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Volumn 1706, Issue 1-2, 2005, Pages 12-39

Supramolecular organization of thylakoid membrane proteins in green plants

Author keywords

Cyclic electron transport; Cytochrome b 6 f complex; Grana; Light harvesting complex; Nonphotochemical quenching; Photosynthesis; Photosystem I; Photosystem II; State transition; Supercomplex; Thylakoid membrane

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CYTOCHROME B; DIMER; MEMBRANE PROTEIN; MONOMER; VEGETABLE PROTEIN;

EID: 11044234285     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.09.009     Document Type: Review
Times cited : (729)

References (235)
  • 1
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 angstrom resolution
    • P. Jordan, P. Fromme, H.T. Witt, O. Kuklas, W. Saenger, and N. Krauss Three-dimensional structure of cyanobacterial photosystem I at 2.5 angstrom resolution Nature 411 2001 909 917
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Kuklas, O.4    Saenger, W.5    Krauss, N.6
  • 2
    • 0348148910 scopus 로고    scopus 로고
    • Crystal structure of plant photosystem I
    • A. Ben-Shem, F. Frolow, and N. Nelson 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
  • 3
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 angstrom resolution
    • A. Zouni, H.T. Witt, J. Kern, P. Fromme, N. Krauss, W. Saenger, and P. Orth Crystal structure of photosystem II from Synechococcus elongatus at 3.8 angstrom resolution Nature 409 2001 739 743
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1    Witt, H.T.2    Kern, J.3    Fromme, P.4    Krauss, N.5    Saenger, W.6    Orth, P.7
  • 4
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-angstrom resolution
    • N. Kamiya, and J.R. Shen Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-angstrom resolution Proc. Natl. Acad. Sci. U. S. A. 100 2003 98 103
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 98-103
    • Kamiya, N.1    Shen, J.R.2
  • 6
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • W. Kühlbrandt, D.N. Wang, and Y. Fujiyoshi Atomic model of plant light-harvesting complex by electron crystallography Nature 367 1994 614 621
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 7
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach light-harvesting complex at 2.72 Å resolution
    • Z. Liu, H. Yan, K. Wang, T. Kuang, J. Zhang, L. Gui, X. An, and W. Chang Crystal structure of spinach light-harvesting complex at 2.72 Å resolution Nature 428 2004 287 292
    • (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
  • 8
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • J.P. Abrahams, A.G. Leslie, R. Lutter, and J.E. Walker Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria Nature 370 1994 621 628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 9
    • 0035846822 scopus 로고    scopus 로고
    • The structure of the chloroplast F1-ATPase at 3.2 Å resolution
    • G. Groth, and E. Pohl The structure of the chloroplast F1-ATPase at 3.2 Å resolution J. Biol. Chem. 276 2001 1345 1352
    • (2001) J. Biol. Chem. , vol.276 , pp. 1345-1352
    • Groth, G.1    Pohl, E.2
  • 10
    • 0242494128 scopus 로고    scopus 로고
    • Structure of the cytochrome b(6)f complex of oxygenic photosynthesis: Tuning the cavity
    • G. Kurisu, H. Zhang, J.L. Smith, and W.A. Cramer Structure of the cytochrome b(6)f complex of oxygenic photosynthesis: tuning the cavity Science 302 2003 1009 1014
    • (2003) Science , vol.302 , pp. 1009-1014
    • Kurisu, G.1    Zhang, H.2    Smith, J.L.3    Cramer, W.A.4
  • 12
    • 0037056045 scopus 로고    scopus 로고
    • Respiratory chain supercomplexes of mitochondria and bacteria
    • H. Schägger Respiratory chain supercomplexes of mitochondria and bacteria Biochim. Biophys. Acta 1555 2002 154 159
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 154-159
    • Schägger, H.1
  • 15
    • 0036535897 scopus 로고    scopus 로고
    • The assembly of protein subunits and cofactors in photosystem I
    • W. Saenger, P. Jordan, and N. Krauss The assembly of protein subunits and cofactors in photosystem I Curr. Opin. Struct. Biol. 12 2002 244 254
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 244-254
    • Saenger, W.1    Jordan, P.2    Krauss, N.3
  • 16
    • 0036469776 scopus 로고    scopus 로고
    • Reaction centres: The structure and evolution of biological solar power
    • P. Heathcote, P.K. Fyfe, and M.R. Jones Reaction centres: the structure and evolution of biological solar power Trends Biochem. Sci. 27 2002 79 87
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 79-87
    • Heathcote, P.1    Fyfe, P.K.2    Jones, M.R.3
  • 17
    • 18644372534 scopus 로고    scopus 로고
    • Functional implications on the mechanism of the function of photosystem II including water oxidation based on the structure of photosystem II
    • P. Fromme, J. Kern, B. Loll, J. Biesiadka, W. Saenger, H.T. Witt, N. Krauss, and A. Zouni Functional implications on the mechanism of the function of photosystem II including water oxidation based on the structure of photosystem II Philos. Trans. R. Soc. Lond., B 357 2002 1337 1345
    • (2002) Philos. Trans. R. Soc. Lond., B , vol.357 , pp. 1337-1345
    • Fromme, P.1    Kern, J.2    Loll, B.3    Biesiadka, J.4    Saenger, W.5    Witt, H.T.6    Krauss, N.7    Zouni, A.8
  • 20
    • 0242277341 scopus 로고    scopus 로고
    • Molecular dissection of photosystem I in higher plants: Topology, structure and function
    • P.E. Jensen, A. Haldrup, L. Rosgaard, and H.V. Scheller Molecular dissection of photosystem I in higher plants: topology, structure and function Physiol. Plant. 119 2003 313 321
    • (2003) Physiol. Plant. , vol.119 , pp. 313-321
    • Jensen, P.E.1    Haldrup, A.2    Rosgaard, L.3    Scheller, H.V.4
  • 21
    • 0035976020 scopus 로고    scopus 로고
    • Energy transfer and trapping in photosystem I
    • B. Gobets, and R. van Grondelle 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
  • 22
    • 0023195968 scopus 로고
    • Evidence for a trimeric organization of the photosystem I complex from the thermophilic cyanobacterium Synechococcus sp
    • E.J. Boekema, J.P. Dekker, M. van Heel, M. Rögner, W. Saenger, I. Witt, and H.T. Witt Evidence for a trimeric organization of the photosystem I complex from the thermophilic cyanobacterium Synechococcus sp FEBS Lett. 217 1987 283 286
    • (1987) FEBS Lett. , vol.217 , pp. 283-286
    • Boekema, E.J.1    Dekker, J.P.2    Van Heel, M.3    Rögner, M.4    Saenger, W.5    Witt, I.6    Witt, H.T.7
  • 24
    • 0027522441 scopus 로고
    • Characterization of trimeric Photosystem I particles from the prochlorophyte Prochlorothrix hollandica by electron microscopy and image analysis
    • G.W.M. van der Staay, E.J. Boekema, J.P. Dekker, and H.C.P. Matthijs Characterization of trimeric Photosystem I particles from the prochlorophyte Prochlorothrix hollandica by electron microscopy and image analysis Biochim. Biophys. Acta 1142 1993 189 193
    • (1993) Biochim. Biophys. Acta , vol.1142 , pp. 189-193
    • Van Der Staay, G.W.M.1    Boekema, E.J.2    Dekker, J.P.3    Matthijs, H.C.P.4
  • 25
    • 0035846108 scopus 로고    scopus 로고
    • Oxyphotobacteria-antenna ring around photosystem I
    • T.S. Bibby, J. Nield, F. Partensky, and J. Barber Oxyphotobacteria- antenna ring around photosystem I Nature 413 2001 590
    • (2001) Nature , vol.413 , pp. 590
    • Bibby, T.S.1    Nield, J.2    Partensky, F.3    Barber, J.4
  • 26
    • 0041363271 scopus 로고    scopus 로고
    • Low-light-adapted Prochlorococcus species possess specific antennae for each photosystem. J. Barber
    • T.S. Bibby, I. Mary, J. Nield, and F. Partensky Low-light-adapted Prochlorococcus species possess specific antennae for each photosystem. J. Barber Nature 424 2003 1051 1054
    • (2003) Nature , vol.424 , pp. 1051-1054
    • Bibby, T.S.1    Mary, I.2    Nield, J.3    Partensky, F.4
  • 28
    • 0027142977 scopus 로고
    • PsaL subunit is required for the formation of photosystem I trimers in the cyanobacterium Synechocystis sp. PCC 6803
    • V.P. Chitnis, and P.R. Chitnis PsaL subunit is required for the formation of photosystem I trimers in the cyanobacterium Synechocystis sp. PCC 6803 FEBS Lett. 336 1993 330 334
    • (1993) FEBS Lett. , vol.336 , pp. 330-334
    • Chitnis, V.P.1    Chitnis, P.R.2
  • 29
    • 1942436332 scopus 로고    scopus 로고
    • Evolution of photosystem I-from symmetry through pseudosymmetry to asymmetry
    • A. Ben-Shem, F. Frolow, and N. Nelson Evolution of photosystem I-from symmetry through pseudosymmetry 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
  • 30
    • 0037174173 scopus 로고    scopus 로고
    • Chlorophyll b inhibits the formation of photosystem I trimer in Synechocystis sp. PCC 6803
    • S. Satoh, and A. Tanaka Chlorophyll b inhibits the formation of photosystem I trimer in Synechocystis sp. PCC 6803 FEBS Lett. 528 2002 235 240
    • (2002) FEBS Lett. , vol.528 , pp. 235-240
    • Satoh, S.1    Tanaka, A.2
  • 31
    • 0036788599 scopus 로고    scopus 로고
    • Pigment organization and energy transfer dynamics in isolated, photosystem I (PSI) complexes from Arabidopsis thaliana depleted of the PSI-G, PSI-K, PSI-L, or PSI-N subunit
    • J.A. Ihalainen, P.E. Jensen, A. Haldrup, I.H.M. van Stokkum, R. van Grondelle, H.V. Scheller, and J.P. Dekker Pigment organization and energy transfer dynamics in isolated, photosystem I (PSI) complexes from Arabidopsis thaliana depleted of the PSI-G, PSI-K, PSI-L, or PSI-N subunit Biophys. J. 83 2002 2190 2201
    • (2002) Biophys. J. , vol.83 , pp. 2190-2201
    • Ihalainen, J.A.1    Jensen, P.E.2    Haldrup, A.3    Van Stokkum, I.H.M.4    Van Grondelle, R.5    Scheller, H.V.6    Dekker, J.P.7
  • 32
    • 0034637484 scopus 로고    scopus 로고
    • The PSI-K subunit of photosystem I is involved in the interaction between light-harvesting complex I and the photosystem I reaction center core
