메뉴 건너뛰기




Volumn 2, Issue , 2009, Pages 603-637

The Cytochrome b6f Complex

Author keywords

[No Author keywords available]

Indexed keywords


EID: 78650246205     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-370873-1.00025-3     Document Type: Chapter
Times cited : (9)

References (152)
  • 1
    • 33747184794 scopus 로고    scopus 로고
    • Prediction of transmembrane helix orientation in polytopic membrane proteins
    • Adamian L., Liang J. Prediction of transmembrane helix orientation in polytopic membrane proteins. BMC Struct. Biol. 2006, 6:13.
    • (2006) BMC Struct. Biol. , vol.6 , pp. 13
    • Adamian, L.1    Liang, J.2
  • 3
    • 0028272427 scopus 로고
    • A nuclear mutation in maize blocks the processing and translation of several chloroplast mRNAs and provides evidence for the differential translation of alternative mRNA forms
    • Barkan A., Walker M., Nolasco M., Johnson D. A nuclear mutation in maize blocks the processing and translation of several chloroplast mRNAs and provides evidence for the differential translation of alternative mRNA forms. EMBO J. 1994, 13:3170-3181.
    • (1994) EMBO J. , vol.13 , pp. 3170-3181
    • Barkan, A.1    Walker, M.2    Nolasco, M.3    Johnson, D.4
  • 5
    • 0028944579 scopus 로고
    • Cyclic photophosphorylation and electron-transport
    • Bendall D.S., Manasse R.S. Cyclic photophosphorylation and electron-transport. Biochim. Biophys. Acta 1995, 1229:23-38.
    • (1995) Biochim. Biophys. Acta , vol.1229 , pp. 23-38
    • Bendall, D.S.1    Manasse, R.S.2
  • 6
    • 0028807043 scopus 로고
    • The deletion of petG in Chlamydomonas reinhardtii disrupts the cytochrome bf complex
    • Berthold D.A., Schmidt C.L., Malkin R. The deletion of petG in Chlamydomonas reinhardtii disrupts the cytochrome bf complex. J. Biol. Chem. 1995, 270:29293-29298.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29293-29298
    • Berthold, D.A.1    Schmidt, C.L.2    Malkin, R.3
  • 7
    • 0034608009 scopus 로고    scopus 로고
    • 6f complex induced by inhibitor binding
    • 6f complex induced by inhibitor binding. J. Biol. Chem. 2000, 275:13195-13201.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13195-13201
    • Breyton, C.1
  • 8
    • 33750996424 scopus 로고    scopus 로고
    • Redox modulation of cyclic electron flow around photosystem I in C3 plants
    • Breyton C., Nandha B., Johnson G.N., Joliot P., Finazzi G. Redox modulation of cyclic electron flow around photosystem I in C3 plants. Biochemistry 2006, 45:13465-13475.
    • (2006) Biochemistry , vol.45 , pp. 13465-13475
    • Breyton, C.1    Nandha, B.2    Johnson, G.N.3    Joliot, P.4    Finazzi, G.5
  • 10
    • 0032481317 scopus 로고    scopus 로고
    • Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes
    • Burrows P.A., Sazanov L.A., Svab Z., Maliga P., Nixon P.J. Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes. EMBO J. 1998, 17:868-876.
    • (1998) EMBO J. , vol.17 , pp. 868-876
    • Burrows, P.A.1    Sazanov, L.A.2    Svab, Z.3    Maliga, P.4    Nixon, P.J.5
  • 11
    • 0034604237 scopus 로고    scopus 로고
    • X-ray structure of a truncated form of cytochrome f from Chlamydomonas reinhardtii
    • Chi Y.I., Huang L.S., Zhang Z., Fernandez-Velasco J.G., Berry E.A. X-ray structure of a truncated form of cytochrome f from Chlamydomonas reinhardtii. Biochemistry 2000, 39:7689-7701.
