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Volumn 1837, Issue 9, 2014, Pages 1454-1462

Proteomic characterization and three-dimensional electron microscopy study of PSII-LHCII supercomplexes from higher plants

Author keywords

Proteomics; PSII LHCII supercomplex; Single particle analysis; Structure; Thylakoids; Transmission electron microscopy

Indexed keywords

AMINO ACID; COMPLEMENT; LHCB3 PROTEIN; LHCB6 PROTEIN; MEMBRANE PROTEIN; POLYPEPTIDE; PROTEIN; UNCLASSIFIED DRUG;

EID: 84906306160     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2013.11.004     Document Type: Article
Times cited : (35)

References (52)
  • 1
    • 84887486678 scopus 로고    scopus 로고
    • Structural, functional and auxiliary proteins of photosystem II
    • C. Pagliano, G. Saracco, and J. Barber Structural, functional and auxiliary proteins of photosystem II Photosynth. Res. 116 2013 167 188
    • (2013) Photosynth. Res. , vol.116 , pp. 167-188
    • Pagliano, C.1    Saracco, G.2    Barber, J.3
  • 2
    • 0032548142 scopus 로고    scopus 로고
    • Three-dimensional structure of the plant photosystem II reaction centre at 8 A resolution
    • DOI 10.1038/24421
    • K.-H. Rhee, E.P. Morris, J. Barber, and W. Kühlbrandt Three-dimensional structure of the plant photosystem II reaction centre at 8 Å resolution Nature 396 1998 283 286 (Pubitemid 28541395)
    • (1998) Nature , vol.396 , Issue.6708 , pp. 283-286
    • Rhee, K.-H.1    Morris, E.P.2    Barber, J.3    Kuhlbrandt, W.4
  • 3
    • 0035783236 scopus 로고    scopus 로고
    • Three-dimensional structure of the photosystem II core dimer of higher plants determined by electron microscopy
    • B. Hankamer, E.P. Morris, J. Nield, C. Gerle, and J. Barber Three-dimensional structure of the photosystem II core dimer of higher plants determined by electron microscopy J. Struct. Biol. 135 2001 262 269
    • (2001) J. Struct. Biol. , vol.135 , pp. 262-269
    • Hankamer, B.1    Morris, E.P.2    Nield, J.3    Gerle, C.4    Barber, J.5
  • 4
    • 2442543556 scopus 로고    scopus 로고
    • Crystal structure of the PsbP protein of photosystem II from Nicotiana tabacum
    • DOI 10.1038/sj.embor.7400113
    • K. Ifuku, T. Nakatsu, H. Kato, and F. Sato Crystal structure of the PsbP protein of photosystem II from Nicotiana tabacum EMBO Rep. 5 2004 362 367 (Pubitemid 38618277)
    • (2004) EMBO Reports , vol.5 , Issue.4 , pp. 362-367
    • Ifuku, K.1    Nakatsu, T.2    Kato, H.3    Sato, F.4
  • 6
    • 21744439800 scopus 로고    scopus 로고
    • The 1.49 A resolution crystal structure of PsbQ from photosystem II of Spinacia oleracea reveals a PPII structure in the N-terminal region
    • DOI 10.1016/j.jmb.2005.05.044, PII S0022283605005991
    • M. Balsera, J.B. Arellano, J.L. Revuelta, J. De Las Rivas, and J.A. Hermoso The 1.49 Å resolution crystal structure of PsbQ from photosystem II of Spinacia oleracea reveals a PPII structure in the N-terminal region J. Mol. Biol. 350 2005 1051 1060 (Pubitemid 40943461)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.5 , pp. 1051-1060
    • Balsera, M.1    Arellano, J.B.2    Revuelta, J.L.3    De Las Rivas, J.4    Hermoso, J.A.5
  • 7
    • 0028058268 scopus 로고
    • The light-harvesting chlorophyll a/b-binding proteins
    • DOI 10.1016/0005-2728(94)90148-1
    • S. Jansson The light-harvesting chlorophyll a/b binding proteins Biochim. Biophys. Acta 1184 1994 1 19 (Pubitemid 24048853)
