메뉴 건너뛰기




Volumn 52, Issue 9, 2011, Pages 1560-1568

Structure of the chloroplast NADH dehydrogenase-like complex: Nomenclature for nuclear-encoded subunits

Author keywords

Arabidopsis; Cyclic electron transport; Maize; NADH dehydrogenase (EC 1.6.99.3) like complex

Indexed keywords

FERREDOXIN; MULTIENZYME COMPLEX; PLASTOQUINONE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; SULFIDE QUINONE REDUCTASE;

EID: 80052879596     PISSN: 00320781     EISSN: 14719053     Source Type: Journal    
DOI: 10.1093/pcp/pcr098     Document Type: Review
Times cited : (155)

References (67)
  • 1
    • 33750514379 scopus 로고    scopus 로고
    • Structural characterization of NDH-1 complexes of Thermosynechococcus elongatus by single particle electron microscopy
    • DOI 10.1016/j.bbabio.2006.05.042, PII S0005272806001769
    • Arteni, A.A., Zhang, P., Battchikova, N., Ogawa, T., Aro, E.-M. and Boekema, E.J. (2006) Structural characterization of NDH-1 complexes of Thermosynechococcus elongatus by single particle electron microscopy. Biochim. Biophys. Acta 1757: 1469-1475. (Pubitemid 44666665)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.11 , pp. 1469-1475
    • Arteni, A.A.1    Zhang, P.2    Battchikova, N.3    Ogawa, T.4    Aro, E.-M.5    Boekema, E.J.6
  • 2
    • 79958120495 scopus 로고
    • Cyanobacterial NDH-1 complexes: Novel insights and remaining puzzles
    • Battchikova, N., Eisenhut, M. and Aro, E.-M. (2011) Cyanobacterial NDH-1 complexes: novel insights and remaining puzzles. Biochim. Biophys. Acta 1807: 935-944.
    • (1807) Biochim. Biophys. Acta , pp. 935-944
    • Battchikova, N.1    Eisenhut, M.2    Aro, E.-M.3
  • 3
    • 13244281728 scopus 로고    scopus 로고
    • Identification of NdHL and Ssl1690 (NdhO) in NDH-1L and NDH-1M complexes of Synechocystis sp. PCC 6803
    • DOI 10.1074/jbc.M410914200
    • Battchikova, N., Zhang, P., Rudd, S., Ogawa, T. and Aro, E.-M. (2005) Identification of NdhL and Ssl1690 (NdhO) in NDH-1L and NDH-1M complexes of Synechocystis sp. PCC 6803. J. Biol. Chem. 280: 2587-2595. (Pubitemid 40189361)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.4 , pp. 2587-2595
    • Battchikova, N.1    Zhang, P.2    Rudd, S.3    Ogawa, T.4    Aro, E.-M.5
  • 4
    • 77954761012 scopus 로고    scopus 로고
    • Possibilities of subunit localization with fluorescent protein tags and electron microscopy examplified by a cyanobacterial NDH-1 study
    • Birungi, M., Folea, M., Battchikova, N., Xu, M., Mi, H., Ogawa, T. et al. (2010) Possibilities of subunit localization with fluorescent protein tags and electron microscopy examplified by a cyanobacterial NDH-1 study. Biochim. Biophys. Acta 1797: 1681-6168.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1681-6168
    • Birungi, M.1    Folea, M.2    Battchikova, N.3    Xu, M.4    Mi, H.5    Ogawa, T.6
  • 5
    • 0032481317 scopus 로고    scopus 로고
    • Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes
    • DOI 10.1093/emboj/17.4.868
    • Burrows, P.A., Sazanov, L.A., Svab, Z., Maliga, P. and Nixon, P.J. (1998) Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes. EMBO J. 17: 868-876. (Pubitemid 28077641)
    • (1998) EMBO Journal , vol.17 , Issue.4 , pp. 868-876
    • Burrows, P.A.1    Sazanov, L.A.2    Svab, Z.3    Maliga, P.4    Nixon, P.J.5
  • 6
    • 38749133045 scopus 로고    scopus 로고
    • A Complex Containing PGRL1 and PGR5 Is Involved in the Switch between Linear and Cyclic Electron Flow in Arabidopsis
    • DOI 10.1016/j.cell.2007.12.028, PII S0092867408000457
    • DalCorso, G., Pesaresi, P., Masiero, S., Aseeva, E., Schuenemann, D., Finazzi, G. et al. (2008) A complex containing PGRL1 and PGR5 is involved in the switch between linear and cyclic electron flow in Arabidopsis. Cell 132: 273-285. (Pubitemid 351181233)
    • (2008) Cell , vol.132 , Issue.2 , pp. 273-285
    • DalCorso, G.1    Pesaresi, P.2    Masiero, S.3    Aseeva, E.4    Schunemann, D.5    Finazzi, G.6    Joliot, P.7    Barbato, R.8    Leister, D.9
  • 7
    • 77952979824 scopus 로고    scopus 로고
    • The architecture of respiratory complex i
    • Efremov, R.G., Baradaran, R. and Sazanov, L.A. (2010) The architecture of respiratory complex I. Nature 465: 441-445.