    • (2000) Biochemistry , vol.39 , pp. 7689-7701
    • Chi, Y.I.1    Huang, L.S.2    Zhang, Z.3    Fernandez-Velasco, J.G.4    Berry, E.A.5
  • 12
    • 0033865042 scopus 로고    scopus 로고
    • Synthesis, assembly and degradation of thylakoid membrane proteins
    • Choquet Y., Vallon O. Synthesis, assembly and degradation of thylakoid membrane proteins. Biochimie 2000, 82:615-634.
    • (2000) Biochimie , vol.82 , pp. 615-634
    • Choquet, Y.1    Vallon, O.2
  • 13
    • 0032516017 scopus 로고    scopus 로고
    • Translation of cytochrome f is autoregulated through the 5′ untranslated region of petA mRNA in Chlamydomonas chloroplasts
    • Choquet Y., Stern D.B., Wostrikoff K., Kuras R., Girard-Bascou J., Wollman F.A. Translation of cytochrome f is autoregulated through the 5′ untranslated region of petA mRNA in Chlamydomonas chloroplasts. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:4380-4385.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 4380-4385
    • Choquet, Y.1    Stern, D.B.2    Wostrikoff, K.3    Kuras, R.4    Girard-Bascou, J.5    Wollman, F.A.6
  • 15
    • 0038118626 scopus 로고    scopus 로고
    • Cytochrome f translation in Chlamydomonas chloroplast is autoregulated by its carboxyl-terminal domain
    • Choquet Y., Zito F., Wostrikoff K., Wollman F.A. Cytochrome f translation in Chlamydomonas chloroplast is autoregulated by its carboxyl-terminal domain. Plant Cell 2003, 15:1443-1454.
    • (2003) Plant Cell , vol.15 , pp. 1443-1454
    • Choquet, Y.1    Zito, F.2    Wostrikoff, K.3    Wollman, F.A.4
  • 16
    • 33745584611 scopus 로고    scopus 로고
    • 6f complex for its charge transfer pathways
    • 6f complex for its charge transfer pathways. Biochim. Biophys. Acta 2006, 1757:339-345.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 339-345
    • Cramer, W.A.1    Zhang, H.2
  • 18
    • 18844402628 scopus 로고    scopus 로고
    • 6f complex: New prosthetic groups, Q-space, and the "hors d'oeuvres hypothesis" for assembly of the complex
    • 6f complex: New prosthetic groups, Q-space, and the "hors d'oeuvres hypothesis" for assembly of the complex. Photosynth. Res. 2005, 85:133-143.
    • (2005) Photosynth. Res. , vol.85 , pp. 133-143
    • Cramer, W.A.1    Yan, J.2    Zhang, H.3    Kurisu, G.4    Smith, J.L.5
  • 20
    • 1942447877 scopus 로고    scopus 로고
    • 1 complex: Function in the context of structure
    • 1 complex: Function in the context of structure. Annu. Rev. Physiol. 2004, 66:689-733.
    • (2004) Annu. Rev. Physiol. , vol.66 , pp. 689-733
    • Crofts, A.R.1
  • 21
    • 0001104663 scopus 로고
    • The role of the quinone pool in the cyclic electron-transfer chain in Rhodopseudomonas sphaeroides: A modified Q-cycle mechanism
    • Crofts A.R., Meinhardt S.W., Jones K.R., Snozzi M. The role of the quinone pool in the cyclic electron-transfer chain in Rhodopseudomonas sphaeroides: A modified Q-cycle mechanism. Biochim. Biophys. Acta 1983, 723:202-218.
    • (1983) Biochim. Biophys. Acta , vol.723 , pp. 202-218
    • Crofts, A.R.1    Meinhardt, S.W.2    Jones, K.R.3    Snozzi, M.4
  • 22
    • 0033619729 scopus 로고    scopus 로고
    • Mechanism of ubiquinol oxidation by the bc1 complex: role of the iron sulfur protein and its mobility.