    • (1994) Biochimica et Biophysica Acta - Bioenergetics , vol.1184 , Issue.1 , pp. 1-19
    • Jansson, S.1
  • 8
    • 0035795160 scopus 로고    scopus 로고
    • Identification of Lhcb1/Lhcb2/Lhcb3 heterotrimers of the main light-harvesting chlorophyll a/b-protein complex of Photosystem II (LHC II)
    • DOI 10.1016/S0005-2728(00)00262-0, PII S0005272800002620
    • G. Jackowski, K. Kacprzak, and S. Jansson Identification of Lhcb1/Lhcb2/Lhcb3 heterotrimers of the main light-harvesting chlorophyll a/b-protein complex of photosystem II (LHCII) Biochim. Biophys. Acta 1504 2001 340 345 (Pubitemid 32201905)
    • (2001) Biochimica et Biophysica Acta - Bioenergetics , vol.1504 , Issue.2-3 , pp. 340-345
    • Jackowski, G.1    Kacprzak, K.2    Jansson, S.3
  • 9
    • 3242665135 scopus 로고    scopus 로고
    • A look within LHCII: Differential analysis of the Lhcb1-3 complexes building the major trimeric antenna complex of higher-plant photosynthesis
    • DOI 10.1021/bi036265i
    • S. Caffarri, R. Croce, L. Cattivelli, and R. Bassi A look within LHCII: differential analysis of the Lhcb1-3 complexes building the major trimeric antenna complex of higher-plant photosynthesis Biochemistry 43 2004 9467 9476 (Pubitemid 38955479)
    • (2004) Biochemistry , vol.43 , Issue.29 , pp. 9467-9476
    • Caffarri, S.1    Croce, R.2    Cattivelli, L.3    Bassi, R.4
  • 11
    • 16344363252 scopus 로고    scopus 로고
    • Mechanisms of photoprotection and nonphotochemical quenching in pea light harvesting complex at 2.5 Å resolution
    • J. Standfuss, A.C.T. van Scheltinga, M. Lamborghini, and W. Kühlbrandt Mechanisms of photoprotection and nonphotochemical quenching in pea light harvesting complex at 2.5 Å resolution EMBO J. 24 2005 918 928
    • (2005) EMBO J. , vol.24 , pp. 918-928
    • Standfuss, J.1    Van Scheltinga, A.C.T.2    Lamborghini, M.3    Kühlbrandt, W.4
  • 13
    • 11044234285 scopus 로고    scopus 로고
    • Supramolecular organization of thylakoid membrane proteins in green plants
    • DOI 10.1016/j.bbabio.2004.09.009, PII S0005272804002749
    • J.P. Dekker, and E.J. Boekema Supramolecular organization of thylakoid membrane proteins in green plants Biochim. Biophys. Acta 1706 2005 12 39 (Pubitemid 40044704)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1706 , Issue.1-2 , pp. 12-39
    • Dekker, J.P.1    Boekema, E.J.2
  • 15
    • 70350565366 scopus 로고    scopus 로고
    • Functional architecture of higher plant photosystem II supercomplexes
    • S. Caffarri, R. Kouřil, S. Kereïche, E.J. Boekema, and R. Croce Functional architecture of higher plant photosystem II supercomplexes EMBO J. 28 2009 3052 3063
    • (2009) EMBO J. , vol.28 , pp. 3052-3063
    • Caffarri, S.1    Kouřil, R.2    Kereïche, S.3    Boekema, E.J.4    Croce, R.5
  • 16
    • 0039848607 scopus 로고    scopus 로고
    • Multiple types of association of photosystem II and its light-harvesting antenna in partially solubilized photosystem II membranes
    • DOI 10.1021/bi9827161
    • 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 (Pubitemid 29102782)
    • (1999) Biochemistry , vol.38 , Issue.8 , pp. 2233-2239
    • Boekema, E.J.1    Van Roon, H.2    Calkoen, F.3    Bassi, R.4    Dekker, J.P.5
  • 17
    • 84869219071 scopus 로고    scopus 로고
    • Characterization of PSII-LHCII supercomplexes isolated from pea thylakoid membrane by one-step treatment with α- And β-dodecyl-D-maltoside
