메뉴 건너뛰기




Volumn , Issue , 2008, Pages 65-81

A Glimpse into the Atomic Structure of Plant Photosystem I

Author keywords

Electron transfer; Light harvesting complex; Photosystem I; Plants; Reaction center

Indexed keywords


EID: 65149085740     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527623464.ch3     Document Type: Chapter
Times cited : (3)

References (78)
  • 2
    • 0001295974 scopus 로고
    • A developmental study of Photosystem I peripheral chlorophyll proteins
    • Mullet, J.E., Burke, J.J. and Arntzen, C.J. (1980) A developmental study of Photosystem I peripheral chlorophyll proteins. Plant Physiology, 65, 823-7.
    • (1980) Plant Physiology , vol.65 , pp. 823-827
    • Mullet, J.E.1    Burke, J.J.2    Arntzen, C.J.3
  • 4
    • 0348148910 scopus 로고    scopus 로고
    • Crystal structure of plant photosystem I
    • Ben-Shem, A., Frolow, F. and Nelson, N. (2003) Crystal structure of plant photosystem I. Nature, 426, 630-5.
    • (2003) Nature , vol.426 , pp. 630-635
    • Ben-Shem, A.1    Frolow, F.2    Nelson, N.3
  • 6
    • 33745936562 scopus 로고    scopus 로고
    • Structure and function of photosystems I and II
    • Nelson, N. and Yocum, C. (2006) Structure and function of photosystems I and II. Annual Review of Plant Biology, 57, 521-65.
    • (2006) Annual Review of Plant Biology , vol.57 , pp. 521-565
    • Nelson, N.1    Yocum, C.2
  • 7
    • 0016861451 scopus 로고
    • Purification and properties of the photosystem I reaction center from chloroplasts
    • Bengis, C. and Nelson, N. (1975) Purification and properties of the photosystem I reaction center from chloroplasts. Journal of Biological Chemistry, 250, 2783-8.
    • (1975) Journal of Biological Chemistry , vol.250 , pp. 2783-2788
    • Bengis, C.1    Nelson, N.2
  • 8
    • 0017397279 scopus 로고
    • Subunit structure of chloroplast photosystem I reaction center
    • Bengis, C. and Nelson, N. (1977) Subunit structure of chloroplast photosystem I reaction center. Journal of Biological Chemistry, 252, 4564-9.
    • (1977) Journal of Biological Chemistry , vol.252 , pp. 4564-4569
    • Bengis, C.1    Nelson, N.2
  • 9
    • 0036410161 scopus 로고    scopus 로고
    • Photosystem I reaction center: past and future
    • Nelson, N. and Ben-Shem, A. (2002) Photosystem I reaction center: past and future. Photosynthesis Research, 73, 193-206.
    • (2002) Photosynthesis Research , vol.73 , pp. 193-206
    • Nelson, N.1    Ben-Shem, A.2
  • 10
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 angstrom resolution
    • Jordan, P., Fromme, P., Witt, H.T., Klukas, O., Saenger, W. and Krauss, N. (2001) Three-dimensional structure of cyanobacterial photosystem I at 2.5 angstrom resolution. Nature, 411, 909-17.
    • (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
  • 12
    • 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. (2007) The structure of a plant photosystem I supercomplex at 3.4 Å resolution. Nature, 447, 58-63.
    • (2007) Nature , vol.447 , pp. 58-63
    • Amunts, A.1    Drory, O.2    Nelson, N.3
  • 14
    • 1942436332 scopus 로고    scopus 로고
    • Evolution of Photosystem I-from symmetry through pseudosymmetry to asymmetry
    • Ben-Shem, A., Frolow, F. and Nelson, N. (2004) Evolution of Photosystem I-from symmetry through pseudosymmetry to asymmetry. FEBS Letters, 564, 274-80.
    • (2004) FEBS Letters , vol.564 , pp. 274-280
    • Ben-Shem, A.1    Frolow, F.2    Nelson, N.3
  • 15
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach major light-harvesting complex at 2.72 A resolution
    • Liu, Z., Yan, H., Wang, K., Kuang, T., Zhang, J., Gui, L., An, X. and Chang, W. (2004) Crystal structure of spinach major light-harvesting complex at 2.72 A resolution. Nature, 428, 287-92.