    • Crofts A.R., Guergova-Kuras M., Huang L., Kuras R., Zhang Z., Berry E.A. Mechanism of ubiquinol oxidation by the bc1 complex: role of the iron sulfur protein and its mobility. Biochemistry 1999, 38:15791-15806.
    • (1999) Biochemistry , vol.38 , pp. 15791-15806
    • Crofts, A.R.1    Guergova-Kuras, M.2    Huang, L.3    Kuras, R.4    Zhang, Z.5    Berry, E.A.6
  • 23
    • 20444434349 scopus 로고    scopus 로고
    • Isolation and structural characterization of the Ndh complex from mesophyll and bundle sheath chloroplasts of Zea mays
    • Darie C.C., Biniossek M.L., Winter V., Mutschler B., Haehnel W. Isolation and structural characterization of the Ndh complex from mesophyll and bundle sheath chloroplasts of Zea mays. FEBS J. 2005, 272:2705-2716.
    • (2005) FEBS J. , vol.272 , pp. 2705-2716
    • Darie, C.C.1    Biniossek, M.L.2    Winter, V.3    Mutschler, B.4    Haehnel, W.5
  • 25
    • 0032703525 scopus 로고    scopus 로고
    • Mutants of Chlamydomonas: Tools to study thylakoid membrane structure, function and biogenesis
    • de Vitry C., Vallon O. Mutants of Chlamydomonas: Tools to study thylakoid membrane structure, function and biogenesis. Biochimie 1999, 81:631-643.
    • (1999) Biochimie , vol.81 , pp. 631-643
    • de Vitry, C.1    Vallon, O.2
  • 26
    • 15844384218 scopus 로고    scopus 로고
    • 6f complex. Nucleic acid and protein sequences, targeting signals, transmembrane topology
    • 6f complex. Nucleic acid and protein sequences, targeting signals, transmembrane topology. J. Biol. Chem. 1996, 271:10667-10671.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10667-10671
    • de Vitry, C.1    Breyton, C.2    Pierre, Y.3    Popot, J.L.4
  • 27
    • 0033213399 scopus 로고    scopus 로고
    • Analysis of the nucleus-encoded and chloroplast-targeted Rieske protein by classic and site-directed mutagenesis of Chlamydomonas
    • de Vitry C., Finazzi G., Baymann F., Kallas T. Analysis of the nucleus-encoded and chloroplast-targeted Rieske protein by classic and site-directed mutagenesis of Chlamydomonas. Plant Cell 1999, 11:2031-2044.
    • (1999) Plant Cell , vol.11 , pp. 2031-2044
    • de Vitry, C.1    Finazzi, G.2    Baymann, F.3    Kallas, T.4
  • 29
    • 7244220013 scopus 로고    scopus 로고
    • The chloroplast Rieske iron-sulfur protein. At the crossroad of electron transport and signal transduction
    • de Vitry C., Ouyang Y., Finazzi G., Wollman F.A., Kallas T. The chloroplast Rieske iron-sulfur protein. At the crossroad of electron transport and signal transduction. J. Biol. Chem. 2004, 279:44621-44627.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44621-44627
    • de Vitry, C.1    Ouyang, Y.2    Finazzi, G.3    Wollman, F.A.4    Kallas, T.5
  • 30
    • 0034724331 scopus 로고    scopus 로고
    • 6f turnovers from the study of H/D substitution effects on the electrogenicity and electron transfer reactions
    • 6f turnovers from the study of H/D substitution effects on the electrogenicity and electron transfer reactions. Biochemistry 2000, 39:3304-3310.
    • (2000) Biochemistry , vol.39 , pp. 3304-3310
    • Deniau, C.1    Rappaport, F.2
  • 31
    • 0037423885 scopus 로고    scopus 로고
    • Role of chloroplast protein kinase Stt7 in LHCII phosphorylation and state transition in Chlamydomonas
    • Depège N., Bellafiore S., Rochaix J.D. Role of chloroplast protein kinase Stt7 in LHCII phosphorylation and state transition in Chlamydomonas. Science 2003, 299:1572-1575.