    • P.E. Jensen, M. Gilpin, J. Knoetzel, and H.V. Scheller The PSI-K subunit of photosystem I is involved in the interaction between light-harvesting complex I and the photosystem I reaction center core J. Biol. Chem. 275 2000 24701 24708
    • (2000) J. Biol. Chem. , vol.275 , pp. 24701-24708
    • Jensen, P.E.1    Gilpin, M.2    Knoetzel, J.3    Scheller, H.V.4
  • 33
    • 0030250383 scopus 로고    scopus 로고
    • Nearest-neighbor analysis of higher-plant photosystem I holocomplex
    • S. Jansson, B. Andersen, and H.V. Scheller Nearest-neighbor analysis of higher-plant photosystem I holocomplex Plant Physiol. 112 1996 409 420
    • (1996) Plant Physiol. , vol.112 , pp. 409-420
    • Jansson, S.1    Andersen, B.2    Scheller, H.V.3
  • 34
    • 0037169520 scopus 로고    scopus 로고
    • Photosystem I activity is increased in the absence of the PSI-G subunit
    • P.E. Jensen, L. Rosgaard, J. Knoetzel, and H.V. Scheller Photosystem I activity is increased in the absence of the PSI-G subunit J. Biol. Chem. 277 2002 2798 2803
    • (2002) J. Biol. Chem. , vol.277 , pp. 2798-2803
    • Jensen, P.E.1    Rosgaard, L.2    Knoetzel, J.3    Scheller, H.V.4
  • 35
    • 0028058268 scopus 로고
    • The light-harvesting chlorophyll a/b binding proteins
    • S. Jansson The light-harvesting chlorophyll a/b binding proteins Biochim. Biophys. Acta 1184 1994 1 19
    • (1994) Biochim. Biophys. Acta , vol.1184 , pp. 1-19
    • Jansson, S.1
  • 36
    • 0033012091 scopus 로고    scopus 로고
    • A guide to the Lhc genes and their relatives in Arabidopsis
    • S. Jansson A guide to the Lhc genes and their relatives in Arabidopsis Trends Plant Sci. 4 1999 236 240
    • (1999) Trends Plant Sci. , vol.4 , pp. 236-240
    • Jansson, S.1
  • 37
    • 0030740474 scopus 로고    scopus 로고
    • In vitro reconstitution of the photosystem I light-harvesting complex LHCI-730: Heterodimerization is required for antenna pigment organization
    • V.H.R. Schmid, K.V. Cammarata, B.U. Bruns, and G.W. Schmidt In vitro reconstitution of the photosystem I light-harvesting complex LHCI-730: heterodimerization is required for antenna pigment organization Proc. Natl. Acad. Sci. U. S. A. 94 1997 7667 7672
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 7667-7672
    • Schmid, V.H.R.1    Cammarata, K.V.2    Bruns, B.U.3    Schmidt, G.W.4
  • 38
    • 0031788230 scopus 로고    scopus 로고
    • Chlorina and viridis mutants of barley (Hordeum vulgare L.) allow assignment of long-wavelength chlorophyll forms to individual Lhca proteins of photosystem I in vivo
    • J. Knoetzel, B. Bossmann, and L.H. Grimme Chlorina and viridis mutants of barley (Hordeum vulgare L.) allow assignment of long-wavelength chlorophyll forms to individual Lhca proteins of photosystem I in vivo FEBS Lett. 436 1998 339 342
    • (1998) FEBS Lett. , vol.436 , pp. 339-342
    • Knoetzel, J.1    Bossmann, B.2    Grimme, L.H.3
  • 39
    • 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
    • V.H.R. Schmid, H. Paulsen, and J. Rupprecht 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.R.1    Paulsen, H.2    Rupprecht, J.3
  • 40
    • 0034810957 scopus 로고    scopus 로고
    • The properties of the chlorophyll a/b-binding proteins Lhca2 and Lhca3 studied in vivo using antisense inhibition
    • U. Ganeteg, A. Strand, P. Gustafsson, and S. Jansson The properties of the chlorophyll a/b-binding proteins Lhca2 and Lhca3 studied in vivo using antisense inhibition Plant Physiol. 127 2001 150 158
    • (2001) Plant Physiol. , vol.127 , pp. 150-158
    • Ganeteg, U.1    Strand, A.2    Gustafsson, P.3    Jansson, S.4
  • 42
    • 0035543903 scopus 로고    scopus 로고
    • Towards functional proteomics of membrane protein complexes: Analysis of thylakoid membranes from Chlamydomonas reinhardtii
    • M. Hippler, J. Klein, A. Fink, T. Allinger, and P. Hoerth Towards functional proteomics of membrane protein complexes: analysis of thylakoid membranes from Chlamydomonas reinhardtii Plant J. 28 2001 595 606
    • (2001) Plant J. , vol.28 , pp. 595-606
    • Hippler, M.1    Klein, J.2    Fink, A.3    Allinger, T.4    Hoerth, P.5
  • 43
    • 0027070688 scopus 로고
    • Characterization of chlorophyll a/b proteins from Chlamydomonas reinhardtii
    • R. Bassi, S.Y. Soen, G. Frank, H. Zuber, and J.-D. Rochaix Characterization of chlorophyll a/b proteins from Chlamydomonas reinhardtii J. Biol. Chem. 267 1992 25714 25721
    • (1992) J. Biol. Chem. , vol.267 , pp. 25714-25721
    • Bassi, R.1    Soen, S.Y.2    Frank, G.3    Zuber, H.4    Rochaix, J.-D.5
  • 45
    • 0027957259 scopus 로고
    • Evidence for a common origin of chloroplasts with light-harvesting complexes of different pigmentation
    • G.R. Wolfe, F.X. Cunningham, D. Durnford, B.R. Green, and E. Gantt Evidence for a common origin of chloroplasts with light-harvesting complexes of different pigmentation Nature 367 1994 566 568
    • (1994) Nature , vol.367 , pp. 566-568
    • Wolfe, G.R.1    Cunningham, F.X.2    Durnford, D.3    Green, B.R.4    Gantt, E.5
  • 46
    • 1542572121 scopus 로고    scopus 로고
    • The nature of a chlorophyll ligand in Lhca proteins determines the far red fluorescence emission typical of photosystem I
    • T. Morosinotto, J. Breton, R. Bassi, and R. Croce The nature of a chlorophyll ligand in Lhca proteins determines the far red fluorescence emission typical of photosystem I J. Biol. Chem. 278 2003 49223 49229
    • (2003) J. Biol. Chem. , vol.278 , pp. 49223-49229
    • Morosinotto, T.1    Breton, J.2    Bassi, R.3    Croce, R.4
  • 47
    • 0034732960 scopus 로고    scopus 로고
    • Fluorescence decay and spectral evolution in intact photosystem I of higher plants
    • R. Croce, D. Dorra, A.R. Holzwarth, and R.C. Jennings Fluorescence decay and spectral evolution in intact photosystem I of higher plants Biochemistry 39 2000 6341 6348
    • (2000) Biochemistry , vol.39 , pp. 6341-6348
    • Croce, R.1    Dorra, D.2    Holzwarth, A.R.3    Jennings, R.C.4
  • 48
    • 0037077690 scopus 로고    scopus 로고
    • Supramolecular organization of photosystem I and light- harvesting complex I in Chlamydomonas reinhardtii
    • M. Germano, A.E. Yakushevska, W. Keegstra, H.J. van Gorkom, J.P. Dekker, and E.J. Boekema 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.J.6
  • 49
    • 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
    • J. Kargul, J. Nield, and J. Barber 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
  • 50
    • 2942750314 scopus 로고    scopus 로고
    • Comparison of the subunit compositions of the PSI-LHCI supercomplex and the LHCI in the green alga Chlamydomonas reinhardtii
    • Y. Takahashi, T.-A. Yasui, E.J. Stauber, and M. Hippler Comparison of the subunit compositions of the PSI-LHCI supercomplex and the LHCI in the green alga Chlamydomonas reinhardtii Biochemistry 43 2004 7816 7823
    • (2004) Biochemistry , vol.43 , pp. 7816-7823
    • Takahashi, Y.1    Yasui, T.-A.2    Stauber, E.J.3    Hippler, M.4
  • 51
    • 0035899432 scopus 로고    scopus 로고
    • Iron deficiency induces the formation of an antenna ring around trimeric photosystem I in cyanobacteria
    • T.S. Bibby, J. Nield, and J. Barber Iron deficiency induces the formation of an antenna ring around trimeric photosystem I in cyanobacteria Nature 412 2001 743 745
    • (2001) Nature , vol.412 , pp. 743-745
    • Bibby, T.S.1    Nield, J.2    Barber, J.3
  • 53
    • 0037465820 scopus 로고    scopus 로고
    • Structural analysis of the photosystem I supercomplex of cyanobacteria induced by iron deficiency
    • J. Nield, E.P. Morris, T.S. Bibby, and J. Barber Structural analysis of the photosystem I supercomplex of cyanobacteria induced by iron deficiency Biochemistry 42 2003 3180 3188
    • (2003) Biochemistry , vol.42 , pp. 3180-3188
    • Nield, J.1    Morris, E.P.2    Bibby, T.S.3    Barber, J.4
  • 54
    • 1642506316 scopus 로고    scopus 로고
    • Adaptation of the photosynthetic electron transport chain in cyanobacteria to iron deficiency: The function of IdiA and IsiA
    • K.-P. Michel, and E.K. Pistorius Adaptation of the photosynthetic electron transport chain in cyanobacteria to iron deficiency: The function of IdiA and IsiA Physiol. Plant. 120 2004 36 50
    • (2004) Physiol. Plant. , vol.120 , pp. 36-50
    • Michel, K.-P.1    Pistorius, E.K.2
  • 55
    • 0036322691 scopus 로고    scopus 로고
    • The structure and function of CP47 and CP43 in photosystem II
    • T.M. Bricker, and L.K. Frankel The structure and function of CP47 and CP43 in photosystem II Photosynth. Res. 72 2002 131 146
    • (2002) Photosynth. Res. , vol.72 , pp. 131-146
    • Bricker, T.M.1    Frankel, L.K.2
  • 57
    • 0345701499 scopus 로고    scopus 로고
    • Time-resolved absorption and emission show that the CP43 ' antenna ring of iron-stressed Synechocystis sp PCC6803 is efficiently coupled to the photosystem I reaction center core
    • A.N. Melkozernov, T.S. Bibby, S. Lin, J. Barber, and R.E. Blankenship Time-resolved absorption and emission show that the CP43 ' antenna ring of iron-stressed Synechocystis sp PCC6803 is efficiently coupled to the photosystem I reaction center core Biochemistry 42 2003 3893 3903
    • (2003) Biochemistry , vol.42 , pp. 3893-3903
    • Melkozernov, A.N.1    Bibby, T.S.2    Lin, S.3    Barber, J.4    Blankenship, R.E.5
  • 58
    • 2642583884 scopus 로고    scopus 로고
    • Energy transfer and trapping in the photosystem I complex of Synechococcus PCC 7942 and in its supercomplex with IsiA
    • E.G. Andrizhiyevskaya, D. Frolov, R. van Grondelle, and J.P. Dekker Energy transfer and trapping in the photosystem I complex of Synechococcus PCC 7942 and in its supercomplex with IsiA Biochim. Biophys. Acta 1656 2004 104 113
    • (2004) Biochim. Biophys. Acta , vol.1656 , pp. 104-113
    • Andrizhiyevskaya, E.G.1    Frolov, D.2    Van Grondelle, R.3    Dekker, J.P.4
  • 60
    • 0037464467 scopus 로고    scopus 로고
    • Exploring the ability of chlorophyll b to bind to the CP43 ' protein induced under iron deprivation in a mutant of Synechocystis PCC 6803 containing the cao gene