    • (2010) Nature , vol.465 , pp. 441-445
    • Efremov, R.G.1    Baradaran, R.2    Sazanov, L.A.3
  • 8
    • 44949215814 scopus 로고    scopus 로고
    • Chloroplastic NAD(P)H dehydrogenase complex and cyclic electron transport around photosystem I
    • Endo, T., Ishida, S., Ishikawa, N. and Sato, F. (2008) Chloroplastic NAD(P)H dehydrogenase complex and cyclic electron transport around photosystem I. Mol. Cells 25: 158-162. (Pubitemid 351818990)
    • (2008) Molecules and Cells , vol.25 , Issue.2 , pp. 158-162
    • Endo, T.1    Ishida, S.2    Ishikawa, N.3    Sato, F.4
  • 9
    • 0000229336 scopus 로고    scopus 로고
    • Donation of electrons to plastoquinone by NAD(P)H dehydrogenase and by ferredoxin-quinone reductase in spinach chloroplasts
    • Endo, T., Mi, H., Shikanai, T. and Asada, K. (1997) Donation of electrons to plastoquinone by NAD(P)H dehydrogenase and by ferredoxin-quinone reductase in spinach chloroplasts. Plant Cell Physiol. 38: 1272-1277. (Pubitemid 127493256)
    • (1997) Plant and Cell Physiology , vol.38 , Issue.11 , pp. 1272-1277
    • Endo, T.1    Mi, H.2    Shikanai, T.3    Asada, K.4
  • 10
    • 0032790755 scopus 로고    scopus 로고
    • The role of chloroplastic NAD(P)H dehydrogenase in photoprotection
    • DOI 10.1016/S0014-5793(99)00989-8, PII S0014579399009898
    • Endo, T., Shikanai, T., Takabayashi, A., Asada, K. and Sato, F. (1999) The role of chloroplastic NAD(P)H dehydrogenase in photoprotection. FEBS Lett. 457: 5-8. (Pubitemid 29387398)
    • (1999) FEBS Letters , vol.457 , Issue.1 , pp. 5-8
    • Endo, T.1    Shikanai, T.2    Takabayashi, A.3    Asada, K.4    Sato, F.5
  • 11
    • 0032490117 scopus 로고    scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli
    • DOI 10.1016/S0005-2728(98)00024-3, PII S0005272898000243
    • Friedrich, T. (1998) The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochim. Biophys. Acta 1364: 134-146. (Pubitemid 28291836)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1364 , Issue.2 , pp. 134-146
    • Friedrich, T.1
  • 12
    • 0034637432 scopus 로고    scopus 로고
    • The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases
    • DOI 10.1016/S0014-5793(00)01867-6, PII S0014579300018676
    • Friedrich, T. and Scheide, D. (2000) The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases. FEBS Lett. 479: 1-5. (Pubitemid 30625247)
    • (2000) FEBS Letters , vol.479 , Issue.1-2 , pp. 1-5
    • Friedrich, T.1    Scheide, D.2
  • 13
    • 0030295294 scopus 로고    scopus 로고
    • The NADH-binding subunit of respiratory chain complex I is nuclear-encoded in plants and identified only in mitochondria
    • DOI 10.1046/j.1365-313X.1996.10050793.x
    • Grohmann, L., Rasmusson, A.G., Heiser, V. and Brennicke, A. (1996) The NADH-binding subunit of respiratory chain complex I is nuclear-encoded in plants and identified only in mitochondria. Plant J. 10: 793-803. (Pubitemid 27102995)
    • (1996) Plant Journal , vol.10 , Issue.5 , pp. 793-803
    • Grohmann, L.1    Rasmusson, A.G.2    Heiser, V.3    Thieck, O.4    Brennicke, A.5
  • 14
    • 0345393082 scopus 로고    scopus 로고
    • A nucleus-encoded factor, CRR2, is essential for the expression of chloroplast ndhB in Arabidopsis
    • DOI 10.1046/j.1365-313X.2003.01900.x
    • Hashimoto, M., Endo, T., Peltier, G., Tasaka, M. and Shikanai, T. (2003) A nucleus-encoded factor, CRR2, is essential for the expression of chloroplast ndhB in Arabidopsis. Plant J. 36: 541-549. (Pubitemid 37457941)
    • (2003) Plant Journal , vol.36 , Issue.4 , pp. 541-549
    • Hashimoto, M.1    Endo, T.2    Peltier, G.3    Tasaka, M.4    Shikanai, T.5
  • 15
    • 0001391899 scopus 로고
    • Concerning a dual function of coupled cyclic electron transport in leaves
    • Heber, U. and Walker, D.A. (1992) Concerning a dual function of coupled cyclic electron transport in leaves. Plant Physiol. 100: 1621-1626.
    • (1992) Plant Physiol. , vol.100 , pp. 1621-1626
    • Heber, U.1    Walker, D.A.2
  • 16
    • 0033849066 scopus 로고    scopus 로고
    • Targeted inactivation of the plastid ndhB gene in tobacco results in an enhanced sensitivity of photosynthesis to moderate stomatal closure
    • Horváth, E.M., Peter, S.O., Joët, T., Rumeau, D., Cournac, L., Horváth, G.V. et al. (2000) Targeted inactivation of the plastid ndhB gene in tobacco results in an enhanced sensitivity of photosynthesis to moderate stomatal closure. Plant Physiol. 123: 1337-1350.