    • (2004) Nature , vol.428 , pp. 287-292
    • Liu, Z.1    Yan, H.2    Wang, K.3    Kuang, T.4    Zhang, J.5    Gui, L.6    An, X.7    Chang, W.8
  • 16
    • 16344363252 scopus 로고    scopus 로고
    • Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 A resolution
    • Standfuss, J., Terwisscha van Scheltinga, A.C., Lamborghini, M. and Kuhlbrandt, W. (2005) Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 A resolution. EMBO Journal, 24, 919-28.
    • (2005) EMBO Journal , vol.24 , pp. 919-928
    • Standfuss, J.1    Terwisscha Van Scheltinga, A.C.2    Lamborghini, M.3    Kuhlbrandt, W.4
  • 18
    • 0030250383 scopus 로고    scopus 로고
    • Nearest-neighbor analysis of higher-plant photosystem I holocomplex
    • Jansson, S., Andersen, B. and Scheller, H.V. (1996) Nearest-neighbor analysis of higher-plant photosystem I holocomplex. Plant Physiology, 112, 409-20.
    • (1996) Plant Physiology , vol.112 , pp. 409-420
    • Jansson, S.1    Andersen, B.2    Scheller, H.V.3
  • 20
    • 0034735803 scopus 로고    scopus 로고
    • The PSI-H subunit of photosystem I is essential for state transitions in plant photosynthesis
    • Lunde, P., Jensen, P.E., Haldrup, A., Knoetzel, J. and Scheller, H.V. (2000) The PSI-H subunit of photosystem I is essential for state transitions in plant photosynthesis. Nature, 408, 613-15.
    • (2000) Nature , vol.408 , pp. 613-615
    • Lunde, P.1    Jensen, P.E.2    Haldrup, A.3    Knoetzel, J.4    Scheller, H.V.5
  • 21
    • 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. (2006) 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. Journal of Biological Chemistry, 281, 10548-54.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 10548-10554
    • Zygadlo, A.1    Robinson, C.2    Scheller, H.V.3    Mant, A.4    Jensen, P.E.5
  • 23
    • 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. (1998) 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. Proceedings of the National Academy of Sciences of the United States of America, 95, 7339-44.
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , pp. 7339-7344
    • Hippler, M.1    Drepper, F.2    Haehnel, W.3    Rochaix, J.D.4
  • 24
    • 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 Muhlenhoff, U. (1999) 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. Journal of Biological Chemistry, 274, 4180-8.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 4180-4188
    • Hippler, M.1    Drepper, F.2    Rochaix, J.D.3    Muhlenhoff, U.4
  • 25
    • 0025724097 scopus 로고
    • Molecular cloning and targeted mutagenesis of the gene psaF encoding subunit III of photosystem I from the cyanobacterium Synechocystis sp. PCC 6803
    • Chitnis, P.R., Purvis, D. and Nelson, N. (1991) Molecular cloning and targeted mutagenesis of the gene psaF encoding subunit III of photosystem I from the cyanobacterium Synechocystis sp. PCC 6803. Journal of Biological Chemistry, 266, 20146-51.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 20146-20151
    • Chitnis, P.R.1    Purvis, D.2    Nelson, N.3
  • 26
    • 0032504023 scopus 로고    scopus 로고
    • A common ancestor for oxygenic and anoxygenic photosynthetic systems: a comparison based on the structural model of photosystem I
    • Schubert, W.D., Klukas, O., Saenger, W., Witt, H.T., Fromme, P. and Krauss, N.A. (1998) A common ancestor for oxygenic and anoxygenic photosynthetic systems: a comparison based on the structural model of photosystem I. Journal of Molecular Biology, 280, 297-314.
    • (1998) Journal of Molecular Biology , vol.280 , pp. 297-314
    • Schubert, W.D.1    Klukas, O.2    Saenger, W.3    Witt, H.T.4    Fromme, P.5    Krauss, N.A.6
  • 28
    • 26244457474 scopus 로고    scopus 로고
    • The structure of photosystem I and evolution of photosynthesis
    • Nelson, N. and Ben-Shem, A. (2005) The structure of photosystem I and evolution of photosynthesis. Bioessays, 27, 914-22.