    • (2003) Science , vol.299 , pp. 1572-1575
    • Depège, N.1    Bellafiore, S.2    Rochaix, J.D.3
  • 32
    • 0031910348 scopus 로고    scopus 로고
    • In vivo evidence for 5′ → >3′ exoribonuclease degradation of an unstable chloroplast mRNA
    • Drager R.G., Girard-Bascou J., Choquet Y., Kindle K.L., Stern D.B. In vivo evidence for 5′ → >3′ exoribonuclease degradation of an unstable chloroplast mRNA. Plant J. 1998, 13:85-96.
    • (1998) Plant J. , vol.13 , pp. 85-96
    • Drager, R.G.1    Girard-Bascou, J.2    Choquet, Y.3    Kindle, K.L.4    Stern, D.B.5
  • 33
    • 0033199033 scopus 로고    scopus 로고
    • 5′ to 3′ exoribonucleolytic activity is a normal component of chloroplast mRNA decay pathways
    • Drager R.G., Higgs D.C., Kindle K.L., Stern D.B. 5′ to 3′ exoribonucleolytic activity is a normal component of chloroplast mRNA decay pathways. Plant J. 1999, 19:521-531.
    • (1999) Plant J. , vol.19 , pp. 521-531
    • Drager, R.G.1    Higgs, D.C.2    Kindle, K.L.3    Stern, D.B.4
  • 34
    • 84882907875 scopus 로고    scopus 로고
    • CCS5, a new locus required for chloroplast c-type cytochrome synthesis
    • Kluwer Academic Publishers, The Netherlands, G. Garab (Ed.)
    • Dreyfuss B.W., Merchant S. CCS5, a new locus required for chloroplast c-type cytochrome synthesis. Photosynthesis: Mechanisms and Effects 1999, Vol. IV:3221-3226. Kluwer Academic Publishers, The Netherlands. G. Garab (Ed.).
    • (1999) Photosynthesis: Mechanisms and Effects , vol.4 , pp. 3221-3226
    • Dreyfuss, B.W.1    Merchant, S.2
  • 35
    • 0037462683 scopus 로고    scopus 로고
    • Functional analysis of a divergent system II protein, Ccs1, involved in c-type cytochrome biogenesis
    • Dreyfuss B.W., Hamel P.P., Nakamoto S.S., Merchant S. Functional analysis of a divergent system II protein, Ccs1, involved in c-type cytochrome biogenesis. J. Biol. Chem. 2003, 278:2604-2613.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2604-2613
    • Dreyfuss, B.W.1    Hamel, P.P.2    Nakamoto, S.S.3    Merchant, S.4
  • 36
    • 0035112249 scopus 로고    scopus 로고
    • A nucleus-encoded suppressor defines a new factor which can promote petD mRNA stability in the chloroplast of Chlamydomonas reinhardtii
    • Esposito D., Higgs D.C., Drager R.G., Stern D.B., Girard-Bascou J. A nucleus-encoded suppressor defines a new factor which can promote petD mRNA stability in the chloroplast of Chlamydomonas reinhardtii. Curr. Genet. 2001, 39:40-48.
    • (2001) Curr. Genet. , vol.39 , pp. 40-48
    • Esposito, D.1    Higgs, D.C.2    Drager, R.G.3    Stern, D.B.4    Girard-Bascou, J.5
  • 37
    • 33645809956 scopus 로고    scopus 로고
    • Recombinant cytochromes c biogenesis systems I and II and analysis of haem delivery pathways in Escherichia coli
    • Feissner R.E., Richard-Fogal C.L., Frawley E.R., Loughman J.A., Earley K.W., Kranz R.G. Recombinant cytochromes c biogenesis systems I and II and analysis of haem delivery pathways in Escherichia coli. Mol. Microbiol. 2006, 60:563-577.