    • S. Barera, C. Pagliano, T. Pape, G. Saracco, and J. Barber Characterization of PSII-LHCII supercomplexes isolated from pea thylakoid membrane by one-step treatment with α- and β-dodecyl-D-maltoside Phil. Trans. R. Soc. B 67 2012 3389 3399
    • (2012) Phil. Trans. R. Soc. B , vol.67 , pp. 3389-3399
    • Barera, S.1    Pagliano, C.2    Pape, T.3    Saracco, G.4    Barber, J.5
  • 18
    • 0033989509 scopus 로고    scopus 로고
    • 3D map of the plant photosystem II supercomplex obtained by cryoelectron microscopy and single particle analysis
    • DOI 10.1038/71242
    • J. Nield, E.V. Orlova, E.P. Morris, B. Gowen, M. van Heel, and J. Barber 3D map of the plant photosystem two supercomplex obtained by cryoelectron microscopy and single particle analysis Nat. Struct. Biol. 7 2000 44 47 (Pubitemid 30043247)
    • (2000) Nature Structural Biology , vol.7 , Issue.1 , pp. 44-47
    • Nield, J.1    Orlova, E.V.2    Morris, E.P.3    Gowen, B.4    Van Heel, M.5    Barber, J.6
  • 19
    • 0037177852 scopus 로고    scopus 로고
    • Three-dimensional electron cryo-microscopy study of the extrinsic domains of the oxygen-evolving complex of spinach. Assignment of the PsbO protein
    • DOI 10.1074/jbc.M110549200
    • J. Nield, M. Balsera, J. De Las Rivas, and J. Barber Three-dimensional electron cryo-microscopy study of the extrinsic domains of the oxygen-evolving complex of spinach: assignment of the PsbO protein J. Biol. Chem. 277 2002 15006 15012 (Pubitemid 34952576)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.17 , pp. 15006-15012
    • Nield, J.1    Balsera, M.2    De Rivas, J.L.3    Barber, J.4
  • 20
    • 33745585779 scopus 로고    scopus 로고
    • Refinement of the structural model for the Photosystem II supercomplex of higher plants
    • DOI 10.1016/j.bbabio.2006.03.019, PII S0005272806000740
    • J. Nield, and J. Barber Refinement of the structural model for the photosystem II supercomplex of higher plants Biochim. Biophys. Acta 1757 2006 353 361 (Pubitemid 43993853)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.5-6 , pp. 353-361
    • Nield, J.1    Barber, J.2
  • 22
    • 84862221877 scopus 로고    scopus 로고
    • Comparison of the α and β isomeric forms of the detergent n-dodecyl-D-maltoside for solubilizing photosynthetic complexes from pea thylakoid membranes
    • C. Pagliano, S. Barera, F. Chimirri, G. Saracco, and J. Barber Comparison of the α and β isomeric forms of the detergent n-dodecyl-D-maltoside for solubilizing photosynthetic complexes from pea thylakoid membranes Biochim. Biophys. Acta 1817 2012 1506 1515
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1506-1515
    • Pagliano, C.1    Barera, S.2    Chimirri, F.3    Saracco, G.4    Barber, J.5
  • 23
    • 0001844190 scopus 로고
    • Copper enzymes in isolated chloroplasts, polyphenoloxidase in Beta vulgaris
    • D.J. Arnon Copper enzymes in isolated chloroplasts, polyphenoloxidase in Beta vulgaris Plant Physiol. 24 1949 1 14
    • (1949) Plant Physiol. , vol.24 , pp. 1-14
    • Arnon, D.J.1
  • 24
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • H. Schagger, and G. von Jagow Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form Anal. Biochem. 199 1991 223 231
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schagger, H.1    Von Jagow, G.2
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0035030294 scopus 로고    scopus 로고
    • An improved sodium dodecyl sulfate-polyacrylamide gel electrophoresis system for the analysis of membrane protein complexes