    • (2005) Bioessays , vol.27 , pp. 914-922
    • Nelson, N.1    Ben-Shem, A.2
  • 29
    • 10044249999 scopus 로고    scopus 로고
    • Unique constitution of photosystem I with a novel subunit in the cyanobacterium Gloeobacter violaceus PCC 7421
    • Inoue, H., Tsuchiya, T., Satoh, S., Miyashita, H., Kaneko, T., Tabata, S., Tanaka, A. and Mimuro, M. (2004) Unique constitution of photosystem I with a novel subunit in the cyanobacterium Gloeobacter violaceus PCC 7421. FEBS Letters, 578, 275-9.
    • (2004) FEBS Letters , vol.578 , pp. 275-279
    • Inoue, H.1    Tsuchiya, T.2    Satoh, S.3    Miyashita, H.4    Kaneko, T.5    Tabata, S.6    Tanaka, A.7    Mimuro, M.8
  • 30
    • 0004279464 scopus 로고    scopus 로고
    • Molecular Mechanisms of Photosynthesis
    • Blackwell Science, Oxford, UK
    • Blankenship, R.E. (2002) Molecular Mechanisms of Photosynthesis, Blackwell Science, Oxford, UK.
    • (2002)
    • Blankenship, R.E.1
  • 31
    • 0034802694 scopus 로고    scopus 로고
    • Acclimation of Arabidopsis thaliana to the light environment: the existence of separate low light and high light responses
    • Bailey, S., Walters, R.G., Jansson, S. and Horton, P. (2001) Acclimation of Arabidopsis thaliana to the light environment: the existence of separate low light and high light responses. Planta, 213, 794-801.
    • (2001) Planta , vol.213 , pp. 794-801
    • Bailey, S.1    Walters, R.G.2    Jansson, S.3    Horton, P.4
  • 32
    • 0037183991 scopus 로고    scopus 로고
    • Mutation analysis of Lhca1 antenna complex. Low energy absorption forms originate from pigment-pigment interactions
    • Morosinotto, T., Castelletti, S., Breton, J., Bassi, R. and Croce, R. (2002) Mutation analysis of Lhca1 antenna complex. Low energy absorption forms originate from pigment-pigment interactions. Journal of Biological Chemistry, 277, 36253-61.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 36253-36261
    • Morosinotto, T.1    Castelletti, S.2    Breton, J.3    Bassi, R.4    Croce, R.5
  • 33
    • 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. (2005) Structure of the higher plant light harvesting complex I: in vivo characterization and structural interdependence of the Lhca proteins. Biochemistry, 44, 3065-73.
    • (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
  • 35
    • 0000784913 scopus 로고    scopus 로고
    • The Light Reactions in Oxygenic Photosynthesis, Kluwer Academic Publishers
    • Dordrecht, The Netherlands
    • Pichersky, E. and Jansson, S. (1996) The Light Reactions in Oxygenic Photosynthesis, Kluwer Academic Publishers, Dordrecht, The Netherlands, pp. 507-21.
    • (1996) , pp. 507-521
    • Pichersky, E.1    Jansson, S.2
  • 36
    • 30744470900 scopus 로고    scopus 로고
    • Light harvesting in photosystem I supercomplexes
    • Melkozernov, A.N., Barber, J. and Blankenship, R.E. (2006) Light harvesting in photosystem I supercomplexes. Biochemistry, 45, 331-45.
    • (2006) Biochemistry , vol.45 , pp. 331-345
    • Melkozernov, A.N.1    Barber, J.2    Blankenship, R.E.3
  • 38
    • 0036667743 scopus 로고    scopus 로고
    • Photosystem II: a multisubunit membrane protein that oxidises water
    • Barber, J. (2002) Photosystem II: a multisubunit membrane protein that oxidises water. Current Opinion in Structural Biology, 12, 523-30.
    • (2002) Current Opinion in Structural Biology , vol.12 , pp. 523-530
    • Barber, J.1
  • 39
    • 0032951790 scopus 로고    scopus 로고
    • A phylogenetic assessment of the eukaryotic light-harvesting antenna proteins, with implications for plastid evolution
    • Durnford, G., Deane, J.A., Tan, S., McFadden, G.I., Gantt, E. and Green, B.R. (1999) A phylogenetic assessment of the eukaryotic light-harvesting antenna proteins, with implications for plastid evolution. Journal of Molecular Evolution, 48, 59-68.
    • (1999) Journal of Molecular Evolution , vol.48 , pp. 59-68
    • Durnford, G.1    Deane, J.A.2    Tan, S.3    McFadden, G.I.4    Gantt, E.5    Green, B.R.6
  • 40
    • 4043077853 scopus 로고    scopus 로고
    • Light-harvesting features revealed by the structure of plant photosystem I
    • Ben-Shem, A., Frolow, F. and Nelson, N. (2004) Light-harvesting features revealed by the structure of plant photosystem I. Photosynthesis Research, 81, 239-50.