    • J. Duncan, T. Bibby, A. Tanaka, and J. Barber Exploring the ability of chlorophyll b to bind to the CP43 ' protein induced under iron deprivation in a mutant of Synechocystis PCC 6803 containing the cao gene FEBS Lett. 541 2003 171 175
    • (2003) FEBS Lett. , vol.541 , pp. 171-175
    • Duncan, J.1    Bibby, T.2    Tanaka, A.3    Barber, J.4
  • 61
    • 0035923691 scopus 로고    scopus 로고
    • Chlorophyll b can serve as the major pigment in functional photosystem II complexes of cyanobacteria
    • H. Xu, D. Vavilin, and W. Vermaas Chlorophyll b can serve as the major pigment in functional photosystem II complexes of cyanobacteria Proc. Natl. Acad. Sci. U. S. A. 98 2001 14168 14173
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 14168-14173
    • Xu, H.1    Vavilin, D.2    Vermaas, W.3
  • 62
    • 0030758030 scopus 로고    scopus 로고
    • Structural organization of the major subunits in cyanobacterial photosystem 1-localization of subunits PsaC, -D, -E, -F, and -J
    • J. Kruip, P.R. Chitnis, B. Lagoutte, M. Rögner, and E.J. Boekema Structural organization of the major subunits in cyanobacterial photosystem 1-localization of subunits PsaC, -D, -E, -F, and -J J. Biol. Chem. 272 1997 17061 17069
    • (1997) J. Biol. Chem. , vol.272 , pp. 17061-17069
    • Kruip, J.1    Chitnis, P.R.2    Lagoutte, B.3    Rögner, M.4    Boekema, E.J.5
  • 65
    • 8644256371 scopus 로고    scopus 로고
    • B.R. Green W.W. Parson Kluwer Academic Publishers The Netherlands
    • B.R. Green B.R. Green W.W. Parson Light-Harvesting Antennas in Photosynthesis 2003 Kluwer Academic Publishers The Netherlands 129 168
    • (2003) Light-Harvesting Antennas in Photosynthesis , pp. 129-168
    • Green, B.R.1
  • 66
    • 0038731187 scopus 로고    scopus 로고
    • The A-type ATP synthase subunit K of Methanopyrus kandleri is deduced from its sequence to form a monomeric rotor comprising 13 hairpin domains
    • J.S. Lolkema, and E.J. Boekema The A-type ATP synthase subunit K of Methanopyrus kandleri is deduced from its sequence to form a monomeric rotor comprising 13 hairpin domains FEBS Lett. 543 2003 47 50
    • (2003) FEBS Lett. , vol.543 , pp. 47-50
    • Lolkema, J.S.1    Boekema, E.J.2
  • 68
    • 0032534790 scopus 로고    scopus 로고
    • Yeast mitochondrial F1F0-ATP synthase exists as a dimer: Identification of three dimer-specific subunits
    • I. Arnold, K. Pfeiffer, W. Neupert, R.A. Stuart, and H. Schagger Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits EMBO J. 17 1998 7170 7178
    • (1998) EMBO J. , vol.17 , pp. 7170-7178
    • Arnold, I.1    Pfeiffer, K.2    Neupert, W.3    Stuart, R.A.4    Schagger, H.5
  • 69
    • 0141786914 scopus 로고    scopus 로고
    • New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II
    • H. Eubel, L. Jansch, and H.P. Braun New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II Plant Physiol. 133 2003 274 286
    • (2003) Plant Physiol. , vol.133 , pp. 274-286
    • Eubel, H.1    Jansch, L.2    Braun, H.P.3
  • 72
    • 1542321529 scopus 로고    scopus 로고
    • 6f: Structure for signalling and vectorial metabolism
    • 6f: structure for signalling and vectorial metabolism Trends Plant Sci. 9 2004 130 137
    • (2004) Trends Plant Sci. , vol.9 , pp. 130-137
    • Allen, J.F.1
  • 73
    • 0037423885 scopus 로고    scopus 로고
    • Role of chloroplast protein kinase Stt7 in LHCII phosphorylation and state transition in Chlamydomonas
    • N. Depege, S. Bellafiore, and J.-D. Rochaix Role of chloroplast protein kinase Stt7 in LHCII phosphorylation and state transition in Chlamydomonas Science 299 2003 1572 1575
    • (2003) Science , vol.299 , pp. 1572-1575
    • Depege, N.1    Bellafiore, S.2    Rochaix, J.-D.3
  • 74
    • 0035898532 scopus 로고    scopus 로고
    • State transitions reveal the dynamics and flexibility of the photosynthetic apparatus
    • F.-A. Wollman State transitions reveal the dynamics and flexibility of the photosynthetic apparatus EMBO J. 20 2001 3623 3630
    • (2001) EMBO J. , vol.20 , pp. 3623-3630
    • Wollman, F.-A.1
  • 75
    • 3242754429 scopus 로고    scopus 로고
    • Proteomic approach to characterize the supramolecular organization of photosystems in higher plants
    • J. Heinemeyer, H. Eubel, D. Wehmhöner, L. Jänsch, and H.-P. Braun Proteomic approach to characterize the supramolecular organization of photosystems in higher plants Phytochemistry 65 2004 1683 1692
    • (2004) Phytochemistry , vol.65 , pp. 1683-1692
    • Heinemeyer, J.1    Eubel, H.2    Wehmhöner, D.3    Jänsch, L.4    Braun, H.-P.5
  • 76
    • 0026766411 scopus 로고
    • Plastoquinone compartmentation in chloroplasts: 1. Evidence for domains with different rates of photoreduction
    • P. Joliot, J. Lavergne, and D. Beal Plastoquinone compartmentation in chloroplasts: 1. Evidence for domains with different rates of photoreduction Biochim. Biophys. Acta 1101 1992 1 12
    • (1992) Biochim. Biophys. Acta , vol.1101 , pp. 1-12
    • Joliot, P.1    Lavergne, J.2    Beal, D.3
  • 77
    • 0034691753 scopus 로고    scopus 로고
    • Control of the photosynthetic electron transport by PQ diffusion microdomains in thylakoids of higher plants
    • H. Kirchhoff, S. Horstmann, and E. Weiss Control of the photosynthetic electron transport by PQ diffusion microdomains in thylakoids of higher plants Biochim. Biophys. Acta 1459 2000 148 168
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 148-168
    • Kirchhoff, H.1    Horstmann, S.2    Weiss, E.3
  • 78
    • 0026631287 scopus 로고
    • Plastoquinone compartmentation in chloroplasts. 2. Theoretical aspects
    • J. Lavergne, J.-P. Bouchaud, and P. Joliot Plastoquinone compartmentation in chloroplasts. 2. Theoretical aspects Biochim. Biophys. Acta 1101 1992 13 22
    • (1992) Biochim. Biophys. Acta , vol.1101 , pp. 13-22
    • Lavergne, J.1    Bouchaud, J.-P.2    Joliot, P.3
  • 79
    • 0037117740 scopus 로고    scopus 로고
    • Molecular architecture of the thylakoid membrane: Lipid diffusion space for plastoquinone
    • H. Kirchhoff, U. Mukherjee, and H.J. Galla Molecular architecture of the thylakoid membrane: lipid diffusion space for plastoquinone Biochemistry 41 2002 4872 4882
    • (2002) Biochemistry , vol.41 , pp. 4872-4882
    • Kirchhoff, H.1    Mukherjee, U.2    Galla, H.J.3
  • 80
    • 2642556998 scopus 로고    scopus 로고
    • Cyclic electron flow under saturating excitation of dark-adapted Arabidopsis leaves
    • P. Joliot, D. Béal, and A. Joliot Cyclic electron flow under saturating excitation of dark-adapted Arabidopsis leaves Biochim. Biophys. Acta 1656 2004 166 176
    • (2004) Biochim. Biophys. Acta , vol.1656 , pp. 166-176
    • Joliot, P.1    Béal, D.2    Joliot, A.3
  • 81
    • 1042290470 scopus 로고    scopus 로고
    • The low molecular mass subunits of the photosynthetic supracomplex, photosystem II
    • L.-X. Shi, and W.P. Schröder The low molecular mass subunits of the photosynthetic supracomplex, photosystem II Biochim. Biophys. Acta 1608 2004 75 96
    • (2004) Biochim. Biophys. Acta , vol.1608 , pp. 75-96
    • Shi, L.-X.1    Schröder, W.P.2
  • 82
    • 0033679186 scopus 로고    scopus 로고
    • Primary charge separation in photosystem II
    • J.P. Dekker, and R. van Grondelle Primary charge separation in photosystem II Photosynth. Res. 63 2000 195 208
    • (2000) Photosynth. Res. , vol.63 , pp. 195-208
    • Dekker, J.P.1    Van Grondelle, R.2
  • 83
    • 0036999722 scopus 로고    scopus 로고
    • Structure, dynamics, and energetics of the primary photochemistry of photosystem II of oxygenic photosynthesis
    • B.A. Diner, and F. Rappaport Structure, dynamics, and energetics of the primary photochemistry of photosystem II of oxygenic photosynthesis Annu. Rev. Plant Biol. 53 2002 551 580
    • (2002) Annu. Rev. Plant Biol. , vol.53 , pp. 551-580
    • Diner, B.A.1    Rappaport, F.2
  • 85
    • 0000237688 scopus 로고
    • Refined purification and further characterization of oxygen-evolving and Tris-treated photosystem II particles from the thermophilic cyanobacterium Synechococcus sp
    • J.P. Dekker, E.J. Boekema, H.T. Witt, and M. Rögner Refined purification and further characterization of oxygen-evolving and Tris-treated photosystem II particles from the thermophilic cyanobacterium Synechococcus sp Biochim. Biophys. Acta 936 1988 307 318
    • (1988) Biochim. Biophys. Acta , vol.936 , pp. 307-318
    • Dekker, J.P.1    Boekema, E.J.2    Witt, H.T.3    Rögner, M.4
  • 86
    • 0000955217 scopus 로고
    • Biochemical evidence that the higher plant photosystem II core complex is organized as a dimer
    • G.F. Peter, and J.P. Thornber Biochemical evidence that the higher plant photosystem II core complex is organized as a dimer Plant Cell Physiol. 32 1991 1237 1250
    • (1991) Plant Cell Physiol. , vol.32 , pp. 1237-1250
    • Peter, G.F.1    Thornber, J.P.2
  • 88
    • 0034623285 scopus 로고    scopus 로고
    • Three-dimensional structure of Chlamydomonas reinhardtii and Synechococcus elongatus photosystem II complexes allows for comparison of their oxygen-evolving complex organization
    • J. Nield, O. Kruse, J. Ruprecht, P. da Fonseca, C. Büchel, and J. Barber Three-dimensional structure of Chlamydomonas reinhardtii and Synechococcus elongatus photosystem II complexes allows for comparison of their oxygen-evolving complex organization J. Biol. Chem. 275 2000 27940 27946
    • (2000) J. Biol. Chem. , vol.275 , pp. 27940-27946
    • Nield, J.1    Kruse, O.2    Ruprecht, J.3    Da Fonseca, P.4    Büchel, C.5    Barber, J.6
  • 89
    • 0041806500 scopus 로고    scopus 로고
    • Structure of a photosystem II supercomplex isolated from Prochlorion didemni retaining its chlorophyll a/b light-harvesting system
    • T.S. Bibby, J. Nield, M. Chen, A.W.D. Larkum, and J. Barber Structure of a photosystem II supercomplex isolated from Prochlorion didemni retaining its chlorophyll a/b light-harvesting system Proc. Natl. Acad. Sci. U. S. A. 100 2003 9050 9054
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 9050-9054