    • DOI 10.1002/1522-2683 22:6<1004::AID-ELPS1004>3.0.CO;2-Y
    • Y. Kashino, H. Koike, and K. Satoh An improved sodium dodecyl sulfate-polyacrylamide gel electrophoresis system for the analysis of membrane protein complexes Electrophoresis 22 2001 1004 1007 (Pubitemid 32409365)
    • (2001) Electrophoresis , vol.22 , Issue.6 , pp. 1004-1007
    • Kashino, Y.1    Koike, H.2    Satoh, K.3
  • 27
    • 0028983813 scopus 로고
    • Improvement of an "in-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing
    • U. Hellmann, C. Wernstedt, J. Gonez, and C.H. Heldin Improvement of an "In-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing Anal. Biochem. 224 1995 451 455
    • (1995) Anal. Biochem. , vol.224 , pp. 451-455
    • Hellmann, U.1    Wernstedt, C.2    Gonez, J.3    Heldin, C.H.4
  • 28
    • 79958765107 scopus 로고    scopus 로고
    • One-step isolation and biochemical characterization of a highly active plant PSII monomeric core
    • C. Pagliano, F. Chimirri, G. Saracco, F. Marsano, and J. Barber One-step isolation and biochemical characterization of a highly active plant PSII monomeric core Photosynth. Res. 108 2011 33 46
    • (2011) Photosynth. Res. , vol.108 , pp. 33-46
    • Pagliano, C.1    Chimirri, F.2    Saracco, G.3    Marsano, F.4    Barber, J.5
  • 29
    • 0035326344 scopus 로고    scopus 로고
    • Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching
    • DOI 10.1021/ac0013709
    • A. Shevchenko, S. Sunyaev, A. Loboba, A. Shevchenko, P. Bork, W. Ens, and K.G. Standing Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of flight mass spectrometry and BLAST homology searching Anal. Chem. 73 2001 1917 1926 (Pubitemid 32862395)
    • (2001) Analytical Chemistry , vol.73 , Issue.9 , pp. 1917-1926
    • Shevchenko, A.1    Sunyaev, S.2    Loboda, A.3    Shevchenko, A.4    Bork, P.5    Ens, W.6    Standing, K.G.7
  • 30
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • DOI 10.1016/j.jsb.2006.05.009, PII S1047847706001894, Software Tools for Macromolecular Microscopy
    • G. Tang, L. Peng, P.R. Baldwin, D.S. Mann, W. Jiang, I. Rees, and S.J. Ludtke EMAN2: an extensible image processing suite for electron microscopy J. Struct. Biol. 157 2007 38 46 (Pubitemid 44880785)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5    Rees, I.6    Ludtke, S.J.7
  • 32
    • 0027418576 scopus 로고
    • The portal protein of bacteriophage SPP1: A DNA pump with 13-fold symmetry
    • P. Dube, P. Tavares, R. Lurz, and M. van Heel The portal protein of bacteriophage SPP1: a DNA pump with 13-fold symmetry EMBO J. 12 1993 1303 1309 (Pubitemid 23112785)
    • (1993) EMBO Journal , vol.12 , Issue.4 , pp. 1303-1309
    • Dube, P.1    Tavares, P.2    Lurz, R.3    Van Heel, M.4
  • 33
    • 0023102907 scopus 로고
    • Angular reconstitution: A posteriori assignment of projection directions for 3D reconstruction
    • DOI 10.1016/0304-3991(87)90078-7
    • M. Van Heel Angular reconstitution: a posteriori assignment of projection directions for 3D reconstruction Ultramicroscopy 21 1987 111 123 (Pubitemid 17018207)
    • (1987) Ultramicroscopy , vol.21 , Issue.2 , pp. 111-123
    • Van Heel, M.1
  • 34
    • 0001339881 scopus 로고
    • Three-dimensional reconstruction of single particles from random and nonrandom tilt series
    • M. Radermacher Three-dimensional reconstruction of single particles from random and nonrandom tilt series J. Electron. Microsc. Tech. 9 1988 359 394