    • (2000) Plant Physiol. , vol.123 , pp. 1337-1350
    • Horváth, E.M.1    Peter, S.O.2    Joët, T.3    Rumeau, D.4    Cournac, L.5    Horváth, G.V.6
  • 17
    • 78349253827 scopus 로고    scopus 로고
    • Stimulation of cyclic electron flow during recovery after chilling-induced photoinhibition of PSII
    • Huang, W., Zhang, S.B. and Cao, K.F. (2010) Stimulation of cyclic electron flow during recovery after chilling-induced photoinhibition of PSII. Plant Cell Physiol. 51: 1922-1928.
    • (2010) Plant Cell Physiol. , vol.51 , pp. 1922-1928
    • Huang, W.1    Zhang, S.B.2    Cao, K.F.3
  • 18
    • 79951562295 scopus 로고    scopus 로고
    • Cyclic electron flow plays an important role in photoprotection of tropical trees illuminated at temporal chilling temperature
    • Huang, W., Zhang, S.B. and Cao, K.F. (2011) Cyclic electron flow plays an important role in photoprotection of tropical trees illuminated at temporal chilling temperature. Plant Cell Physiol. 52: 297-305.
    • (2011) Plant Cell Physiol. , vol.52 , pp. 297-305
    • Huang, W.1    Zhang, S.B.2    Cao, K.F.3
  • 19
    • 77955143668 scopus 로고    scopus 로고
    • Molecular functions of oxygen-evolving complex family proteins in photosynthetic electron flow
    • Ifuku, K., Ishihara, S. and Sato, F. (2010) Molecular functions of oxygen-evolving complex family proteins in photosynthetic electron flow. J. Integr. Plant Biol. 52: 723-734.
    • (2010) J. Integr. Plant Biol. , vol.52 , pp. 723-734
    • Ifuku, K.1    Ishihara, S.2    Sato, F.3
  • 20
    • 60149090748 scopus 로고    scopus 로고
    • A novel nuclear-encoded protein, NDH-dependent cyclic electron flow 5, is essential for the accumulation of chloroplast NAD(P)H dehydrogenase complexes
    • Ishida, S., Takabayashi, A., Ishikawa, N., Hano, Y., Endo, T. and Sato, F. (2009) A novel nuclear-encoded protein, NDH-dependent cyclic electron flow 5, is essential for the accumulation of chloroplast NAD(P)H dehydrogenase complexes. Plant Cell Physiol. 50: 383-393.
    • (2009) Plant Cell Physiol. , vol.50 , pp. 383-393
    • Ishida, S.1    Takabayashi, A.2    Ishikawa, N.3    Hano, Y.4    Endo, T.5    Sato, F.6
  • 21
    • 36248982591 scopus 로고    scopus 로고
    • Distinct functions for the two PsbP-like proteins PPL1 and PPL2 in the chloroplast thylakoid lumen of Arabidopsis
    • DOI 10.1104/pp.107.105866
    • Ishihara, S., Takabayashi, A., Ido, K., Endo, T., Ifuku, K. and Sato, F. (2007) Distinct functions for the two PsbP-like proteins PPL1 and PPL2 in the chloroplast thylakoid lumen of Arabidopsis. Plant Physiol. 145: 668-679. (Pubitemid 350127601)
    • (2007) Plant Physiology , vol.145 , Issue.3 , pp. 668-679
    • Ishihara, S.1    Takabayashi, A.2    Ido, K.3    Endo, T.4    Ifuku, K.5    Sato, F.6
  • 22
    • 47249158473 scopus 로고    scopus 로고
    • NDF6: A thylakoid protein specific to terrestrial plants is essential for activity of chloroplastic NAD(P)H dehydrogenase in Arabidopsis
    • DOI 10.1093/pcp/pcn083
    • Ishikawa, N., Takabayashi, A., Ishida, S., Hano, Y., Endo, T. and Sato, F. (2008) NDF6: a thylakoid protein specific to terrestrial plants is essential for activity of chloroplastic NAD(P)H dehydrogenase in Arabidopsis. Plant Cell Physiol. 49: 1066-1073. (Pubitemid 351989694)
    • (2008) Plant and Cell Physiology , vol.49 , Issue.7 , pp. 1066-1073
    • Ishikawa, N.1    Takabayashi, A.2    Ishida, S.3    Hano, Y.4    Endo, T.5    Sato, F.6
  • 23
    • 77951622488 scopus 로고    scopus 로고
    • Isolation of the elusive supercomplex that drives cyclic electron flow in photosynthesis
    • Iwai, M., Takizawa, K., Tokutsu, R., Okamura, A., Takahashi, Y. and Minagawa, J. (2010) Isolation of the elusive supercomplex that drives cyclic electron flow in photosynthesis. Nature 464: 1210-1213.
    • (2010) Nature , vol.464 , pp. 1210-1213
    • Iwai, M.1    Takizawa, K.2    Tokutsu, R.3    Okamura, A.4    Takahashi, Y.5    Minagawa, J.6
  • 24
    • 79958159154 scopus 로고
    • Physiology of PSI cyclic electron transport in higher plants
    • Johnson, G.M. (2011) Physiology of PSI cyclic electron transport in higher plants. Biochim. Biophys. Acta 1807: 906-911.