    • Bibby, T.S.1    Nield, J.2    Chen, M.3    Larkum, A.W.D.4    Barber, J.5
  • 90
    • 0036667743 scopus 로고    scopus 로고
    • Photosystem II: A multisubunit membrane protein that oxidises water
    • J. Barber Photosystem II: a multisubunit membrane protein that oxidises water Curr. Opin. Struct. Biol. 12 2002 523 530
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 523-530
    • Barber, J.1
  • 91
    • 0031587034 scopus 로고    scopus 로고
    • Stabilization of photosystem two dimers by phosphorylation: Implication for the regulation of the turnover of D1 protein
    • O. Kruse, D. Zheleva, and J. Barber Stabilization of photosystem two dimers by phosphorylation: implication for the regulation of the turnover of D1 protein FEBS Lett. 408 1997 276 280
    • (1997) FEBS Lett. , vol.408 , pp. 276-280
    • Kruse, O.1    Zheleva, D.2    Barber, J.3
  • 93
    • 0034536337 scopus 로고    scopus 로고
    • The low molecular mass PsbW protein is involved in the stabilization of the dimeric photosystem II complex in Arabidopsis thaliana
    • L.-X. Shi, Z.J. Lorkovic, R. Oelmüller, and W.P. Schröder The low molecular mass PsbW protein is involved in the stabilization of the dimeric photosystem II complex in Arabidopsis thaliana J. Biol. Chem. 275 2000 37945 37950
    • (2000) J. Biol. Chem. , vol.275 , pp. 37945-37950
    • Shi, L.-X.1    Lorkovic, Z.J.2    Oelmüller, R.3    Schröder, W.P.4
  • 94
    • 0032568955 scopus 로고    scopus 로고
    • Isolation and characterization of monomeric and dimeric CP47-reaction center photosystem II complexes
    • D. Zheleva, J. Sharma, M. Panico, H.R. Morris, and J. Barber Isolation and characterization of monomeric and dimeric CP47-reaction center photosystem II complexes J. Biol. Chem. 273 1998 16122 16127
    • (1998) J. Biol. Chem. , vol.273 , pp. 16122-16127
    • Zheleva, D.1    Sharma, J.2    Panico, M.3    Morris, H.R.4    Barber, J.5
  • 95
    • 0034711009 scopus 로고    scopus 로고
    • Conformational changes in photosystem II supercomplexes upon removal of extrinsic subunits
    • E.J. Boekema, J.F.L. van Breemen, H. van Roon, and J.P. Dekker Conformational changes in photosystem II supercomplexes upon removal of extrinsic subunits Biochemistry 39 2000 12907 12915
    • (2000) Biochemistry , vol.39 , pp. 12907-12915
    • Boekema, E.J.1    Van Breemen, J.F.L.2    Van Roon, H.3    Dekker, J.P.4
  • 96
    • 0036338886 scopus 로고    scopus 로고
    • Photosystem II solubilizes as a monomer by mild detergent treatment of unstacked thylakoid membranes
    • J.P. Dekker, M. Germano, H. van Roon, and E.J. Boekema Photosystem II solubilizes as a monomer by mild detergent treatment of unstacked thylakoid membranes Photosynth. Res. 72 2002 203 210
    • (2002) Photosynth. Res. , vol.72 , pp. 203-210
    • Dekker, J.P.1    Germano, M.2    Van Roon, H.3    Boekema, E.J.4
  • 97
    • 0037195309 scopus 로고    scopus 로고
    • Biogenesis, assembly and turnover of photosystem II units
    • E. Baena-Gonzalez, and E.-M. Aro Biogenesis, assembly and turnover of photosystem II units Philos. Trans. R. Soc. Lond., B 357 2002 1451 1460
    • (2002) Philos. Trans. R. Soc. Lond., B , vol.357 , pp. 1451-1460
    • Baena-Gonzalez, E.1    Aro, E.-M.2
  • 98
    • 0035979783 scopus 로고    scopus 로고
    • Subunit positioning and transmembrane helix organisation in the core dimer of photosystem II
    • B. Hankamer, E. Morris, J. Nield, A. Carne, and J. Barber Subunit positioning and transmembrane helix organisation in the core dimer of photosystem II FEBS Lett. 504 2001 142 151
    • (2001) FEBS Lett. , vol.504 , pp. 142-151
    • Hankamer, B.1    Morris, E.2    Nield, J.3    Carne, A.4    Barber, J.5
  • 99
    • 0028982949 scopus 로고
    • A nuclear-encoded subunit of the photosystem II reaction center
    • K.D. Irrgang, L.-X. Shi, C. Funk, and W.P. Schröder A nuclear-encoded subunit of the photosystem II reaction center J. Biol. Chem. 270 1995 17588 17593
    • (1995) J. Biol. Chem. , vol.270 , pp. 17588-17593
    • Irrgang, K.D.1    Shi, L.-X.2    Funk, C.3    Schröder, W.P.4
  • 101
    • 0001473449 scopus 로고
    • Determination of the aggregate size in detergent solution of the light-harvesting chlorophyll a/b complex from chloroplast membranes
    • J.P.G. Butler, and W. Kühlbrandt Determination of the aggregate size in detergent solution of the light-harvesting chlorophyll a/b complex from chloroplast membranes Proc. Natl. Acad. Sci. U. S. A. 85 1988 3797 3801
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 3797-3801
    • Butler, J.P.G.1    Kühlbrandt, W.2
  • 102
    • 0032317945 scopus 로고    scopus 로고
    • Higher plants light harvesting proteins. Structure and function as revealed by mutation analysis of either protein or chromophore moieties
    • D. Sandona, R. Croce, A. Pagano, M. Crimi, and R. Bassi Higher plants light harvesting proteins. Structure and function as revealed by mutation analysis of either protein or chromophore moieties Biochim. Biophys. Acta 1365 1998 207 214
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 207-214
    • Sandona, D.1    Croce, R.2    Pagano, A.3    Crimi, M.4    Bassi, R.5
  • 103
    • 0033621082 scopus 로고    scopus 로고
    • Mutational analysis of a higher plant antenna protein provides identification of chromophores bound into multiple sites
    • R. Bassi, R. Croce, D. Cugini, and D. Sandona Mutational analysis of a higher plant antenna protein provides identification of chromophores bound into multiple sites Proc. Natl. Acad. Sci. U. S. A. 96 1999 10056 10061
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 10056-10061
    • Bassi, R.1    Croce, R.2    Cugini, D.3    Sandona, D.4
  • 104
    • 0037062584 scopus 로고    scopus 로고
    • Chromophore organization in the higher-plant photosystem II antenna protein CP26
    • R. Croce, G. Canino, F. Ros, and R. Bassi Chromophore organization in the higher-plant photosystem II antenna protein CP26 Biochemistry 41 2002 7334 7343
    • (2002) Biochemistry , vol.41 , pp. 7334-7343
    • Croce, R.1    Canino, G.2    Ros, F.3    Bassi, R.4
  • 106
    • 0037151045 scopus 로고    scopus 로고
    • Biochemical properties of the PsbS subunit of photosystem II either purified from chloroplast or recombinant
    • P. Dominici, S. Caffari, F. Armenante, S. Ceoldo, M. Crimi, and R. Bassi Biochemical properties of the PsbS subunit of photosystem II either purified from chloroplast or recombinant J. Biol. Chem. 277 2002 22750 22758
    • (2002) J. Biol. Chem. , vol.277 , pp. 22750-22758
    • Dominici, P.1    Caffari, S.2    Armenante, F.3    Ceoldo, S.4    Crimi, M.5    Bassi, R.6
  • 107
    • 0029417223 scopus 로고
    • The nuclear-encoded chlorophyll-binding photosystem-II-S protein is stable in the absence of pigments
    • C. Funk, I. Adamska, B.R. Green, B. Andersson, and G. Renger The nuclear-encoded chlorophyll-binding photosystem-II-S protein is stable in the absence of pigments J. Biol. Chem. 270 1995 30141 30147
    • (1995) J. Biol. Chem. , vol.270 , pp. 30141-30147
    • Funk, C.1    Adamska, I.2    Green, B.R.3    Andersson, B.4    Renger, G.5
  • 110
    • 0031028204 scopus 로고    scopus 로고
    • Isolation and biochemical characterisation of monomeric and dimeric photosystem II complexes from spinach and their relevance to the organisation of photosystem II in vivo
    • B. Hankamer, J. Nield, D. Zheleva, E.J. Boekema, S. Jansson, and J. Barber Isolation and biochemical characterisation of monomeric and dimeric photosystem II complexes from spinach and their relevance to the organisation of photosystem II in vivo Eur. J. Biochem. 243 1997 422 429
    • (1997) Eur. J. Biochem. , vol.243 , pp. 422-429
    • Hankamer, B.1    Nield, J.2    Zheleva, D.3    Boekema, E.J.4    Jansson, S.5    Barber, J.6
  • 111
    • 0034730964 scopus 로고    scopus 로고
    • Supermolecular structure of photosystem II and location of the PsbS protein
    • J. Nield, C. Funk, and J. Barber Supermolecular structure of photosystem II and location of the PsbS protein Proc. R. Soc. Lond. 355 2000 1337 1344
    • (2000) Proc. R. Soc. Lond. , vol.355 , pp. 1337-1344
    • Nield, J.1    Funk, C.2    Barber, J.3
  • 112
    • 0037181144 scopus 로고    scopus 로고
    • Novel approach reveals localisation and assembly pathway of the PsbS and PsbW proteins into the photosystem II dimer
    • E. Thidholm, V. Lindström, C. Tissier, C. Robinson, W.P. Schröder, and C. Funk Novel approach reveals localisation and assembly pathway of the PsbS and PsbW proteins into the photosystem II dimer FEBS Lett. 513 2002 217 222
    • (2002) FEBS Lett. , vol.513 , pp. 217-222
    • Thidholm, E.1    Lindström, V.2    Tissier, C.3    Robinson, C.4    Schröder, W.P.5    Funk, C.6
  • 113
    • 0033989509 scopus 로고    scopus 로고
    • 3D map of the plant photosystem II supercomplex obtained by cryoelectron microscopy and single particle analysis
    • J. Nield, E.V. Orlova, E.P. Morris, B. Gowen, M. van Heel, and J. Barber 3D map of the plant photosystem II supercomplex obtained by cryoelectron microscopy and single particle analysis Nat. Struct. Biol. 7 2000 44 47
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 44-47
    • Nield, J.1    Orlova, E.V.2    Morris, E.P.3    Gowen, B.4    Van Heel, M.5    Barber, J.6
  • 114
    • 0038043211 scopus 로고    scopus 로고
    • Associations between light-harvesting complexes and photosystem II from Marchantia polymorpha L. determined by two- and three-dimensional electron microscopy
    • R. Harrer Associations between light-harvesting complexes and photosystem II from Marchantia polymorpha L. determined by two- and three-dimensional electron microscopy Photosynth. Res. 75 2003 249 258
    • (2003) Photosynth. Res. , vol.75 , pp. 249-258
    • Harrer, R.1
  • 115
    • 0036156186 scopus 로고    scopus 로고
    • An alternative model for photosystem II/light harvesting complex II in grana membranes based on cryo-electron microscopy studies
    • R.C. Ford, S.S. Stoylova, and A. Holzenburg An alternative model for photosystem II/light harvesting complex II in grana membranes based on cryo-electron microscopy studies Eur. J. Biochem. 269 2002 326 336