    • (2004) Photosynthesis Research , vol.81 , pp. 239-250
    • Ben-Shem, A.1    Frolow, F.2    Nelson, N.3
  • 41
    • 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. (2002) Identification of N-and C -terminal amino acids of Lhca1 and Lhca4 required for formation of the heterodimeric peripheral photosystem I antenna LHCI-730. B iochemistry, 41, 9126-31.
    • (2002) B iochemistry , vol.41 , pp. 9126-9131
    • Schmid, V.H.1    Paulsen, H.2    Rupprecht, J.3
  • 42
    • 4544357205 scopus 로고    scopus 로고
    • Lhca5-an LHC-type protein associated with photosystem I
    • Ganeteg, U., Klimmek, F. and Jansson, S. (2004) Lhca5-an LHC-type protein associated with photosystem I. Plant Molecular Biology, 54, 641-51.
    • (2004) Plant Molecular Biology , vol.54 , pp. 641-651
    • Ganeteg, U.1    Klimmek, F.2    Jansson, S.3
  • 43
    • 14044252837 scopus 로고    scopus 로고
    • Pigment binding, fluorescence properties, and oligomerization behavior of Lhca5, a novel light-harvesting protein
    • Storf, S., Jansson, S. and Schmid, V.H. (2005) Pigment binding, fluorescence properties, and oligomerization behavior of Lhca5, a novel light-harvesting protein. Journal of Biological Chemistry, 280, 5163-8.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 5163-5168
    • Storf, S.1    Jansson, S.2    Schmid, V.H.3
  • 45
    • 0014669751 scopus 로고
    • Interaction between ferredoxin and ferredoxin nicotinamide adenine dinucleotide phosphate reductase in pyridine nucleotide photoreduction and some partial reactions. I. Inhibition of ferredoxin nicotinamide adenine dinucleotide phosphate reductase by ferredoxin
    • Nelson, N. and Neumann, J. (1969) Interaction between ferredoxin and ferredoxin nicotinamide adenine dinucleotide phosphate reductase in pyridine nucleotide photoreduction and some partial reactions. I. Inhibition of ferredoxin nicotinamide adenine dinucleotide phosphate reductase by ferredoxin. Journal of Biological Chemistry, 244, l926-31.
    • (1969) Journal of Biological Chemistry , vol.244
    • Nelson, N.1    Neumann, J.2
  • 46
    • 0014669752 scopus 로고
    • Interaction between ferredoxin and ferredoxin nicotinamide adenine dinucleotide phosphate reductase in pyridine nucleotide photoreduction and some partial reactions. II. Complex formation between ferredoxin and ferredoxin nicotinamide adenine dinucleotide phosphate reductase and its relevance to pyridine nucleotide photoreduction
    • Nelson, N. and Neumann, J. (1969) Interaction between ferredoxin and ferredoxin nicotinamide adenine dinucleotide phosphate reductase in pyridine nucleotide photoreduction and some partial reactions. II. Complex formation between ferredoxin and ferredoxin nicotinamide adenine dinucleotide phosphate reductase and its relevance to pyridine nucleotide photoreduction. Journal of Biological Chemistry, 244, 1932-6.
    • (1969) Journal of Biological Chemistry , vol.244 , pp. 1932-1936
    • Nelson, N.1    Neumann, J.2
  • 48
    • 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. (1984) Evidence for the existence of a thylakoid intrinsic protein that binds ferredoxin-NADP+ oxidoreductase. Journal of Biological Chemistry, 259, 8048-51.
    • (1984) Journal of Biological Chemistry , vol.259 , pp. 8048-8051
    • Vallejos, R.H.1    Ceccarelli, E.2    Chan, R.3
  • 49
    • 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. (1986) Removal of ferredoxin:NADP+ oxidoreductase from thylakoid membranes, rebinding to depleted membranes, and identification of the binding site. Journal of Biological Chemistry, 261, 12154-8.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 12154-12158
    • Matthijs, H.C.1    Coughlan, S.J.2    Hind, G.3
  • 50
    • 0000510117 scopus 로고
    • Association of ferredoxin-NADP + oxidoreductase with the chloroplast cytochrome b-f complex
    • Clark, R.D., Hawkesford, M.J., Coughlan, S.J., Bennett, J. and Hind, G. (1984) Association of ferredoxin-NADP + oxidoreductase with the chloroplast cytochrome b-f complex. FEBS Letters, 174, 137-42.