    • (2006) Mol. Microbiol. , vol.60 , pp. 563-577
    • Feissner, R.E.1    Richard-Fogal, C.L.2    Frawley, E.R.3    Loughman, J.A.4    Earley, K.W.5    Kranz, R.G.6
  • 38
    • 3042803660 scopus 로고    scopus 로고
    • Rapid evolution of RNA editing sites in a small non-essential plastid gene
    • Fiebig A., Stegemann S., Bock R. Rapid evolution of RNA editing sites in a small non-essential plastid gene. Nucleic Acids Res. 2004, 32:3615-3622.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3615-3622
    • Fiebig, A.1    Stegemann, S.2    Bock, R.3
  • 39
    • 13944249172 scopus 로고    scopus 로고
    • The central role of the green alga Chlamydomonas reinhardtii in revealing the mechanism of state transitions
    • Finazzi G. The central role of the green alga Chlamydomonas reinhardtii in revealing the mechanism of state transitions. J. Exp. Bot. 2005, 56:383-388.
    • (2005) J. Exp. Bot. , vol.56 , pp. 383-388
    • Finazzi, G.1
  • 42
    • 0036208158 scopus 로고    scopus 로고
    • Involvement of state transitions in the switch between linear and cyclic electron flow in Chlamydomonas reinhardtii
    • Finazzi G., Rappaport F., Furia A., Fleischmann M., Rochaix J.D., Zito F., Forti G. Involvement of state transitions in the switch between linear and cyclic electron flow in Chlamydomonas reinhardtii. EMBO Reports 2002, 3:280-285.
    • (2002) EMBO Reports , 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
  • 43
    • 0037450644 scopus 로고    scopus 로고
    • Thylakoid targeting of Tat passenger proteins shows no delta pH dependence in vivo
    • Finazzi G., Chasen C., Wollman F.A., de Vitry C. Thylakoid targeting of Tat passenger proteins shows no delta pH dependence in vivo. EMBO J. 2003, 22:807-815.
    • (2003) EMBO J. , vol.22 , pp. 807-815
    • Finazzi, G.1    Chasen, C.2    Wollman, F.A.3    de Vitry, C.4
  • 44
    • 0033522445 scopus 로고    scopus 로고
    • Molecular cloning of the maize gene crp1 reveals similarity between regulators of mitochondrial and chloroplast gene expression
    • Fisk D.G., Walker M.B., Barkan A. Molecular cloning of the maize gene crp1 reveals similarity between regulators of mitochondrial and chloroplast gene expression. EMBO J. 1999, 18:2621-2630.
    • (1999) EMBO J. , vol.18 , pp. 2621-2630
    • Fisk, D.G.1    Walker, M.B.2    Barkan, A.3
  • 46
    • 0025896455 scopus 로고
    • The "positive-inside rule" applies to thylakoid membrane proteins
    • Gavel Y., Steppuhn J., Herrmann R., von Heijne G. The "positive-inside rule" applies to thylakoid membrane proteins. FEBS Lett. 1991, 282:41-46.
    • (1991) FEBS Lett. , vol.282 , pp. 41-46
    • Gavel, Y.1    Steppuhn, J.2    Herrmann, R.3    von Heijne, G.4
  • 47
    • 0019974543 scopus 로고
    • Evidence for a membrane-bound NADH-plastoquinone-oxidoreductase in Chlamydomonas reinhardii CW-15
    • Godde D. Evidence for a membrane-bound NADH-plastoquinone-oxidoreductase in Chlamydomonas reinhardii CW-15. Arch. Microbiol. 1982, 131:197-202.