    • (2002) Eur. J. Biochem. , vol.269 , pp. 326-336
    • Ford, R.C.1    Stoylova, S.S.2    Holzenburg, A.3
  • 116
    • 0033034478 scopus 로고    scopus 로고
    • Isolation of a highly active PSII-LHCII supercomplex from thylakoid membranes by a direct method
    • S. Eshagi, B. Andersson, and J. Barber Isolation of a highly active PSII-LHCII supercomplex from thylakoid membranes by a direct method FEBS Lett. 446 1999 23 26
    • (1999) FEBS Lett. , vol.446 , pp. 23-26
    • Eshagi, S.1    Andersson, B.2    Barber, J.3
  • 117
    • 0034474886 scopus 로고    scopus 로고
    • Solubilization of green plant thylakoid membranes with n-dodecyl-α,d-maltoside. Implications for the structural organization of the Photosystem II, Photosystem I, ATP synthase and cytochrome b(6)f complexes
    • H. van Roon, J.F.L. van Breemen, F.L. de Weerd, J.P. Dekker, and E.J. Boekema Solubilization of green plant thylakoid membranes with n-dodecyl-α,d-maltoside. Implications for the structural organization of the Photosystem II, Photosystem I, ATP synthase and cytochrome b(6)f complexes Photosynth. Res. 64 2000 155 166
    • (2000) Photosynth. Res. , vol.64 , pp. 155-166
    • Van Roon, H.1    Van Breemen, J.F.L.2    De Weerd, F.L.3    Dekker, J.P.4    Boekema, E.J.5
  • 118
    • 1942470702 scopus 로고    scopus 로고
    • Structural analysis of photosystem II in far-red-light-adapted thylakoid membranes-new crystal forms provide evidence for a dynamic reorganization of light-harvesting antennae subunits
    • S. Stoylova, T.D. Flint, R.C. Ford, and A. Holzenburg Structural analysis of photosystem II in far-red-light-adapted thylakoid membranes-new crystal forms provide evidence for a dynamic reorganization of light-harvesting antennae subunits Eur. J. Biochem. 267 2000 207 215
    • (2000) Eur. J. Biochem. , vol.267 , pp. 207-215
    • Stoylova, S.1    Flint, T.D.2    Ford, R.C.3    Holzenburg, A.4
  • 119
    • 0033629352 scopus 로고    scopus 로고
    • The polypeptides of photosystem II and their influence on manganotyrosyl-based oxygen evolution
    • R.J. Debus The polypeptides of photosystem II and their influence on manganotyrosyl-based oxygen evolution Met. Ions Biol. Syst. 37 2000 657 711
    • (2000) Met. Ions Biol. Syst. , vol.37 , pp. 657-711
    • Debus, R.J.1
  • 120
    • 0037161244 scopus 로고    scopus 로고
    • Electron crystallographic study of photosystem II from the cyanobacterium Synechococcus elongatus
    • P. da Fonseca, E.P. Morris, B. Hankamer, and J. Barber Electron crystallographic study of photosystem II from the cyanobacterium Synechococcus elongatus Biochemistry 41 2002 5163 5167
    • (2002) Biochemistry , vol.41 , pp. 5163-5167
    • Da Fonseca, P.1    Morris, E.P.2    Hankamer, B.3    Barber, J.4
  • 121
    • 0032032367 scopus 로고    scopus 로고
    • Localization of the 23-kDa subunit of the oxygen-evolving complex of photosystem II by electron microscopy
    • E.J. Boekema, J. Nield, B. Hankamer, and J. Barber Localization of the 23-kDa subunit of the oxygen-evolving complex of photosystem II by electron microscopy Eur. J. Biochem. 252 1998 268 276
    • (1998) Eur. J. Biochem. , vol.252 , pp. 268-276
    • Boekema, E.J.1    Nield, J.2    Hankamer, B.3    Barber, J.4
  • 122
    • 0000932046 scopus 로고    scopus 로고
    • Localization of cyanobacterial photosystem II donor-side subunits by electron microscopy and the supramolecular organization of photosystem II in the thylakoid membrane
    • H. Kuhl, M. Rögner, J.F.L. van Breemen, and E.J. Boekema Localization of cyanobacterial photosystem II donor-side subunits by electron microscopy and the supramolecular organization of photosystem II in the thylakoid membrane Eur. J. Biochem. 266 1999 453 459
    • (1999) Eur. J. Biochem. , vol.266 , pp. 453-459
    • Kuhl, H.1    Rögner, M.2    Van Breemen, J.F.L.3    Boekema, E.J.4
  • 123
    • 0041875132 scopus 로고    scopus 로고
    • Electron microscopy in structural studies of photosystem II
    • L. Bumba, and F. Vacha Electron microscopy in structural studies of photosystem II Photosynth. Res. 77 2003 1 19
    • (2003) Photosynth. Res. , vol.77 , pp. 1-19
    • Bumba, L.1    Vacha, F.2
  • 124
    • 0030611016 scopus 로고    scopus 로고
    • Mutation Val235Ala weakens binding of the 33-kDa manganese stabilizing protein of photosystem II to one of two sites
    • S.D. Betts, J.R. Ross, E. Pichersky, and C.F. Yocum Mutation Val235Ala weakens binding of the 33-kDa manganese stabilizing protein of photosystem II to one of two sites Biochemistry 36 1997 4047 4053
    • (1997) Biochemistry , vol.36 , pp. 4047-4053
    • Betts, S.D.1    Ross, J.R.2    Pichersky, E.3    Yocum, C.F.4
  • 125
    • 0037031244 scopus 로고    scopus 로고
    • N-terminal truncations of manganese stabilizing protein identify two amino acid sequences required for binding of the eukaryotic protein to photosystem II and reveal the absence of one binding-related sequence in cyanobacteria
    • H. Popelkova, M.M. Im, and C.F. Yocum N-terminal truncations of manganese stabilizing protein identify two amino acid sequences required for binding of the eukaryotic protein to photosystem II and reveal the absence of one binding-related sequence in cyanobacteria Biochemistry 41 2002 10038 10045
    • (2002) Biochemistry , vol.41 , pp. 10038-10045
    • Popelkova, H.1    Im, M.M.2    Yocum, C.F.3
  • 126
    • 0032489346 scopus 로고    scopus 로고
    • Specific association of photosystem II and light-harvesting complex II in partially solubilized photosystem II membranes
    • E.J. Boekema, H. van Roon, and J.P. Dekker Specific association of photosystem II and light-harvesting complex II in partially solubilized photosystem II membranes FEBS Lett. 424 1998 95 99
    • (1998) FEBS Lett. , vol.424 , pp. 95-99
    • Boekema, E.J.1    Van Roon, H.2    Dekker, J.P.3
  • 127
    • 0039848607 scopus 로고    scopus 로고
    • Multiple types of association of photosystem II and its light-harvesting antenna in partially solubilized photosystem II membranes
    • E.J. Boekema, H. van Roon, F. Calkoen, R. Bassi, and J.P. Dekker Multiple types of association of photosystem II and its light-harvesting antenna in partially solubilized photosystem II membranes Biochemistry 38 1999 2233 2239
    • (1999) Biochemistry , vol.38 , pp. 2233-2239
    • Boekema, E.J.1    Van Roon, H.2    Calkoen, F.3    Bassi, R.4    Dekker, J.P.5
  • 128
    • 0033486045 scopus 로고    scopus 로고
    • Supramolecular organization of photosystem II and its light-harvesting antenna in partially solubilized photosystem II membranes
    • E.J. Boekema, H. van Roon, J.F.L van Breemen, and J.P. Dekker Supramolecular organization of photosystem II and its light-harvesting antenna in partially solubilized photosystem II membranes Eur. J. Biochem. 266 1999 444 452
    • (1999) Eur. J. Biochem. , vol.266 , pp. 444-452
    • Boekema, E.J.1    Van Roon, H.2    Van Breemen, F.L.3    Dekker, J.P.4
  • 130
    • 0026056608 scopus 로고
    • Biochemical composition and organization of higher plant photosystem II light-harvesting pigment proteins
    • G.F. Peter, and J.P. Thornber Biochemical composition and organization of higher plant photosystem II light-harvesting pigment proteins J. Biol. Chem. 266 1991 16745 16754
    • (1991) J. Biol. Chem. , vol.266 , pp. 16745-16754
    • Peter, G.F.1    Thornber, J.P.2
  • 131
    • 0026541431 scopus 로고
    • A supramolecular light-harvesting complex from chloroplast photosystem II membranes
    • R. Bassi, and P. Dainese A supramolecular light-harvesting complex from chloroplast photosystem II membranes Eur. J. Biochem. 204 1992 317 326
    • (1992) Eur. J. Biochem. , vol.204 , pp. 317-326
    • Bassi, R.1    Dainese, P.2
  • 133
    • 0041565102 scopus 로고    scopus 로고
    • Absence of the Lhcb1 and Lhcb2 proteins of the light-harvesting complex of photosystem II - Effects on photosynthesis, grana stacking and fitness
    • J. Andersson, M. Wentworth, R.G. Walters, C.A. Howard, A.V. Ruban, P. Horton, and S. Jansson Absence of the Lhcb1 and Lhcb2 proteins of the light-harvesting complex of photosystem II - effects on photosynthesis, grana stacking and fitness Plant J. 35 2003 350 381
    • (2003) Plant J. , vol.35 , pp. 350-381
    • Andersson, J.1    Wentworth, M.2    Walters, R.G.3    Howard, C.A.4    Ruban, A.V.5    Horton, P.6    Jansson, S.7
  • 134
    • 0032125846 scopus 로고    scopus 로고
    • Nearest-neighbor analysis of a photosystem II complex from Marchantia polymorpha L. (liverwort), which contains reaction center and antenna proteins
    • R. Harrer, R. Bassi, M.G. Testi, and C. Schäfer Nearest-neighbor analysis of a photosystem II complex from Marchantia polymorpha L. (liverwort), which contains reaction center and antenna proteins Eur. J. Biochem. 255 1998 196 205
    • (1998) Eur. J. Biochem. , vol.255 , pp. 196-205
    • Harrer, R.1    Bassi, R.2    Testi, M.G.3    Schäfer, C.4
  • 136
    • 0035020030 scopus 로고    scopus 로고
    • Antisense inhibition of the photosynthetic antenna proteins CP29 and CP26: Implications for the mechanism of protective energy dissipation
    • J. Andersson, R.G. Walters, P. Horton, and S. Jansson Antisense inhibition of the photosynthetic antenna proteins CP29 and CP26: Implications for the mechanism of protective energy dissipation Plant Cell 13 2001 1193 1204
    • (2001) Plant Cell , vol.13 , pp. 1193-1204
    • Andersson, J.1    Walters, R.G.2    Horton, P.3    Jansson, S.4
  • 137
    • 0037025137 scopus 로고    scopus 로고
    • Rapid regulation of light harvesting and plant fitness in the field
    • C. Külheim, J. Ågren, and S. Jansson Rapid regulation of light harvesting and plant fitness in the field Science 297 2002 91 93
    • (2002) Science , vol.297 , pp. 91-93
    • Külheim, C.1    Ågren, J.2    Jansson, S.3
  • 138
    • 0842263994 scopus 로고    scopus 로고
    • Is each light-harvesting complex protein important for plant fitness?