    • (1807) Biochim. Biophys. Acta , pp. 906-911
    • Johnson, G.M.1
  • 25
    • 0031948338 scopus 로고    scopus 로고
    • Mutagenesis of the genes encoding subunits A, C, H, I, J and K of the plastid NAD(P)H-plastoquinone-oxidoreductase in tobacco by polyethylene glycol-mediated plastome transformation
    • Kofer, W., Koop, H.-U., Wanne, G. and Steinmüller, K. (1998) Mutagenesis of the genes encoding subunits A, C, H, I, J and K of the plastid NAD(P)H-plastoquinone-oxidoreductase in tobacco by polyethylene glycol-mediated plastome transformation. Mol. Gen. Genet. 258: 166-173.
    • (1998) Mol. Gen. Genet. , vol.258 , pp. 166-173
    • Kofer, W.1    Koop, H.-U.2    Wanne, G.3    Steinmüller, K.4
  • 26
    • 0034438086 scopus 로고    scopus 로고
    • 2 in NADP-malic enzyme type species
    • DOI 10.1023/A:1010695402963
    • Laisk, A. and Edwards, G.E. (2000) A mathematical model of C4 photosynthesis: the mechanism of concentrating CO2 in NADP-malic enzyme type species. Photosynth. Res. 66: 199-224. (Pubitemid 32540580)
    • (2000) Photosynthesis Research , vol.66 , Issue.3 , pp. 199-224
    • Laisk, A.1    Edwards, G.E.2
  • 27
    • 80052887521 scopus 로고    scopus 로고
    • Leaf C4 photosynthesis in silico: The CO2 concentrating mechanism
    • Edited by Laisk, S., Nedbal, L. and Govindjee. Springer Science + Business Media B.V., The Netherlands
    • Laisk, A. and Edwards, G. (2009) Leaf C4 photosynthesis in silico: the CO2 concentrating mechanism. In Photosynthesis in Silico: Understanding Complexity from Molecules to Ecosystems. Edited by Laisk, S., Nedbal, L. and Govindjee. pp. 323-348. Springer Science + Business Media B.V., The Netherlands.
    • (2009) Photosynthesis in Silico: Understanding Complexity from Molecules to Ecosystems , pp. 323-348
    • Laisk, A.1    Edwards, G.2
  • 28
    • 36249025556 scopus 로고    scopus 로고
    • Rates and roles of cyclic and alternative electron flow in potato leaves
    • DOI 10.1093/pcp/pcm129
    • Laisk, A., Eichelmann, H., Oja, V., Talts, E. and Scheibe, R. (2007) Rates and roles of cyclic and alternative electron flow in potato leaves. Plant Cell Physiol. 48: 1575-1588. (Pubitemid 350135513)
    • (2007) Plant and Cell Physiology , vol.48 , Issue.11 , pp. 1575-1588
    • Laisk, A.1    Eichelmann, H.2    Oja, V.3    Talts, E.4    Scheibe, R.5
  • 29
    • 76149100874 scopus 로고    scopus 로고
    • Fast cyclic electron transport around photosystem i in leaves under far-red light: A proton-uncoupled pathway?
    • Laisk, A., Talts, E., Oja, V., Eichelmann, H. and Peterson, R. (2010) Fast cyclic electron transport around photosystem I in leaves under far-red light: a proton-uncoupled pathway?. Photosynth. Res. 103: 79-95.
    • (2010) Photosynth. Res. , vol.103 , pp. 79-95
    • Laisk, A.1    Talts, E.2    Oja, V.3    Eichelmann, H.4    Peterson, R.5
  • 30
    • 1042291445 scopus 로고    scopus 로고
    • The function of chloroplastic NAD(P)H dehydrogenase in tobacco during chilling stress under low irradiance
    • DOI 10.1093/pcp/pch011
    • Li, X.G., Duan, W., Meng, Q.W., Zou, Q. and Zhao, S.J. (2004) The function of chloroplastic NAD(P)H dehydrogenase in tobacco during chilling stress under low irradiance. Plant Cell Physiol. 45: 103-108. (Pubitemid 38192339)
    • (2004) Plant and Cell Physiology , vol.45 , Issue.1 , pp. 103-108
    • Li, X.-G.1    Duan, W.2    Meng, Q.-W.3    Zou, Q.4    Zhao, S.-J.5
  • 31
    • 52649096494 scopus 로고    scopus 로고
    • Consequences of C4 differentiation for chloroplast membrane proteomes in maize mesophyll and bundle sheath cells
    • Majeran, W., Zybailov, B., Ytterberg, A.J., Dunsmore, J., Sun, Q. and van Wijk, K.J. (2008) Consequences of C4 differentiation for chloroplast membrane proteomes in maize mesophyll and bundle sheath cells. Mol. Cell. Proteomics 7: 1609-1638.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1609-1638
    • Majeran, W.1    Zybailov, B.2    Ytterberg, A.J.3    Dunsmore, J.4    Sun, Q.5    Van Wijk, K.J.6
  • 32
    • 0028121693 scopus 로고
    • NAD(P)H dehydrogenase-dependent cyclic electron flow around Photosystem I in the cyanobacterium Synechocystis PCC 6803: A study of dark-starved cells and spheroplasts
    • Mi, H., Endo, T., Schreiber, U., Ogawa, T. and Asada, K. (1994) NAD(P)H-dehydrogenase dependent cyclic electron flow around photosystem I in the cyanobacterium Synechocystis PCC 6803: a study of dark-starved cells and spheroplasts. Plant Cell Physiol. 35: 163-173. (Pubitemid 2076734)
    • (1994) Plant and Cell Physiology , vol.35 , Issue.2 , pp. 163-173
    • Mi Hualing1    Endo, T.2    Schreiber, U.3    Ogawa, T.4    Asada, K.5
  • 33
    • 0028814979 scopus 로고
    • Thylakoid membrane-bound, NADPH-specific pyridine nucleotide dehydro-genase complex mediates cyclic electron transport in the cyano-bacterium Synechocystis sp PCC 6803
    • Mi, H., Endo, T., Ogawa, T. and Asada, K. (1995) Thylakoid membrane-bound, NADPH-specific pyridine nucleotide dehydro-genase complex mediates cyclic electron transport in the cyano-bacterium Synechocystis sp. PCC 6803. Plant Cell Physiol. 36: 661-668.