    • (1982) Arch. Microbiol. , vol.131 , pp. 197-202
    • Godde, D.1
  • 52
    • 0037462720 scopus 로고    scopus 로고
    • Essential histidine and tryptophan residues in CcsA, a system II polytopic cytochrome c biogenesis protein
    • Hamel P.P., Dreyfuss B.W., Xie Z., Gabilly S.T., Merchant S. Essential histidine and tryptophan residues in CcsA, a system II polytopic cytochrome c biogenesis protein. J. Biol. Chem. 2003, 278:2593-2603.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2593-2603
    • Hamel, P.P.1    Dreyfuss, B.W.2    Xie, Z.3    Gabilly, S.T.4    Merchant, S.5
  • 53
    • 0033513567 scopus 로고    scopus 로고
    • Small cis-acting sequences that specify secondary structures in a chloroplast mRNA are essential for RNA stability and translation
    • Higgs D.C., Shapiro R.S., Kindle K.L., Stern D.B. Small cis-acting sequences that specify secondary structures in a chloroplast mRNA are essential for RNA stability and translation. Mol. Cell. Biol. 1999, 19:8479-8491.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8479-8491
    • Higgs, D.C.1    Shapiro, R.S.2    Kindle, K.L.3    Stern, D.B.4
  • 54
    • 0031465561 scopus 로고    scopus 로고
    • Ccs1, a nuclear gene required for the post-translational assembly of chloroplast c-type cytochromes
    • Inoue K., Dreyfuss B.W., Kindle K.L., Stern D.B., Merchant S., Sodeinde O.A. Ccs1, a nuclear gene required for the post-translational assembly of chloroplast c-type cytochromes. J. Biol. Chem. 1997, 272:31747-31754.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31747-31754
    • Inoue, K.1    Dreyfuss, B.W.2    Kindle, K.L.3    Stern, D.B.4    Merchant, S.5    Sodeinde, O.A.6
  • 60
    • 33745604530 scopus 로고    scopus 로고
    • Cyclic electron flow in C3 plants
    • Joliot P., Joliot A. Cyclic electron flow in C3 plants. Biochim. Biophys. Acta 2006, 1757:362-368.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 362-368
    • Joliot, P.1    Joliot, A.2
  • 61
    • 0001953303 scopus 로고
    • Inhibition of electron transfer and electrogenic reaction in the cytochrome b/f complex by 2-n-nonyl-4-hydroxyquinoline N-oxide (NQNO) and 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB)
    • Jones R.W., Whitmarsh J. Inhibition of electron transfer and electrogenic reaction in the cytochrome b/f complex by 2-n-nonyl-4-hydroxyquinoline N-oxide (NQNO) and 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB). Biochim. Biophys. Acta 1988, 933:258-268.
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 258-268
    • Jones, R.W.1    Whitmarsh, J.2
  • 62
    • 0003651911 scopus 로고    scopus 로고
    • Assembly of the Rieske iron-sulphur protein into the cytochrome bf complex in thylakoid membranes of isolated pea chloroplasts
    • Kapazoglou A., Mould R.M., Gray J.C. Assembly of the Rieske iron-sulphur protein into the cytochrome bf complex in thylakoid membranes of isolated pea chloroplasts. Eur. J. Biochem. 2000, 267:352-360.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 352-360
    • Kapazoglou, A.1    Mould, R.M.2    Gray, J.C.3
  • 64
    • 29944445891 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis in photosynthetic organisms
    • Kessler D., Papenbrock J. Iron-sulfur cluster biosynthesis in photosynthetic organisms. Photosynth. Res. 2005, 86:391-407.
    • (2005) Photosynth. Res. , vol.86 , pp. 391-407
    • Kessler, D.1    Papenbrock, J.2
  • 66
    • 25844505890 scopus 로고    scopus 로고
    • An anomalous distance dependence of intraprotein chlorophyll-carotenoid triplet energy transfer
    • Kim H., Dashdorj N., Zhang H., Yan J., Cramer W.A., Savikhin S. An anomalous distance dependence of intraprotein chlorophyll-carotenoid triplet energy transfer. Biophys. J. 2005, 89:L28-l30.