    • U. Ganeteg, C. Külheim, J. Andersson, and S. Jansson Is each light-harvesting complex protein important for plant fitness? Plant Physiol. 134 2004 502 509
    • (2004) Plant Physiol. , vol.134 , pp. 502-509
    • Ganeteg, U.1    Külheim, C.2    Andersson, J.3    Jansson, S.4
  • 139
    • 0034678449 scopus 로고    scopus 로고
    • A small chloroplast-encoded protein as a novel architectural component of the light-harvesting antenna
    • S. Ruf, K. Biehler, and R. Bock A small chloroplast-encoded protein as a novel architectural component of the light-harvesting antenna J. Cell Biol. 149 2000 369 378
    • (2000) J. Cell Biol. , vol.149 , pp. 369-378
    • Ruf, S.1    Biehler, K.2    Bock, R.3
  • 141
    • 1642580518 scopus 로고    scopus 로고
    • Protein assembly of photosystem II and accumulation of subcomplexes in the absence of low molecular mass subunits PsbL and PsbJ
    • M. Suorsa, R.E. Regel, V. Paakkarinen, N. Battchikova, R.G. Herrmann, and E.-M. Aro Protein assembly of photosystem II and accumulation of subcomplexes in the absence of low molecular mass subunits PsbL and PsbJ Eur. J. Biochem. 271 2004 96 107
    • (2004) Eur. J. Biochem. , vol.271 , pp. 96-107
    • Suorsa, M.1    Regel, R.E.2    Paakkarinen, V.3    Battchikova, N.4    Herrmann, R.G.5    Aro, E.-M.6
  • 142
    • 0019316151 scopus 로고
    • Lateral heterogeneity in the distribution of chlorophyll-protein complexes of the thylakoid membranes of spinach chloroplasts
    • B. Andersson, and J.M. Anderson Lateral heterogeneity in the distribution of chlorophyll-protein complexes of the thylakoid membranes of spinach chloroplasts Biochim. Biophys. Acta 593 1980 427 440
    • (1980) Biochim. Biophys. Acta , vol.593 , pp. 427-440
    • Andersson, B.1    Anderson, J.M.2
  • 143
    • 0032930879 scopus 로고    scopus 로고
    • Heptameric association of light-harvesting complex II trimers in partially solubilized photosystem II membranes
    • J.P. Dekker, H. van Roon, and E.J. Boekema Heptameric association of light-harvesting complex II trimers in partially solubilized photosystem II membranes FEBS Lett. 449 1999 211 214
    • (1999) FEBS Lett. , vol.449 , pp. 211-214
    • Dekker, J.P.1    Van Roon, H.2    Boekema, E.J.3
  • 144
    • 0033537961 scopus 로고    scopus 로고
    • Determination of the stoichiometry and strength of binding of xanthophylls to the photosystem II light harvesting complexes
    • A.V. Ruban, P.J. Lee, M. Wentworth, A.J. Young, and P. Horton Determination of the stoichiometry and strength of binding of xanthophylls to the photosystem II light harvesting complexes J. Biol. Chem. 274 1999 10458 10465
    • (1999) J. Biol. Chem. , vol.274 , pp. 10458-10465
    • Ruban, A.V.1    Lee, P.J.2    Wentworth, M.3    Young, A.J.4    Horton, P.5
  • 145
    • 0041859209 scopus 로고    scopus 로고
    • Chloroplast structure: From chlorophyll granules to supra-molecular architecture of thylakoid membranes
    • L.A. Staehelin Chloroplast structure: from chlorophyll granules to supra-molecular architecture of thylakoid membranes Photosynth. Res. 76 2003 185 196
    • (2003) Photosynth. Res. , vol.76 , pp. 185-196
    • Staehelin, L.A.1
  • 146
    • 0017190320 scopus 로고
    • Reversible particle movements associated with unstacking and restacking of chloroplast membranes in vitro
    • L.A. Staehelin Reversible particle movements associated with unstacking and restacking of chloroplast membranes in vitro J. Cell Biol. 71 1976 136 158
    • (1976) J. Cell Biol. , vol.71 , pp. 136-158
    • Staehelin, L.A.1
  • 147
    • 0017102622 scopus 로고
    • Light-harvesting chlorophyll-protein complex of photosystem 2. Its location in photosynthetic membrane
    • K.R. Miller, G.J. Miller, and K.R. McIntyre Light-harvesting chlorophyll-protein complex of photosystem 2. Its location in photosynthetic membrane J. Cell Biol. 71 1976 624 638
    • (1976) J. Cell Biol. , vol.71 , pp. 624-638
    • Miller, K.R.1    Miller, G.J.2    McIntyre, K.R.3
  • 148
    • 0001184401 scopus 로고
    • Freeze-fracture studies on barley plastid membranes. 2. Wild-type chloroplast
    • D.J. Simpson Freeze-fracture studies on barley plastid membranes. 2. Wild-type chloroplast Carlsberg Res. Commun. 43 1978 365 389
    • (1978) Carlsberg Res. Commun. , vol.43 , pp. 365-389
    • Simpson, D.J.1
  • 149
    • 0034283146 scopus 로고    scopus 로고
    • Arrangement of photosystem II supercomplexes in crystalline macrodomains within the thylakoid membrane of green plant chloroplasts
    • E.J. Boekema, J.F.L. van Breemen, H. van Roon, and J.P. Dekker Arrangement of photosystem II supercomplexes in crystalline macrodomains within the thylakoid membrane of green plant chloroplasts J. Mol. Biol. 301 2000 1123 1133
    • (2000) J. Mol. Biol. , vol.301 , pp. 1123-1133
    • Boekema, E.J.1    Van Breemen, J.F.L.2    Van Roon, H.3    Dekker, J.P.4
  • 151
    • 0028346592 scopus 로고
    • 3-Dimensional structure of the higher plant photosystem II reaction center and evidence for its dimeric organization in vivo
    • C. Santini, V. Tidu, G. Tognon, A. Ghiretti Magaldi, and R. Bassi 3-Dimensional structure of the higher plant photosystem II reaction center and evidence for its dimeric organization in vivo Eur. J. Biochem. 221 1994 307 315
    • (1994) Eur. J. Biochem. , vol.221 , pp. 307-315
    • Santini, C.1    Tidu, V.2    Tognon, G.3    Ghiretti Magaldi, A.4    Bassi, R.5
  • 152
    • 0034802940 scopus 로고    scopus 로고
    • Identification of Lhcb gene family encoding the light-harvesting chlorophyll a/b proteins of photosystem II in Chlamydomonas reinhardtii
    • H. Teramoto, T.-A. Ono, and J. Minagawa Identification of Lhcb gene family encoding the light-harvesting chlorophyll a/b proteins of photosystem II in Chlamydomonas reinhardtii Plant Cell Physiol. 42 2001 849 856
    • (2001) Plant Cell Physiol. , vol.42 , pp. 849-856
    • Teramoto, H.1    Ono, T.-A.2    Minagawa, J.3
  • 153
    • 0028877960 scopus 로고
    • Particle regularity on thylakoid fracture faces is influenced by storage conditions
    • G.A. Semenova Particle regularity on thylakoid fracture faces is influenced by storage conditions Can. J. Bot. 73 1995 1676 1682
    • (1995) Can. J. Bot. , vol.73 , pp. 1676-1682
    • Semenova, G.A.1
  • 154
    • 0028963541 scopus 로고
    • Factors influencing PS II particle array formation in Arabidopsis thaliana chloroplasts and the relationship of such arrays to the thermostability of PS II
    • N.M. Tsvetkova, E.L. Apostolova, A.P.R. Brain, W.P. Williams, and P.J. Quinn Factors influencing PS II particle array formation in Arabidopsis thaliana chloroplasts and the relationship of such arrays to the thermostability of PS II Biochim. Biophys. Acta 1228 1995 201 210
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 201-210
    • Tsvetkova, N.M.1    Apostolova, E.L.2    Brain, A.P.R.3    Williams, W.P.4    Quinn, P.J.5
  • 155
    • 0343500214 scopus 로고
    • Alterations in chloroplast thylakoids during cold acclimation
    • M.P. Garber, and P.L. Steponkus Alterations in chloroplast thylakoids during cold acclimation Plant Physiol. 57 1976 681 686
    • (1976) Plant Physiol. , vol.57 , pp. 681-686
    • Garber, M.P.1    Steponkus, P.L.2
  • 156
    • 0037417876 scopus 로고    scopus 로고
    • A quantitative structure-function relationship for the Photosystern II reaction center: Supermolecular behavior in natural photosynthesis
    • L.M.C. Barter, J.R. Durrant, and D.R. Klug A quantitative structure-function relationship for the Photosystern II reaction center: supermolecular behavior in natural photosynthesis Proc. Natl. Acad. Sci. U. S. A. 100 2003 946 951
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 946-951
    • Barter, L.M.C.1    Durrant, J.R.2    Klug, D.R.3
  • 159
    • 0035902455 scopus 로고    scopus 로고
    • Excited-state dynamics in photosystem II: Insights from the X-ray crystal structure
    • S. Vasil'ev, P. Orth, A. Zouni, T.G. Owens, and D. Bruce Excited-state dynamics in photosystem II: Insights from the X-ray crystal structure Proc. Natl. Acad. Sci. U. S. A. 98 2001 8602 8607
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 8602-8607
    • Vasil'Ev, S.1    Orth, P.2    Zouni, A.3    Owens, T.G.4    Bruce, D.5
  • 160
    • 1542328222 scopus 로고    scopus 로고
    • The orientations of core antenna chlorophylls in photosystem II are optimized to maximize the quantum yield of photosynthesis
    • S. Vasil'ev, J.-R. Shen, N. Kamiya, and D. Bruce The orientations of core antenna chlorophylls in photosystem II are optimized to maximize the quantum yield of photosynthesis FEBS Lett. 561 2004 111 116
    • (2004) FEBS Lett. , vol.561 , pp. 111-116
    • Vasil'Ev, S.1    Shen, J.-R.2    Kamiya, N.3    Bruce, D.4
  • 163
    • 0001561513 scopus 로고
    • Primary electrogenic reactions of photosystem II as probed by the light gradient method
    • H.-W. Trissl, J. Breton, J. Deprez, and W. Leibl Primary electrogenic reactions of photosystem II as probed by the light gradient method Biochim. Biophys. Acta 893 1987 305 319
    • (1987) Biochim. Biophys. Acta , vol.893 , pp. 305-319
    • Trissl, H.-W.1    Breton, J.2    Deprez, J.3    Leibl, W.4
  • 164
    • 0000341531 scopus 로고
    • Photoelectric study on the kinetics of trapping and charge stabilization in oriented PSII membranes
    • W. Leibl, J. Breton, J. Deprez, and H.-W. Trissl Photoelectric study on the kinetics of trapping and charge stabilization in oriented PSII membranes
    • (1989) Photosynth. Res. , vol.22 , pp. 257-275
    • Leibl, W.1    Breton, J.2    Deprez, J.3    Trissl, H.-W.4
  • 165
    • 0037112863 scopus 로고    scopus 로고
    • From chloroplasts to photosystems: In situ scanning force microscopy on intact thylakoid membranes
    • D. Kaftan, V. Blumfeld, R. Nevo, A. Scherz, and Z. Reich From chloroplasts to photosystems: in situ scanning force microscopy on intact thylakoid membranes EMBO J. 21 2002 6146 6153
    • (2002) EMBO J. , vol.21 , pp. 6146-6153
    • Kaftan, D.1    Blumfeld, V.2    Nevo, R.3    Scherz, A.4    Reich, Z.5
  • 166
    • 0037712992 scopus 로고    scopus 로고
    • Granum revisited. A three-dimensional model-where things fall into place
    • L. Mustárdy, and G. Garab Granum revisited. A three-dimensional model-where things fall into place Trends Plant Sci. 8 2003 117 122
    • (2003) Trends Plant Sci. , vol.8 , pp. 117-122
    • Mustárdy, L.1    Garab, G.2
  • 167
    • 11044232979 scopus 로고    scopus 로고
    • The constant proportion of grana and stroma lamellae in plant chloroplasts
    • P.Å. Albertsson, and E. Andreasson The constant proportion of grana and stroma lamellae in plant chloroplasts Physiol. Plant. 121 2004 334 342
    • (2004) Physiol. Plant. , vol.121 , pp. 334-342
    • Albertsson, P.Å.1    Andreasson, E.2
  • 168
    • 0000639002 scopus 로고
    • Interaction between the lumenal sides of the thylakoid membrane
    • P.-Å. Albertsson Interaction between the lumenal sides of the thylakoid membrane FEBS Lett. 149 1982 186 190