    • (1984) FEBS Letters , vol.174 , pp. 137-142
    • Clark, R.D.1    Hawkesford, M.J.2    Coughlan, S.J.3    Bennett, J.4    Hind, G.5
  • 51
    • 0035851111 scopus 로고    scopus 로고
    • Ferredoxin:NADP+ oxidoreductase is a subunit of the chloroplast cytochrome b6f complex
    • Zhang, H. and Whitelegge, J.P. and Cramer, W.A. (2001) Ferredoxin:NADP+ oxidoreductase is a subunit of the chloroplast cytochrome b6f complex. Journal of Biological Chemistry, 276, 38159-65.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 38159-38165
    • Zhang, H.1    Whitelegge, J.P.2    Cramer, W.A.3
  • 52
    • 33644836833 scopus 로고    scopus 로고
    • Three maize leaf ferredoxin:NADPH oxidoreductases vary in subchloroplast location, expression, and interaction with ferredoxin
    • Okutani, S., Hanke, G.T., Satomi, Y., Takao, T., Kurisu, G., Suzuki, A. and Hase, T. (2005) Three maize leaf ferredoxin:NADPH oxidoreductases vary in subchloroplast location, expression, and interaction with ferredoxin. Plant Physiology, 139, 1451-9.
    • (2005) Plant Physiology , vol.139 , pp. 1451-1459
    • Okutani, S.1    Hanke, G.T.2    Satomi, Y.3    Takao, T.4    Kurisu, G.5    Suzuki, A.6    Hase, T.7
  • 53
    • 0034043661 scopus 로고    scopus 로고
    • Separation by blue-native PAGE and identification of the whole NAD(P)H dehydrogenase complex from barley stroma thylakoids
    • Quiles, M.J., Garcia, A. and Cuello, J. (2000) Separation by blue-native PAGE and identification of the whole NAD(P)H dehydrogenase complex from barley stroma thylakoids. Plant Physiology and Biochemistry, 38, 225-32.
    • (2000) Plant Physiology and Biochemistry , vol.38 , pp. 225-232
    • Quiles, M.J.1    Garcia, A.2    Cuello, J.3
  • 54
    • 0026722604 scopus 로고
    • The PSI-E subunit of photosystem I binds ferredoxin:NADP+ oxidoreductase
    • Andersen, B., Scheller H.V. and Moller, B.L. (1992) The PSI-E subunit of photosystem I binds ferredoxin:NADP+ oxidoreductase. FEBS Letters, 311, 169-73.
    • (1992) FEBS Letters , vol.311 , pp. 169-173
    • Andersen, B.1    Scheller, H.V.2    Moller, B.L.3
  • 58
    • 0345358540 scopus 로고    scopus 로고
    • Tracking the function of the cytochrome c6-like protein in higher plants
    • Weigel, M., Pesaresi, P. and Leister, D. (2003) Tracking the function of the cytochrome c6-like protein in higher plants. Trends in Plant Science, 8, 513-17.
    • (2003) Trends in Plant Science , vol.8 , pp. 513-517
    • Weigel, M.1    Pesaresi, P.2    Leister, D.3
  • 60
    • 18744388311 scopus 로고    scopus 로고
    • Release of oxidized plastocyanin from photosystem I limits electron transfer between photosystem I and cytochrome b6f complex in vivo
    • Finazzi, G., Sommer, F. and Hippler, M. (2005) Release of oxidized plastocyanin from photosystem I limits electron transfer between photosystem I and cytochrome b6f complex in vivo. Proceedings of the National Academy of Sciences, 102, 7031-6.
    • (2005) Proceedings of the National Academy of Sciences , vol.102 , pp. 7031-7036
    • Finazzi, G.1    Sommer, F.2    Hippler, M.3
  • 61
    • 11144292072 scopus 로고    scopus 로고
    • Equilibration between cytochrome f and P700 in intact leaves
    • Golding, A.J., Joliot, P. and Johnsin, G.N. (2005) Equilibration between cytochrome f and P700 in intact leaves. Biochimica et Biophysica Acta, 1706, 105-9.