    • (2005) Biophys. J. , vol.89
    • Kim, H.1    Dashdorj, N.2    Zhang, H.3    Yan, J.4    Cramer, W.A.5    Savikhin, S.6
  • 67
    • 0028324196 scopus 로고
    • Competition among plastoquinol and artificial quinone/quinol couples at the quinol oxidizing site of the cytochrome bf complex
    • Kramer D.M., Joliot A., Joliot P., Crofts A.R. Competition among plastoquinol and artificial quinone/quinol couples at the quinol oxidizing site of the cytochrome bf complex. Biochim. Biophys. Acta 1994, 1184:251-262.
    • (1994) Biochim. Biophys. Acta , vol.1184 , pp. 251-262
    • Kramer, D.M.1    Joliot, A.2    Joliot, P.3    Crofts, A.R.4
  • 68
    • 3042804076 scopus 로고    scopus 로고
    • Dynamic flexibility in the light reactions of photosynthesis governed by both electron and proton transfer reactions
    • Kramer D.M., Avenson T.J., Edwards G.E. Dynamic flexibility in the light reactions of photosynthesis governed by both electron and proton transfer reactions. Trends Plant Sci. 2004, 9:349-357.
    • (2004) Trends Plant Sci. , vol.9 , pp. 349-357
    • Kramer, D.M.1    Avenson, T.J.2    Edwards, G.E.3
  • 69
    • 0031875674 scopus 로고    scopus 로고
    • Molecular mechanisms of cytochrome c biogenesis: Three distinct systems
    • Kranz R., Lill R., Goldman B., Bonnard G., Merchant S. Molecular mechanisms of cytochrome c biogenesis: Three distinct systems. Mol. Microbiol. 1998, 29:383-396.
    • (1998) Mol. Microbiol. , vol.29 , pp. 383-396
    • Kranz, R.1    Lill, R.2    Goldman, B.3    Bonnard, G.4    Merchant, S.5
  • 70
    • 0028178516 scopus 로고
    • 6f complexes: An approach using genetic transformation of the green alga Chlamydomonas reinhardtii
    • 6f complexes: An approach using genetic transformation of the green alga Chlamydomonas reinhardtii. EMBO J. 1994, 13:1019-1027.
    • (1994) EMBO J. , vol.13 , pp. 1019-1027
    • Kuras, R.1    Wollman, F.A.2
  • 71
    • 0028856323 scopus 로고
    • Maturation of pre-apocytochrome f in vivo. A site-directed mutagenesis study in Chlamydomonas reinhardtii
    • Kuras R., Büschlen S., Wollman F.A. Maturation of pre-apocytochrome f in vivo. A site-directed mutagenesis study in Chlamydomonas reinhardtii. J. Biol. Chem. 1995, 270:27797-27803.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27797-27803
    • Kuras, R.1    Büschlen, S.2    Wollman, F.A.3
  • 73
    • 34547407925 scopus 로고    scopus 로고
    • A specific c-type cytochrome maturation system is required for oxygenic photosynthesis
    • Kuras R., Saint-Marcoux D., Wollman F.A., de Vitry C. A specific c-type cytochrome maturation system is required for oxygenic photosynthesis. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:9906-9910.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 9906-9910
    • Kuras, R.1    Saint-Marcoux, D.2    Wollman, F.A.3    de Vitry, C.4
  • 75
    • 0002565747 scopus 로고
    • 6 in an algal mutant lacking photosystem I centers
    • 6 in an algal mutant lacking photosystem I centers. Biochim. Biophys. Acta 1983, 725:25-33.
    • (1983) Biochim. Biophys. Acta , vol.725 , pp. 25-33
    • Lavergne, J.1
  • 78
    • 33644859551 scopus 로고    scopus 로고
    • HCF153, a novel nuclear-encoded factor necessary during a post-translational step in biogenesis of the cytochrome bf complex
    • Lennartz K., Bossmann S., Westhoff P., Bechtold N., Meierhoff K. HCF153, a novel nuclear-encoded factor necessary during a post-translational step in biogenesis of the cytochrome bf complex. Plant J. 2006, 45:101-112.