    • (1982) FEBS Lett. , vol.149 , pp. 186-190
    • Albertsson, P.-Å.1
  • 169
    • 85006166266 scopus 로고
    • Protonation and chloroplast membrane structure
    • S. Murakami, and L. Packer Protonation and chloroplast membrane structure J. Cell Biol. 47 1970 332 351
    • (1970) J. Cell Biol. , vol.47 , pp. 332-351
    • Murakami, S.1    Packer, L.2
  • 170
    • 0037195312 scopus 로고    scopus 로고
    • Structural and functional dynamics of plant photosystem II
    • J.M. Anderson, and W.S. Chow Structural and functional dynamics of plant photosystem II Philos. Trans. R. Soc. Lond., B 357 2002 1421 1430
    • (2002) Philos. Trans. R. Soc. Lond., B , vol.357 , pp. 1421-1430
    • Anderson, J.M.1    Chow, W.S.2
  • 171
    • 0347506349 scopus 로고    scopus 로고
    • The proteome of the chloroplast lumen of higher plants
    • T. Kieselbach, and W.P. Schröder The proteome of the chloroplast lumen of higher plants Photosynth. Res. 78 2003 249 264
    • (2003) Photosynth. Res. , vol.78 , pp. 249-264
    • Kieselbach, T.1    Schröder, W.P.2
  • 172
    • 46149128229 scopus 로고
    • The molecular organization of the photosynthetic membranes of higher plants
    • D.J. Murphy The molecular organization of the photosynthetic membranes of higher plants Biochim. Biophys. Acta 864 1986 33 94
    • (1986) Biochim. Biophys. Acta , vol.864 , pp. 33-94
    • Murphy, D.J.1
  • 173
    • 0035214910 scopus 로고    scopus 로고
    • A quantitative model of the domain structure of the photosynthetic membrane
    • P.-Å. Albertsson A quantitative model of the domain structure of the photosynthetic membrane Trends Plant Sci. 6 2001 349 354
    • (2001) Trends Plant Sci. , vol.6 , pp. 349-354
    • Albertsson, P.-Å.1
  • 174
    • 1642559319 scopus 로고    scopus 로고
    • Quantification of photosystem I and II in different parts of the thylakoid membrane from spinach
    • R. Danielsson, P.-Å. Albertsson, F. Mamedov, and S. Styring Quantification of photosystem I and II in different parts of the thylakoid membrane from spinach Biochim. Biophys. Acta 1608 2004 53 61
    • (2004) Biochim. Biophys. Acta , vol.1608 , pp. 53-61
    • Danielsson, R.1    Albertsson, P.-Å.2    Mamedov, F.3    Styring, S.4
  • 175
    • 0035651544 scopus 로고    scopus 로고
    • Molecular recognition in thylakoid structure and function
    • J.F. Allen, and J. Forsberg 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
  • 176
    • 0345170107 scopus 로고    scopus 로고
    • Dependence of plastoquinol diffusion on the shape, size, and density of integral thylakoid proteins
    • I.G. Tremmel, H. Kirchhoff, E. Weis, and G.D. Farquhar Dependence of plastoquinol diffusion on the shape, size, and density of integral thylakoid proteins Biochim. Biophys. Acta 1607 2003 97 109
    • (2003) Biochim. Biophys. Acta , vol.1607 , pp. 97-109
    • Tremmel, I.G.1    Kirchhoff, H.2    Weis, E.3    Farquhar, G.D.4
  • 177
    • 0002439821 scopus 로고
    • Distribution of the cytochromes of spinach chloroplasts between the appressed membranes of grana stacks and stroma-exposed thylakoid regions
    • J.M. Anderson Distribution of the cytochromes of spinach chloroplasts between the appressed membranes of grana stacks and stroma-exposed thylakoid regions FEBS Lett. 138 1982 62 66
    • (1982) FEBS Lett. , vol.138 , pp. 62-66
    • Anderson, J.M.1
  • 178
    • 11044220426 scopus 로고
    • 6f complex and coupling factor ATP synthetase complexes of chloroplast thylakoid membranes
    • 6f complex and coupling factor ATP synthetase complexes of chloroplast thylakoid membranes Plant Physiol. 78 1985 199 202
    • (1985) Plant Physiol. , vol.78 , pp. 199-202
    • Allred, D.R.1    Staehelin, L.A.2
  • 180
    • 0000075484 scopus 로고
    • A highly-resolved, oxygen-evolving photosystem II preparation from spinach thylakoid membranes
    • D.A. Berthold, G.T. Babcock, and C.F. Yocum A highly-resolved, oxygen-evolving photosystem II preparation from spinach thylakoid membranes FEBS Lett. 134 1981 231 234
    • (1981) FEBS Lett. , vol.134 , pp. 231-234
    • Berthold, D.A.1    Babcock, G.T.2    Yocum, C.F.3
  • 181
    • 0000376012 scopus 로고
    • Structural, biochemical and biophysical characterization of four oxygen-evolving photosystem II preparations from spinach
    • T.G. Dunahay, L.A. Staehelin, M. Seibert, P.D. Ogilvie, and S.P. Berg Structural, biochemical and biophysical characterization of four oxygen-evolving photosystem II preparations from spinach Biochim. Biophys. Acta 764 1984 179 193
    • (1984) Biochim. Biophys. Acta , vol.764 , pp. 179-193
    • Dunahay, T.G.1    Staehelin, L.A.2    Seibert, M.3    Ogilvie, P.D.4    Berg, S.P.5
  • 182
    • 0024075788 scopus 로고
    • Biogenesis of thylakoid membranes is controlled by light intensity in the conditional chlorophyll b-deficient CD3 mutant of wheat
    • K.D. Allen, M.E. Duysen, and L.A. Staehelin Biogenesis of thylakoid membranes is controlled by light intensity in the conditional chlorophyll b-deficient CD3 mutant of wheat J. Cell Biol. 107 1988 907 919
    • (1988) J. Cell Biol. , vol.107 , pp. 907-919
    • Allen, K.D.1    Duysen, M.E.2    Staehelin, L.A.3
  • 183
    • 0026069088 scopus 로고
    • Surface charges, the heterogeneous lateral distribution of the two photosystems, and thylakoid stacking
    • W.S. Chow, C. Miller, and J.M. Anderson Surface charges, the heterogeneous lateral distribution of the two photosystems, and thylakoid stacking Biochim. Biophys. Acta 1057 1991 69 77
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 69-77
    • Chow, W.S.1    Miller, C.2    Anderson, J.M.3
  • 184
    • 0001299286 scopus 로고
    • Influence of surface charges on thylakoid structure and function
    • J. Barber Influence of surface charges on thylakoid structure and function Annu. Rev. Plant Physiol. 33 1982 261 295
    • (1982) Annu. Rev. Plant Physiol. , vol.33 , pp. 261-295
    • Barber, J.1
  • 186
    • 0026562059 scopus 로고
    • The structure of photosystem I from the thermophilic cyanobacterium Synechococcus sp. determined by electron microscopy of two-dimensional crystals
    • B. Böttcher, P. Gräber, and E.J. Boekema The structure of photosystem I from the thermophilic cyanobacterium Synechococcus sp. determined by electron microscopy of two-dimensional crystals Biochim. Biophys. Acta 1100 1992 125 136
    • (1992) Biochim. Biophys. Acta , vol.1100 , pp. 125-136
    • Böttcher, B.1    Gräber, P.2    Boekema, E.J.3
  • 187
    • 0033865042 scopus 로고    scopus 로고
    • Synthesis, assembly and degradation of thylakoid membrane proteins
    • Y. Choquet, and O. Vallon Synthesis, assembly and degradation of thylakoid membrane proteins Biochimie 82 2000 615 634
    • (2000) Biochimie , vol.82 , pp. 615-634
    • Choquet, Y.1    Vallon, O.2
  • 188
    • 0032910388 scopus 로고    scopus 로고
    • The biogenesis and assembly of photosynthetic proteins in thylakoid membranes
    • F.-A. Wollman, L. Minai, and R. Nechustai The biogenesis and assembly of photosynthetic proteins in thylakoid membranes Biochim. Biophys. Acta 1411 1999 21 85
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 21-85
    • Wollman, F.-A.1    Minai, L.2    Nechustai, R.3
  • 189
    • 0027359059 scopus 로고
    • Why do thylakoid membranes from higher plants form grana stacks?
    • H.-W. Trissl, and C. Wilhelm Why do thylakoid membranes from higher plants form grana stacks? Trends Biochem. Sci. 18 1993 415 419
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 415-419
    • Trissl, H.-W.1    Wilhelm, C.2
  • 190
    • 0033371842 scopus 로고    scopus 로고
    • Are grana necessary for regulation of light harvesting?
    • P. Horton Are grana necessary for regulation of light harvesting? Aust. J. Plant Physiol. 26 1999 659 669
    • (1999) Aust. J. Plant Physiol. , vol.26 , pp. 659-669
    • Horton, P.1
  • 191
    • 0002276039 scopus 로고
    • Photoregulation of the composition, function and structure of thylakoid membranes
    • J.M. Anderson Photoregulation of the composition, function and structure of thylakoid membranes Annu. Rev. Plant Physiol. Plant Mol. Biol. 37 1986 93 136
    • (1986) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.37 , pp. 93-136
    • Anderson, J.M.1
  • 194
    • 0035653682 scopus 로고    scopus 로고
    • Balance of power: A view of the mechanism of photosynthetic state transitions
    • A. Haldrup, P.E. Jensen, C. Lunde, and H.V. Scheller Balance of power: a view of the mechanism of photosynthetic state transitions Trends Plant Sci. 6 2001 301 305
    • (2001) Trends Plant Sci. , vol.6 , pp. 301-305
    • Haldrup, A.1    Jensen, P.E.2    Lunde, C.3    Scheller, H.V.4
  • 195
    • 0037423884 scopus 로고    scopus 로고
    • State transitions-a question of balance
    • J.F. Allen State transitions-a question of balance Science 299 2003 1530 1532
    • (2003) Science , vol.299 , pp. 1530-1532
    • Allen, J.F.1
  • 196
    • 0033515448 scopus 로고    scopus 로고
    • TAKs, thylakoid membrane protein kinases associated with energy transduction
    • S. Snyders, and B.D. Kohorn TAKs, thylakoid membrane protein kinases associated with energy transduction J. Biol. Chem. 274 1999 9137 9140
    • (1999) J. Biol. Chem. , vol.274 , pp. 9137-9140
    • Snyders, S.1    Kohorn, B.D.2
  • 197
    • 0035943616 scopus 로고    scopus 로고
    • Disruption of thylakoid-associated kinase 1 leads to alteration of light-harvesting in Arabidopsis
    • S. Snyders, and B.D. Kohorn Disruption of thylakoid-associated kinase 1 leads to alteration of light-harvesting in Arabidopsis J. Biol. Chem. 276 2001 32169 32176
    • (2001) J. Biol. Chem. , vol.276 , pp. 32169-32176
    • Snyders, S.1    Kohorn, B.D.2
  • 198
    • 0347579832 scopus 로고    scopus 로고
    • Light affects the accessibility of the thylakoid light harvesting complex II (LHCII) phosphorylation site to the membrane protein kinase(s)
    • H. Zer, M. Vink, S. Schochat, R.G. Herrmann, B. Andersson, and I. Ohad Light affects the accessibility of the thylakoid light harvesting complex II (LHCII) phosphorylation site to the membrane protein kinase(s) Biochemistry 42 2003 728 738
    • (2003) Biochemistry , vol.42 , pp. 728-738
    • Zer, H.1    Vink, M.2    Schochat, S.3    Herrmann, R.G.4    Andersson, B.5    Ohad, I.6
  • 199
    • 0030794462 scopus 로고    scopus 로고
    • Phosphorylation controls the three-dimensional structure of plant light-harvesting complex II
    • A. Nilsson, D. Stys, T. Drakenberg, M.D. Spangfort, S. Forsén, and J.F. Allen Phosphorylation controls the three-dimensional structure of plant light-harvesting complex II J. Biol. Chem. 272 1997 18350 18357
    • (1997) J. Biol. Chem. , vol.272 , pp. 18350-18357
    • Nilsson, A.1    Stys, D.2    Drakenberg, T.3    Spangfort, M.D.4    Forsén, S.5    Allen, J.F.6
  • 200
    • 0034735803 scopus 로고    scopus 로고
    • The PSI-H subunit of photosystem I is essential for state transitions in plant photosynthesis