    • (2005) Biochimica et Biophysica Acta , vol.1706 , pp. 105-109
    • Golding, A.J.1    Joliot, P.2    Johnsin, G.N.3
  • 62
    • 0031574117 scopus 로고    scopus 로고
    • The involvement of the two acidic patches of spinach plastocyanin in the reaction with photosystem I
    • Young, S., Sigfridsson, K., Olesen, K. and Hansson, O. (1997) The involvement of the two acidic patches of spinach plastocyanin in the reaction with photosystem I. Biochimica et Biophysica Acta, 1322, 106-14.
    • (1997) Biochimica et Biophysica Acta , vol.1322 , pp. 106-114
    • Young, S.1    Sigfridsson, K.2    Olesen, K.3    Hansson, O.4
  • 63
    • 0039550890 scopus 로고    scopus 로고
    • Electron transfer to photosystem 1 from spinach plastocyanin mutated in the small acidic patch: ionic strength dependence of kinetics and comparison of mechanistic models
    • Olesen, K., Ejdeback, M., Crnogorac, M.M., Kostic, N.M. and Hansson, O. (1999) Electron transfer to photosystem 1 from spinach plastocyanin mutated in the small acidic patch: ionic strength dependence of kinetics and comparison of mechanistic models. Biochemistry, 38, 16695-705.
    • (1999) Biochemistry , vol.38 , pp. 16695-16705
    • Olesen, K.1    Ejdeback, M.2    Crnogorac, M.M.3    Kostic, N.M.4    Hansson, O.5
  • 64
    • 0037155169 scopus 로고    scopus 로고
    • The luminal helix l of PsaB is essential for recognition of plastocyanin or cytochrome c6 and fast electron transfer to photosystem I in Chlamydomonas reinhardtii
    • Sommer, F., Drepper, F. and Hippler, M. (2002) The luminal helix l of PsaB is essential for recognition of plastocyanin or cytochrome c6 and fast electron transfer to photosystem I in Chlamydomonas reinhardtii. Journal of Biological Chemistry, 277, 6573-81.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 6573-6581
    • Sommer, F.1    Drepper, F.2    Hippler, M.3
  • 65
    • 10644251528 scopus 로고    scopus 로고
    • Evolutionary timing of the origins of mesophilic sulphate reduction and oxygenic photosynthesis: a phylogenomic dating approach
    • Blank, C.E. (2004) Evolutionary timing of the origins of mesophilic sulphate reduction and oxygenic photosynthesis: a phylogenomic dating approach. Geobiology, 2, 1-20.
    • (2004) Geobiology , vol.2 , pp. 1-20
    • Blank, C.E.1
  • 66
    • 3042721884 scopus 로고    scopus 로고
    • Engine of life and big bang of evolution: a personal perspective
    • Barber, J. (2004) Engine of life and big bang of evolution: a personal perspective. Photosynthesis Research, 80, 137-55.
    • (2004) Photosynthesis Research , vol.80 , pp. 137-155
    • Barber, J.1
  • 67
    • 0038152799 scopus 로고    scopus 로고
    • Euglena gracilis rhodoquinone:ubiquinone ratio and mitochondrial proteome differ under aerobic and anaerobic conditions
    • Martin, W., Rotte, C., Hoffmeister, M., Theissen, U., Gelius-Dietrich, G., Ahr, S. and Henze, K. (2003) Euglena gracilis rhodoquinone:ubiquinone ratio and mitochondrial proteome differ under aerobic and anaerobic conditions. IUBMB Life, 55, 193-204.
    • (2003) IUBMB Life , vol.55 , pp. 193-204
    • Martin, W.1    Rotte, C.2    Hoffmeister, M.3    Theissen, U.4    Gelius-Dietrich, G.5    Ahr, S.6    Henze, K.7
  • 68
    • 33646360208 scopus 로고    scopus 로고
    • Selective forces for the origin of the eukaryotic nucleus
    • Lopez-Garcia, P. and Moreira, D. (2006) Selective forces for the origin of the eukaryotic nucleus. Bioessays, 28, 525-33.
    • (2006) Bioessays , vol.28 , pp. 525-533
    • Lopez-Garcia, P.1    Moreira, D.2
  • 69
    • 12544255323 scopus 로고    scopus 로고
    • The real " kingdoms " of eukaryotes
    • Simpson, A.G. and Roger, A.J. (2004) The real " kingdoms " of eukaryotes. Current Biology, 14, 693-6.