    • (1988) J. Electron. Microsc. Tech. , vol.9 , pp. 359-394
    • Radermacher, M.1
  • 35
    • 25144494651 scopus 로고    scopus 로고
    • Fourier shell correlation threshold criteria
    • DOI 10.1016/j.jsb.2005.05.009, PII S1047847705001292
    • M. van Heel, and M. Schatz Fourier shell correlation threshold criteria J. Struct. Biol. 151 2005 250 262 (Pubitemid 41338732)
    • (2005) Journal of Structural Biology , vol.151 , Issue.3 , pp. 250-262
    • Van Heel, M.1    Schatz, M.2
  • 37
    • 1642331709 scopus 로고    scopus 로고
    • Architecture of the photosynthetic oxygen-evolving center
    • DOI 10.1126/science.1093087
    • K.N. Ferreira, T.M. Iverson, K. Maghlaoui, J. Barber, and S. Iwata Architecture of the photosynthetic oxygen-evolving center Science 303 2004 1831 1838 (Pubitemid 38374869)
    • (2004) Science , vol.303 , Issue.5665 , pp. 1831-1838
    • Ferreira, K.N.1    Iverson, T.M.2    Maghlaoui, K.3    Barber, J.4    Iwata, S.5
  • 38
    • 4043080672 scopus 로고    scopus 로고
    • Analysis of the structure of the PsbO protein and its implications
    • DOI 10.1023/B:PRES.0000036889.44048.e4
    • J. De Las Rivas, and J. Barber Analysis of the structure of the PsbO protein and its implications Photosynth. Res. 81 2004 329 343 (Pubitemid 39059693)
    • (2004) Photosynthesis Research , vol.81 , Issue.3 , pp. 329-343
    • De Las Rivas, J.1    Barber, J.2
  • 39
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å
    • Y. Umena, K. Kawakami, J.R. Shen, and N. Kamiya Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å Nature 473 2011 55 60
    • (2011) Nature , vol.473 , pp. 55-60
    • Umena, Y.1    Kawakami, K.2    Shen, J.R.3    Kamiya, N.4
  • 40
    • 0000229460 scopus 로고
    • Close association of the 33-kDa extrinsic protein with the apoprotein of Cpa1 in photosystem II
    • T.M. Bricker, W.R. Odom, and C.B. Queirolo Close association of the 33-kDa extrinsic protein with the apoprotein of Cpa1 in photosystem II FEBS Lett. 231 1988 111 117
    • (1988) FEBS Lett. , vol.231 , pp. 111-117
    • Bricker, T.M.1    Odom, W.R.2    Queirolo, C.B.3
  • 41
    • 0002300895 scopus 로고
    • Nearest neighbor relationships among constituent proteins of oxygen-evolving photosystem II membranes - Binding and function of the extrinsic 33 kDa protein
    • I. Enami, T. Miyaoka, Y. Mochizuki, J.R. Shen, K. Satoh, and S. Katoh Nearest neighbor relationships among constituent proteins of oxygen-evolving photosystem II membranes - binding and function of the extrinsic 33 kDa protein Biochim. Biophys. Acta 973 1989 35 40
    • (1989) Biochim. Biophys. Acta , vol.973 , pp. 35-40
    • Enami, I.1    Miyaoka, T.2    Mochizuki, Y.3    Shen, J.R.4    Satoh, K.5    Katoh, S.6
  • 42
    • 0030128825 scopus 로고    scopus 로고
    • On the role of the N-terminus of the extrinsic 33 kDa protein of Photosystem II
    • A. Seidler, A.W. Rutherford, and H. Michel On the role of the N-terminus of the extrinsic 33 kDa protein of photosystem II Plant Mol. Biol. 31 1996 183 188 (Pubitemid 26320410)
    • (1996) Plant Molecular Biology , vol.31 , Issue.1 , pp. 183-188
    • Seidler, A.1    Rutherford, A.W.2    Michel, H.3
  • 43
    • 79958002353 scopus 로고    scopus 로고
    • Molecular functions of PsbP and PsbQ proteins in the photosystem II supercomplex