    • (1995) Plant Cell Physiol. , vol.36 , pp. 661-668
    • Mi, H.1    Endo, T.2    Ogawa, T.3    Asada, K.4
  • 34
    • 0018786935 scopus 로고
    • Electron transport pathways in spinach chloroplasts Reduction of the primary acceptor of photosystem II by reduced nicotinamide dinucleotide phosphate in the dark
    • Mills, J.D., Crowther, D., Slovacek, R.E., Hind, G. and McCarty, R. (1979) Electron transport pathways in spinach chloroplasts. Reduction of the primary acceptor of photosystem II by reduced nicotinamide dinucleotide phosphate in the dark. Biochim. Biophys. Acta 547: 127-137.
    • (1979) Biochim. Biophys. Acta , vol.547 , pp. 127-137
    • Mills, J.D.1    Crowther, D.2    Slovacek, R.E.3    Hind, G.4    McCarty, R.5
  • 35
    • 78651331355 scopus 로고    scopus 로고
    • Alternative electron flows (water-water cycle and cyclic electron flow around PSI) in photosynthesis: Molecular mechanisms and physiological functions
    • Miyake, C. (2010) Alternative electron flows (water-water cycle and cyclic electron flow around PSI) in photosynthesis: molecular mechanisms and physiological functions. Plant Cell Physiol. 51: 1951-1963.
    • (2010) Plant Cell Physiol. , vol.51 , pp. 1951-1963
    • Miyake, C.1
  • 36
    • 0037047381 scopus 로고    scopus 로고
    • PGR5 is involved in cyclic electron flow around photosystem i and is essential for photoprotection in Arabidopsis
    • Munekage, Y., Hojo, M., Meurer, J., Endo, T., Tasaka, M. and Shikanai, T. (2002) PGR5 is involved in cyclic electron flow around photosystem I and is essential for photoprotection in Arabidopsis. Cell 110: 361-371.
    • (2002) Cell , vol.110 , pp. 361-371
    • Munekage, Y.1    Hojo, M.2    Meurer, J.3    Endo, T.4    Tasaka, M.5    Shikanai, T.6
  • 37
    • 2942537759 scopus 로고    scopus 로고
    • Cyclic electron flow around photosystem I is essential for photosynthesis
    • DOI 10.1038/nature02598
    • Munekage, Y., Hashimoto, M., Miyake, C., Tomizawa, K., Endo, T., Tasaka, M. et al. (2004) Cyclic electron flow around photosystem I is essential for photosynthesis. Nature 429: 579-582. (Pubitemid 38737664)
    • (2004) Nature , vol.429 , Issue.6991 , pp. 579-582
    • Munekage, Y.1    Hashimoto, M.2    Miyake, C.3    Tomizawa, K.-I.4    Endo, T.5    Tasaka, M.6    Shikanai, T.7
  • 38
    • 33845671769 scopus 로고    scopus 로고
    • A eukaryotic factor required for accumulation of the chloroplast NAD(P)H dehydrogenase complex in arabidopsis
    • DOI 10.1104/pp.106.088682
    • Muraoka, R., Okuda, K., Kobayashi, Y. and Shikanai, T. (2006) A eu-karyotic factor required for accumulation of the chloroplast NAD(P)H dehydrogenase complex in Arabidopsis. Plant Physiol. 142: 1683-1689. (Pubitemid 44956942)
    • (2006) Plant Physiology , vol.142 , Issue.4 , pp. 1683-1689
    • Muraoka, R.1    Okuda, K.2    Kobayashi, Y.3    Shikanai, T.4
  • 39
    • 34848843479 scopus 로고    scopus 로고
    • The role of PGR5 in the redox poising of photosynthetic electron transport
    • DOI 10.1016/j.bbabio.2007.07.007, PII S0005272807001612
    • Nandha, B., Finazzi, G., Joliot, P., Hald, S. and Johnson, G.N. (2007) The role of PGR5 in the redox poising of photosynthetic electron transport. Biochim. Biophys. Acta 1767: 1252-1259. (Pubitemid 47498311)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.10 , pp. 1252-1259
    • Nandha, B.1    Finazzi, G.2    Joliot, P.3    Hald, S.4    Johnson, G.N.5
  • 40
    • 0001400342 scopus 로고
    • Identification and characterization of the ictA/ndhL gene product essential to inorganic carbon transport of Synechocystis sp strain PCC6803
    • Ogawa, T. (1992) Identification and characterization of the ictA/ndhL gene product essential to inorganic carbon transport of Synechocystis sp strain PCC6803. Plant Physiol. 99: 1604-1608.