    • (2004) Current Biology , vol.14 , pp. 693-696
    • Simpson, A.G.1    Roger, A.J.2
  • 71
    • 0027359059 scopus 로고
    • Why do thylakoid membranes from higher plants form grana stacks?
    • Trissl, H.W. and Wilhelm, C. (1993) Why do thylakoid membranes from higher plants form grana stacks? Trends in Biochemical Sciences, 18, 415-19.
    • (1993) Trends in Biochemical Sciences , vol.18 , pp. 415-419
    • Trissl, H.W.1    Wilhelm, C.2
  • 72
    • 36849155728 scopus 로고
    • Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems
    • Allen, J.F., Bennett, J., Steinback, K.E. and Arntzen, C.G. (1981) Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems. Nature, 291, 25-9.
    • (1981) Nature , vol.291 , pp. 25-29
    • Allen, J.F.1    Bennett, J.2    Steinback, K.E.3    Arntzen, C.G.4
  • 73
    • 0021103921 scopus 로고
    • Lateral mobility of the light -harvesting complex in chloroplast membranes controls excitation energy distribution in higher plants
    • Kyle, J., Staehelin, L.A. and Arntzen, C.J. (1983) Lateral mobility of the light -harvesting complex in chloroplast membranes controls excitation energy distribution in higher plants. Archives of Biochemistry and Biophysics, 222, 527-41.
    • (1983) Archives of Biochemistry and Biophysics , vol.222 , pp. 527-541
    • Kyle, J.1    Staehelin, L.A.2    Arntzen, C.J.3
  • 74
    • 0037268248 scopus 로고    scopus 로고
    • Cyclic, pseudocyclic and noncyclic photophosphorylation: new links in the chain
    • Allen, J.F. (2003) Cyclic, pseudocyclic and noncyclic photophosphorylation: new links in the chain. Trends in Plant Science, 8, 15-19.
    • (2003) Trends in Plant Science , vol.8 , pp. 15-19
    • Allen, J.F.1
  • 75
    • 0942276401 scopus 로고    scopus 로고
    • Light-harvesting complex II binds to several small subunits of photosystem I
    • Zhang, S. and Scheller, H.V. (2004) Light-harvesting complex II binds to several small subunits of photosystem I. Journal of Biological Chemistry, 279, 3180-7.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 3180-3187
    • Zhang, S.1    Scheller, H.V.2
  • 76
    • 40849083514 scopus 로고    scopus 로고
    • Functional organization of a plant photosystem I-evolution of a highly efficient photochemical machine
    • (in press)
    • Amunts, A. and Nelson, N. (2008) Functional organization of a plant photosystem I-evolution of a highly efficient photochemical machine. Plant Physiology and Biochemistry, 46, 228-37 (in press).
    • (2008) Plant Physiology and Biochemistry , vol.46 , pp. 228-37
    • Amunts, A.1    Nelson, N.2
  • 77
    • 23944511122 scopus 로고    scopus 로고
    • Structural characterization of a complex of photosystem I and light-harvesting complex II of Arabidopsis thaliana
    • Kouril, R., Zygadlo, A., Arteni, A.A., de Wit, C.D., Dekker, J.P., Jensen, P.E., Scheller, H.V. and Boekema, E.J. (2005) Structural characterization of a complex of photosystem I and light-harvesting complex II of Arabidopsis thaliana. Biochemistry, 44, 10935-40.
    • (2005) Biochemistry , vol.44 , pp. 10935-10940
    • Kouril, R.1    Zygadlo, A.2    Arteni, A.A.3    De Wit, C.D.4    Dekker, J.P.5    Jensen, P.E.6    Scheller, H.V.7    Boekema, E.J.8
  • 78
    • 29344451695 scopus 로고    scopus 로고
    • Characterization of a novel Photosystem I-LHCI supercomplex isolated from Chlamydomonas reinhardtii under anaerobic (State II) conditions
    • Subramanyam, R., Jolley, C., Brune, D.C., Fromme, P. and Webber, A.N. (2006) Characterization of a novel Photosystem I-LHCI supercomplex isolated from Chlamydomonas reinhardtii under anaerobic (State II) conditions. FEBS Letters, 580, 233-8.
    • (2006) FEBS Letters , vol.580 , pp. 233-238
    • Subramanyam, R.1    Jolley, C.2    Brune, D.C.3    Fromme, P.4    Webber, A.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.