    • C. Lunde, P.E. Jensen, A. Haldrup, J. Knoetzel, and H.V. Scheller 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
  • 201
    • 2642511507 scopus 로고    scopus 로고
    • The PSI-O subunit of plant photosystem I is involved in balancing the excitation pressure between the two photosystems
    • P.E. Jensen, A. Haldrup, S. Zhang, and H.V. Scheller The PSI-O subunit of plant photosystem I is involved in balancing the excitation pressure between the two photosystems J. Biol. Chem. 279 2004 24212 24217
    • (2004) J. Biol. Chem. , vol.279 , pp. 24212-24217
    • Jensen, P.E.1    Haldrup, A.2    Zhang, S.3    Scheller, H.V.4
  • 202
    • 0030045873 scopus 로고    scopus 로고
    • Changes in light energy distribution upon state transitions: An in vivo photoacoustic study of the wild type and photosynthetic mutants from Chlamydomonas reinhardtii
    • R. Delosme, J. Olive, and F.-A. Wollman Changes in light energy distribution upon state transitions: an in vivo photoacoustic study of the wild type and photosynthetic mutants from Chlamydomonas reinhardtii Biochim. Biophys. Acta 1273 1996 150 158
    • (1996) Biochim. Biophys. Acta , vol.1273 , pp. 150-158
    • Delosme, R.1    Olive, J.2    Wollman, F.-A.3
  • 203
    • 0942276401 scopus 로고    scopus 로고
    • Light-harvesting complex II binds to several small subunits of photosystem I
    • S. Zhang, and H.V. Scheller Light-harvesting complex II binds to several small subunits of photosystem I J. Biol. Chem. 279 2004 3180 3187
    • (2004) J. Biol. Chem. , vol.279 , pp. 3180-3187
    • Zhang, S.1    Scheller, H.V.2
  • 204
    • 0036208158 scopus 로고    scopus 로고
    • Involvement of state transitions in the switch between linear and cyclic electron flow in Chlamydomonas reinhardtii
    • G. Finazzi, F. Rappaport, A. Furia, M. Fleischmann, J.-D. Rochaix, F. Zito, and G. Forti Involvement of state transitions in the switch between linear and cyclic electron flow in Chlamydomonas reinhardtii EMBO Rep. 3 2002 280 285
    • (2002) EMBO Rep. , vol.3 , pp. 280-285
    • Finazzi, G.1    Rappaport, F.2    Furia, A.3    Fleischmann, M.4    Rochaix, J.-D.5    Zito, F.6    Forti, G.7
  • 205
    • 0026556851 scopus 로고
    • Protein phosphorylation in regulation of photosynthesis
    • J.F. Allen Protein phosphorylation in regulation of photosynthesis Biochim. Biophys. Acta 1098 1992 275 335
    • (1992) Biochim. Biophys. Acta , vol.1098 , pp. 275-335
    • Allen, J.F.1
  • 207
    • 85047685989 scopus 로고    scopus 로고
    • Assembly, function and dynamics of the photosynthetic machinery in Chlamydomonas reinhardtii
    • J.-D. Rochaix Assembly, function and dynamics of the photosynthetic machinery in Chlamydomonas reinhardtii Plant Physiol. 127 2001 1394 1398
    • (2001) Plant Physiol. , vol.127 , pp. 1394-1398
    • Rochaix, J.-D.1
  • 208
    • 0026547142 scopus 로고
    • Too much of a good thing: Light can be bad for photosynthesis
    • J. Barber, and B. Andersson Too much of a good thing: light can be bad for photosynthesis Trends Biochem. Sci. 17 1992 61 66
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 61-66
    • Barber, J.1    Andersson, B.2
  • 210
    • 3142546273 scopus 로고    scopus 로고
    • Toward an understanding of the mechanism of non-photochemical quenching in green plants
    • N.E. Holt, G.R. Fleming, and K.K. Niyogi Toward an understanding of the mechanism of non-photochemical quenching in green plants Biochemistry 43 2004 (in press)
    • (2004) Biochemistry , vol.43
    • Holt, N.E.1    Fleming, G.R.2    Niyogi, K.K.3
  • 211
    • 0001938338 scopus 로고    scopus 로고
    • The role of xanthophyll cycle carotenoids in the protection of photosynthesis
    • B. Demmig-Adams, and W.W. Adams III The role of xanthophyll cycle carotenoids in the protection of photosynthesis Trends Plant Sci. 1 1996 21 26
    • (1996) Trends Plant Sci. , vol.1 , pp. 21-26
    • Demmig-Adams, B.1    Adams III, W.W.2
  • 212
    • 2542444370 scopus 로고    scopus 로고
    • Regulation of photosynthetic light harvesting involves intrathylakoid lumen pH sensing by the PsbS protein
    • X.-P. Li, A.M. Gilmore, S. Caffari, R. Bassi, T. Golan, D. Kramer, and K.K. Niyogi Regulation of photosynthetic light harvesting involves intrathylakoid lumen pH sensing by the PsbS protein J. Biol. Chem. 279 2004 22866 22874
    • (2004) J. Biol. Chem. , vol.279 , pp. 22866-22874
    • Li, X.-P.1    Gilmore, A.M.2    Caffari, S.3    Bassi, R.4    Golan, T.5    Kramer, D.6    Niyogi, K.K.7
  • 214
    • 2942700872 scopus 로고    scopus 로고
    • Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity
    • D. Latowski, H.-E. Kerlund, and K. Strzalka Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity Biochemistry 43 2004 4417 4420
    • (2004) Biochemistry , vol.43 , pp. 4417-4420
    • Latowski, D.1    Kerlund, H.-E.2    Strzalka, K.3
  • 217
    • 0035876215 scopus 로고    scopus 로고
    • High-resolution AFM topographs of Rubrivax gelatinosus light-harvesting complex LH2
    • S. Scheuring, F. Reiss-Husson, A. Engel, J.-L. Rigaud, and J.-L. Ranck High-resolution AFM topographs of Rubrivax gelatinosus light-harvesting complex LH2 EMBO J. 20 2001 3029 3035
    • (2001) EMBO J. , vol.20 , pp. 3029-3035
    • Scheuring, S.1    Reiss-Husson, F.2    Engel, A.3    Rigaud, J.-L.4    Ranck, J.-L.5
  • 218
    • 0037452675 scopus 로고    scopus 로고
    • Nanodissection and high-resolution imaging of the Rhodopseudomonas viridis photosynthetic core complex in native membranes by AFM
    • S. Scheuring, J. Seguin, S. Marco, D. Levy, B. Robert, and J.-L. Rigaud Nanodissection and high-resolution imaging of the Rhodopseudomonas viridis photosynthetic core complex in native membranes by AFM Proc. Natl. Acad. Sci. U. S. A. 100 2003 1690 1693
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 1690-1693
    • Scheuring, S.1    Seguin, J.2    Marco, S.3    Levy, D.4    Robert, B.5    Rigaud, J.-L.6
  • 220
    • 2442503725 scopus 로고    scopus 로고
    • Simultaneous atomic-force and two-photon fluorescence imaging of biological membranes
    • C.C. Gradinaru, P. Martinsson, T.J. Aartsma, and T. Schmidt Simultaneous atomic-force and two-photon fluorescence imaging of biological membranes Ultramicroscopy 99 2004 235 245
    • (2004) Ultramicroscopy , vol.99 , pp. 235-245
    • Gradinaru, C.C.1    Martinsson, P.2    Aartsma, T.J.3    Schmidt, T.4
  • 222
    • 84910705655 scopus 로고
    • J. Amesz Elsevier Science Publishers Amsterdam
    • J.M. Anderson J. Amesz Photosynthesis 1987 Elsevier Science Publishers Amsterdam
    • (1987) Photosynthesis
    • Anderson, J.M.1
  • 223
    • 0025636354 scopus 로고
    • Ultrastructure of spinach chloroplasts as revealed by freeze substitution
    • C. Weibull, W. Villiger, and B. Bohrmann Ultrastructure of spinach chloroplasts as revealed by freeze substitution J. Ultrastruct. Res. 104 1990 139 143
    • (1990) J. Ultrastruct. Res. , vol.104 , pp. 139-143
    • Weibull, C.1    Villiger, W.2    Bohrmann, B.3
  • 225
    • 0002068362 scopus 로고
    • Freeze-fracture studies on barley plastid membranes: 3. Location of the light-harvesting chlorophyll protein
    • D.J. Simpson Freeze-fracture studies on barley plastid membranes: 3. Location of the light-harvesting chlorophyll protein Carlsberg Res. Commun. 44 1979 305 336
    • (1979) Carlsberg Res. Commun. , vol.44 , pp. 305-336
    • Simpson, D.J.1
  • 226
    • 0017572514 scopus 로고
    • Chloroplast membrane organization at the supramolecular level and its functional implication
    • L.A. Staehelin, P.A. Armond, and K.R. Miller Chloroplast membrane organization at the supramolecular level and its functional implication Brookhaven Symp. Biol. 28 1977 278 315
    • (1977) Brookhaven Symp. Biol. , vol.28 , pp. 278-315
    • Staehelin, L.A.1    Armond, P.A.2    Miller, K.R.3
  • 227
    • 0001478297 scopus 로고
    • Structural and functional organization of the thylakoid membrane system in photosynthetic apparatus
    • S. Murakami Structural and functional organization of the thylakoid membrane system in photosynthetic apparatus J. Electron Microsc. 41 1992 424 433
    • (1992) J. Electron Microsc. , vol.41 , pp. 424-433
    • Murakami, S.1
  • 228
    • 0025879324 scopus 로고
    • Structural organization of the thylakoid membrane-freeze-fracture and immunocytochemical analysis
    • J. Olive, and O. Vallon Structural organization of the thylakoid membrane-freeze-fracture and immunocytochemical analysis J. Electron Microsc. Tech. 18 1991 360 374
    • (1991) J. Electron Microsc. Tech. , vol.18 , pp. 360-374
    • Olive, J.1    Vallon, O.2
  • 229
    • 0015590205 scopus 로고
    • Chloroplast organization and the ultrastructural localization of photosystem I and II
    • I. Nir, and D.C. Pease Chloroplast organization and the ultrastructural localization of photosystem I and II J. Ultrastruct. Res. 42 1973 534 550
    • (1973) J. Ultrastruct. Res. , vol.42 , pp. 534-550
    • Nir, I.1    Pease, D.C.2
  • 230
    • 0014119249 scopus 로고
    • Subunits in chloroplast lamellae
    • D. Branton, and R.B. Park Subunits in chloroplast lamellae J. Ultrastruct. Res. 19 1967 283 303
    • (1967) J. Ultrastruct. Res. , vol.19 , pp. 283-303
    • Branton, D.1    Park, R.B.2
  • 231
    • 0014306176 scopus 로고
    • Lipid fixation during preparation of chloroplasts for electron microscopy
    • A. Ongun, W.W. Thomson, and J.B. Mudd Lipid fixation during preparation of chloroplasts for electron microscopy J. Lipid Res. 9 1968 416 424
    • (1968) J. Lipid Res. , vol.9 , pp. 416-424
    • Ongun, A.1    Thomson, W.W.2    Mudd, J.B.3
  • 232
    • 0037040876 scopus 로고    scopus 로고
    • Activation of zeaxanthin is an obligatory event in the regulation of photosynthetic light harvesting
    • A.V. Ruban, A.A. Pascal, B. Robert, and P. Horton Activation of zeaxanthin is an obligatory event in the regulation of photosynthetic light harvesting J. Biol. Chem. 277 2002 7785 7789
    • (2002) J. Biol. Chem. , vol.277 , pp. 7785-7789
    • Ruban, A.V.1    Pascal, A.A.2    Robert, B.3    Horton, P.4
  • 233
    • 0015094357 scopus 로고
    • Structure of the photosynthetic apparatus in protein-embedded chloroplasts
    • G.L. Nicolson Structure of the photosynthetic apparatus in protein-embedded chloroplasts J. Cell Biol. 50 1971 258 263
    • (1971) J. Cell Biol. , vol.50 , pp. 258-263
    • Nicolson, G.L.1
  • 234
    • 0017111528 scopus 로고
    • Membranes as observed in frozen sections
    • K.T. Tokuyasu Membranes as observed in frozen sections J. Ultrastruct. Res. 55 1976 281 287
    • (1976) J. Ultrastruct. Res. , vol.55 , pp. 281-287
    • Tokuyasu, K.T.1
  • 235
    • 0033377344 scopus 로고    scopus 로고
    • A model for the topology of the chloroplast thylakoid membrane
    • P.O. Arvidsson, and C. Sundby A model for the topology of the chloroplast thylakoid membrane Aust. J. Plant Physiol. 26 1999 678 694
    • (1999) Aust. J. Plant Physiol. , vol.26 , pp. 678-694
    • Arvidsson, P.O.1    Sundby, C.2


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