    • (1992) Plant Physiol. , vol.99 , pp. 1604-1608
    • Ogawa, T.1
  • 41
    • 44449167983 scopus 로고    scopus 로고
    • Characterization of factors affecting the activity of photosystem I cyclic electron transport in chloroplasts
    • DOI 10.1093/pcp/pcn055
    • Okegawa, Y., Kagawa, Y., Kobayashi, Y. and Shikanai, T. (2008) Characterization of factors affecting the activity of photosystem I cyclic electron transport in chloroplasts. Plant Cell Physiol. 49: 825-834. (Pubitemid 351769886)
    • (2008) Plant and Cell Physiology , vol.49 , Issue.5 , pp. 825-834
    • Okegawa, Y.1    Kagawa, Y.2    Kobayashi, Y.3    Shikanai, T.4
  • 42
    • 77954436604 scopus 로고    scopus 로고
    • Chloroplast stromal proteins, CRR6 and CRR7, are required for assembly of the NAD(P)H dehydrogenase subcomplex A in Arabidopsis
    • Peng, L., Cai, W. and Shikanai, T. (2010) Chloroplast stromal proteins, CRR6 and CRR7, are required for assembly of the NAD(P)H dehydrogenase subcomplex A in Arabidopsis. Plant J. 63: 203-211.
    • (2010) Plant J. , vol.63 , pp. 203-211
    • Peng, L.1    Cai, W.2    Shikanai, T.3
  • 43
    • 73249123281 scopus 로고    scopus 로고
    • Efficient operation of NAD(P)H dehydrogenase requires supercom-plex formation with photosystem i via minor LHCI in Arabidopsis
    • Peng, L., Fukao, Y., Fujiwara, M., Takami, T. and Shikanai, T. (2009) Efficient operation of NAD(P)H dehydrogenase requires supercom-plex formation with photosystem I via minor LHCI in Arabidopsis. Plant Cell 21: 3623-2640.
    • (2009) Plant Cell , vol.21 , pp. 3623-2640
    • Peng, L.1    Fukao, Y.2    Fujiwara, M.3    Takami, T.4    Shikanai, T.5
  • 44
    • 79955492385 scopus 로고    scopus 로고
    • A chaperonin subunit with unique structures is essential for folding of a specific substrate
    • Peng, L., Fukao, Y., Myouga, F., Motohashi, R., Shinozaki, K. and Shikanai, T. (2011b) A chaperonin subunit with unique structures is essential for folding of a specific substrate. PLoS Biol. 9: e1001040.
    • (2011) PLoS Biol. , vol.9
    • Peng, L.1    Fukao, Y.2    Myouga, F.3    Motohashi, R.4    Shinozaki, K.5    Shikanai, T.6
  • 45
    • 79953681329 scopus 로고    scopus 로고
    • Supercomplex formation with photo-system i is required for the stabilization of the chloroplast NADH dehydrogenase-like complex in Arabidopsis
    • Peng, L. and Shikanai, T. (2011) Supercomplex formation with photo-system I is required for the stabilization of the chloroplast NADH dehydrogenase-like complex in Arabidopsis. Plant Physiol. 155: 1629-1639.
    • (2011) Plant Physiol. , vol.155 , pp. 1629-1639
    • Peng, L.1    Shikanai, T.2
  • 46
    • 58049211385 scopus 로고    scopus 로고
    • The chloroplast NAD(P)H dehydrogenase complex interacts with photosystem i in Arabidopsis
    • Peng, L., Shimizu, H. and Shikanai, T. (2008) The chloroplast NAD(P)H dehydrogenase complex interacts with photosystem I in Arabidopsis. J. Biol. Chem. 283: 34873-34879.
    • (2008) J. Biol. Chem. , vol.283 , pp. 34873-34879
    • Peng, L.1    Shimizu, H.2    Shikanai, T.3
  • 47
    • 79958082745 scopus 로고
    • Structure and biogenesis of the chloroplast NAD(P)H dehydrogenase complex
    • Peng, L., Yamamoto, H. and Shikanai, T. (2011a) Structure and biogenesis of the chloroplast NAD(P)H dehydrogenase complex. Biochim. Biophys. Acta 1807: 945-953.