    • K. Ifuku, K. Ido, and F. Sato Molecular functions of PsbP and PsbQ proteins in the photosystem II supercomplex J. Photochem. Photobiol. B 104 2011 158 164
    • (2011) J. Photochem. Photobiol. B , vol.104 , pp. 158-164
    • Ifuku, K.1    Ido, K.2    Sato, F.3
  • 45
    • 0343851071 scopus 로고    scopus 로고
    • A pigment-binding protein essential for regulation of photosynthetic light harvesting
    • DOI 10.1038/35000131
    • X.P. Li, O. Björkman, C. Shih, A.R. Grossman, M. Rosenquist, S. Jansson, and K.K. Niyogi A pigment-binding protein essential for regulation of photosynthetic light harvesting Nature 403 2000 391 395 (Pubitemid 30073080)
    • (2000) Nature , vol.403 , Issue.6768 , pp. 391-395
    • Li, X.-P.1    Bjorkman, O.2    Shih, C.3    Grossman, A.R.4    Rosenquist, M.5    Jansson, S.6    Niyogi, K.K.7
  • 46
    • 77649273780 scopus 로고    scopus 로고
    • The PsbS protein controls the macro-organisation of photosystem II complexes in the grana membranes of higher plant chloroplasts
    • S. Kereïche, A.Z. Kiss, R. Kouřil, E.J. Boekema, and P. Horton The PsbS protein controls the macro-organisation of photosystem II complexes in the grana membranes of higher plant chloroplasts FEBS Lett. 584 2010 759 764
    • (2010) FEBS Lett. , vol.584 , pp. 759-764
    • Kereïche, S.1    Kiss, A.Z.2    Kouřil, R.3    Boekema, E.J.4    Horton, P.5
  • 47
    • 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 Phil. Trans. R. Soc. B 355 2000 1337 1344
    • (2000) Phil. Trans. R. Soc. B , vol.355 , pp. 1337-1344
    • Nield, J.1    Funk, C.2    Barber, J.3
  • 48
    • 0031041452 scopus 로고    scopus 로고
    • Characterization of the low molecular weight photosystem II reaction center subunits and their light-induced modifications by mass spectrometry
    • DOI 10.1074/jbc.272.7.3935
    • J. Sharma, M. Panico, J. Barber, and H.R. Morris Characterization of the low molecular weight photosystem II reaction center subunits and their light-induced modifications by mass spectrometry J. Biol. Chem. 272 1997 3935 3943 (Pubitemid 27078451)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.7 , pp. 3935-3943
    • Sharma, J.1    Panico, M.2    Barber, J.3    Morris, H.R.4
  • 49
    • 0032568955 scopus 로고    scopus 로고
    • Isolation and characterization of monomeric and dimeric CP47-reaction center photosystem II complexes
    • DOI 10.1074/jbc.273.26.16122
    • 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 (Pubitemid 28311382)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.26 , pp. 16122-16127
    • Zheleva, D.1    Sharma, J.2    Panico, M.3    Morris, H.R.4    Barber, J.5
  • 50
    • 60549116192 scopus 로고    scopus 로고
    • Mass spectrometric characterization of membrane integral low molecular weight proteins from photosystem II in barley etioplasts
    • M. Plöscher, B. Granvogl, M. Zoryan, V. Reisinger, and L.A. Eichacker Mass spectrometric characterization of membrane integral low molecular weight proteins from photosystem II in barley etioplasts Proteomics 9 2009 625 635
    • (2009) Proteomics , vol.9 , pp. 625-635
    • Plöscher, M.1    Granvogl, B.2    Zoryan, M.3    Reisinger, V.4    Eichacker, L.A.5
  • 51
    • 0026541431 scopus 로고
    • A supramolecular light-harvesting complex from chloroplast photosystem-II membranes
    • P. Dainese, and R. Bassi 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
    • Dainese, P.1    Bassi, R.2


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