriggen M.D., Tognetti V.B., and Carrillo N. Stress-inducible flavodoxin from photosynthetic microorganisms. The mystery of flavodoxin loss from the plant genome. IUBMB Life 59 (2007) 355-360
    • (2007) IUBMB Life , vol.59 , pp. 355-360
    • Zurbriggen, M.D.1    Tognetti, V.B.2    Carrillo, N.3
  • 145
    • 33744517666 scopus 로고    scopus 로고
    • The properties of the positively charged loop region in PSI-G are essential for its "spontaneous" insertion into thylakoids and rapid assembly into the photosystem I complex
    • Zygadlo A., Robinson C., Scheller H.V., Mant A., and Jensen P.E. The properties of the positively charged loop region in PSI-G are essential for its "spontaneous" insertion into thylakoids and rapid assembly into the photosystem I complex. J. Biol. Chem. 281 (2006) 10548-10554
    • (2006) J. Biol. Chem. , vol.281 , pp. 10548-10554
    • Zygadlo, A.1    Robinson, C.2    Scheller, H.V.3    Mant, A.4    Jensen, P.E.5


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