    • (1807) Biochim. Biophys. Acta , pp. 945-953
    • Peng, L.1    Yamamoto, H.2    Shikanai, T.3
  • 48
    • 3142653751 scopus 로고    scopus 로고
    • Subunit composition of NDH-1 complexes of Synechocystis sp. PCC 6803. Identification of two new ndh gene products with nuclear-encoded homologues in the chloroplast Ndh complex
    • DOI 10.1074/jbc.M401107200
    • Prommeenate, P., Lennon, A.M., Markert, C., Hippler, M. and Nixon, P.J. (2004) Subunit composition of NDH-1 complexes of Synechocystis sp. PCC 6803: identification of two new ndh gene products with nuclear-encoded homologues in the chloroplast Ndh complex. J. Biol. Chem. 279: 28165-28173. (Pubitemid 38900091)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.27 , pp. 28165-28173
    • Prommeenate, P.1    Lennon, A.M.2    Markert, C.3    Hippler, M.4    Nixon, P.J.5
  • 49
    • 18844447930 scopus 로고    scopus 로고
    • New Subunits NDH-M, -N, and -O, encoded by nuclear genes, are essential for plastid Ndh complex functioning in higher plants
    • DOI 10.1105/tpc.104.028282
    • Rumeau, D., Bécuwe-Linka, N., Beyly, A., Louwagie, M., Garin, J. and Peltier, G. (2005) New subunits NDH-M,-N, and-O, encoded by nuclear genes, are essential for plastid Ndh complex functioning in higher plants. Plant Cell 17: 219-232. (Pubitemid 41672998)
    • (2005) Plant Cell , vol.17 , Issue.1 , pp. 219-232
    • Rumeau, D.1    Becuwe-Linka, N.2    Beyly, A.3    Louwagie, M.4    Garin, J.5    Peltier, G.6
  • 50
    • 34250847628 scopus 로고    scopus 로고
    • Cyclic electron transport around photosystem I: Genetic approaches
    • DOI 10.1146/annurev.arplant.58.091406.110525
    • Shikanai, T. (2007) Cyclic electron transport around photosystem I; genetic approaches. Annu. Rev. Plant Biol. 58: 199-217. (Pubitemid 46986323)
    • (2007) Annual Review of Plant Biology , vol.58 , pp. 199-217
    • Shikanai, T.1
  • 52
    • 44449083714 scopus 로고    scopus 로고
    • CRR23/NdhL is a subunit of the chloroplast NAD(P)H dehydrogenase complex in Arabidopsis
    • DOI 10.1093/pcp/pcn058
    • Shimizu, H., Peng, L., Myouga, F., Motohashi, R., Shinozaki, K. and Shikanai, T. (2008) CRR23/NdhL is a subunit of the chloroplast NAD(P)H dehydrogenase complex in Arabidopsis. Plant Cell Physiol. 49: 835-842. (Pubitemid 351769887)
    • (2008) Plant and Cell Physiology , vol.49 , Issue.5 , pp. 835-842
    • Shimizu, H.1    Peng, L.2    Myouga, F.3    Motohashi, R.4    Shinozaki, K.5    Shikanai, T.6
  • 53
    • 35448975268 scopus 로고    scopus 로고
    • Dihydrodipicolinate reductase-like protein, CRR1, is essential for chloroplast NAD(P)H dehydrogenase in Arabidopsis
    • DOI 10.1111/j.1365-313X.2007.03256.x
    • Shimizu, H. and Shikanai, T. (2007) Dihydrodipicolinate reductase-like protein, CRR1, is essential for chloroplast NAD(P)H dehydrogenase in Arabidopsis. Plant J. 52: 539-547. (Pubitemid 47621880)
    • (2007) Plant Journal , vol.52 , Issue.3 , pp. 539-547
    • Shimizu, H.1    Shikanai, T.2
  • 55
    • 67650117729 scopus 로고    scopus 로고
    • AtCYP20-2 is an auxiliary protein of the chloroplast NAD(P)H de-hydrogenase complex
    • Sirpiö, S., Holmström, M., Battchikova, N and Aro, E.-M. (2009b) AtCYP20-2 is an auxiliary protein of the chloroplast NAD(P)H de-hydrogenase complex. FEBS Lett. 583: 2355-2358.
    • (2009) FEBS Lett. , vol.583 , pp. 2355-2358
    • Sirpiö, S.1    Holmström, M.2    Battchikova, N.3    Aro, E.-M.4
  • 56
    • 71249105141 scopus 로고    scopus 로고
    • Towards characterization of the chloroplast NAD(P)H dehydrogenase complex
    • Suorsa, M., Sirpiö, S. and Aro, E.-M. (2009) Towards characterization of the chloroplast NAD(P)H dehydrogenase complex. Mol. Plant 2: 1127-1140.
    • (2009) Mol. Plant , vol.2 , pp. 1127-1140
    • Suorsa, M.1    Sirpiö, S.2    Aro, E.-M.3
  • 57
    • 77953556989 scopus 로고    scopus 로고
    • Two proteins homologous to PsbQ are novel subunits of the chloroplast NAD(P)H dehydrogenase
    • Suorsa, M., Sirpiö, S., Paakkarinen, V., Kumari, N., Holmström, M. and Aro, E.-M. (2010) Two proteins homologous to PsbQ are novel subunits of the chloroplast NAD(P)H dehydrogenase. Plant Cell Physiol. 51: 877-883.
    • (2010) Plant Cell Physiol. , vol.51 , pp. 877-883
    • Suorsa, M.1    Sirpiö, S.2    Paakkarinen, V.3    Kumari, N.4    Holmström, M.5    Aro, E.-M.6
  • 59
    • 0001414438 scopus 로고
    • Role of chloroplast ferredoxin in the energy conversion process of photosynthesis
    • Tagawa, K., Tsujimoto, H.Y. and Arnon, D.I. (1963) Role of chloroplast ferredoxin in the energy conversion process of photosynthesis. Proc. Natl Acad. Sci. USA 49: 567-572.
    • (1963) Proc. Natl Acad. Sci. USA , vol.49 , pp. 567-572
    • Tagawa, K.1    Tsujimoto, H.Y.2    Arnon, D.I.3
  • 61
    • 58349120608 scopus 로고    scopus 로고
    • Three novel subunits of Arabidopsis chloro-plastic NAD(P)H dehydrogenase identified by bioinformatic and reverse genetic approaches
    • Takabayashi, A., Ishikawa, N., Obayashi, T., Ishida, S., Obokata, J., Endo, T. et al. (2009) Three novel subunits of Arabidopsis chloro-plastic NAD(P)H dehydrogenase identified by bioinformatic and reverse genetic approaches. Plant J. 57: 207-219.
    • (2009) Plant J. , vol.57 , pp. 207-219
    • Takabayashi, A.1    Ishikawa, N.2    Obayashi, T.3    Ishida, S.4    Obokata, J.5    Endo, T.6
  • 62
    • 75949107015 scopus 로고    scopus 로고
    • Thylakoid protein phosphorylation in higher plant chloroplasts optimizes electron transfer under fluctuating light
    • Tikkanen, M., Grieco, M., Kangasjärvi, S. and Aro, E.-M. (2010) Thylakoid protein phosphorylation in higher plant chloroplasts optimizes electron transfer under fluctuating light. Plant Physiol. 152: 723-735.
    • (2010) Plant Physiol. , vol.152 , pp. 723-735
    • Tikkanen, M.1    Grieco, M.2    Kangasjärvi, S.3    Aro, E.-M.4
  • 64
    • 33745668217 scopus 로고    scopus 로고
    • Chloroplastic NAD(P)H dehydrogenase in tobacco leaves functions in alleviation of oxidative damage caused by temperature stress
    • DOI 10.1104/pp.105.070490
    • Wang, P., Duan, W., Takabayashi, A., Endo, T., Shikanai, T., Ye, J.Y. et al. (2006) Chloroplastic NAD(P)H dehydrogenase in tobacco leaves functions in alleviation of oxidative damage caused by temperature stress. Plant Physiol. 141: 465-474. (Pubitemid 43974541)
    • (2006) Plant Physiology , vol.141 , Issue.2 , pp. 465-474
    • Wang, P.1    Duan, W.2    Takabayashi, A.3    Endo, T.4    Shikanai, T.5    Ye, J.-Y.6    Mi, H.7
  • 65
    • 77953606649 scopus 로고    scopus 로고
    • Three PsbQ-like proteins are required for the function of the chloroplast NAD(P)H dehydrogenase complex in Arabidopsis
    • Yabuta, S., Ifuku, K., Takabayashi, A., Ishihara, S., Ido, K., Ishikawa, N. et al. (2010) Three PsbQ-like proteins are required for the function of the chloroplast NAD(P)H dehydrogenase complex in Arabidopsis. Plant Cell Physiol. 51: 866-876.
    • (2010) Plant Cell Physiol. , vol.51 , pp. 866-876
    • Yabuta, S.1    Ifuku, K.2    Takabayashi, A.3    Ishihara, S.4    Ido, K.5    Ishikawa, N.6
  • 66
    • 79957773110 scopus 로고    scopus 로고
    • An Src homology 3 domain-like fold protein forms a ferredoxin-binding site for the chloroplast NADH dehydrogenase-like complex in Arabidopsis
    • Yamamoto, H., Peng, L., Fukao, Y. and Shikanai, T. (2011) An Src homology 3 domain-like fold protein forms a ferredoxin-binding site for the chloroplast NADH dehydrogenase-like complex in Arabidopsis. Plant Cell 23: 1480-1493.
    • (2011) Plant Cell , vol.23 , pp. 1480-1493
    • Yamamoto, H.1    Peng, L.2    Fukao, Y.3    Shikanai, T.4
  • 67
    • 18844436373 scopus 로고    scopus 로고
    • Expression and functional roles of the two distinct NDH-1 complexes and the carbon acquisition complex NdhD3/NdhF3/CupA/SII1735 in Synechocystis sp PCC 6803
    • DOI 10.1105/tpc.104.026526
    • Zhang, P., Battchikova, N., Jansen, T., Appel, J., Ogawa, T. and Aro, E.-M. (2004) Expression and functional roles of the two distinct NDH-1 complexes and the carbon acquisition complex NdxD3/NdhF3/CupA/Sll1735 in Synechocystis sp. PCC 6803. Plant Cell 16: 3326-3340. (Pubitemid 41096009)
    • (2004) Plant Cell , vol.16 , Issue.12 , pp. 3326-3340
    • Zhang, P.1    Battchikova, N.2    Jansen, T.3    Appel, J.4    Ogawa, T.5    Aro, E.-M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.