    • (2006) Plant J. , vol.45 , pp. 101-112
    • Lennartz, K.1    Bossmann, S.2    Westhoff, P.3    Bechtold, N.4    Meierhoff, K.5
  • 82
    • 0141563600 scopus 로고    scopus 로고
    • Knock-out of the genes coding for the Rieske protein and the ATP-synthase delta-subunit of Arabidopsis. Effects on photosynthesis, thylakoid protein composition, and nuclear chloroplast gene expression
    • Maiwald D., Dietzmann A., Jahns P., Pesaresi P., Joliot P., Joliot A., Levin J.Z., Salamini F., Leister D. Knock-out of the genes coding for the Rieske protein and the ATP-synthase delta-subunit of Arabidopsis. Effects on photosynthesis, thylakoid protein composition, and nuclear chloroplast gene expression. Plant Physiol. 2003, 133:191-202.
    • (2003) Plant Physiol. , vol.133 , pp. 191-202
    • Maiwald, D.1    Dietzmann, A.2    Jahns, P.3    Pesaresi, P.4    Joliot, P.5    Joliot, A.6    Levin, J.Z.7    Salamini, F.8    Leister, D.9
  • 84
    • 0000466115 scopus 로고
    • 6f complexes of photosynthetic membranes
    • 6f complexes of photosynthetic membranes. Photosynth. Res. 1992, 33:121-136.
    • (1992) Photosynth. Res. , vol.33 , pp. 121-136
    • Malkin, R.1
  • 88
    • 0038457836 scopus 로고    scopus 로고
    • HCF152, an Arabidopsis RNA binding pentatricopeptide repeat protein involved in the processing of chloroplast psbB-psbT-psbH-petB-petD RNAs
    • Meierhoff K., Felder S., Nakamura T., Bechtold N., Schuster G. HCF152, an Arabidopsis RNA binding pentatricopeptide repeat protein involved in the processing of chloroplast psbB-psbT-psbH-petB-petD RNAs. Plant Cell 2003, 15:1480-1495.
    • (2003) Plant Cell , vol.15 , pp. 1480-1495
    • Meierhoff, K.1    Felder, S.2    Nakamura, T.3    Bechtold, N.4    Schuster, G.5
  • 90
    • 27244455478 scopus 로고    scopus 로고
    • The light reactions: A guide to recent acquisitions for the picture gallery
    • Merchant S., Sawaya M.R. The light reactions: A guide to recent acquisitions for the picture gallery. Plant Cell 2005, 17:648-663.
    • (2005) Plant Cell , vol.17 , pp. 648-663
    • Merchant, S.1    Sawaya, M.R.2
  • 91
    • 0016690480 scopus 로고
    • 1 complex in the respiratory chain: Protonmotive ubiquinone cycle
    • 1 complex in the respiratory chain: Protonmotive ubiquinone cycle. FEBS Lett. 1975, 56:1-6.
    • (1975) FEBS Lett. , vol.56 , pp. 1-6
    • Mitchell, P.1
  • 92
    • 28544451847 scopus 로고    scopus 로고
    • Effects of light intensity on cyclic electron flow around PSI and its relationship to non-photochemical quenching of Chl fluorescence in tobacco leaves
    • Miyake C., Horiguchi S., Makino A., Shinzaki Y., Yamamoto H., Tomizawa K. Effects of light intensity on cyclic electron flow around PSI and its relationship to non-photochemical quenching of Chl fluorescence in tobacco leaves. Plant Cell Physiol. 2005, 46:1819-1830.
    • (2005) Plant Cell Physiol. , vol.46 , pp. 1819-1830
    • Miyake, C.1    Horiguchi, S.2    Makino, A.3    Shinzaki, Y.4    Yamamoto, H.5    Tomizawa, K.6
  • 93
    • 18444370287 scopus 로고    scopus 로고
    • 2 response of cyclic electron flow around PSI (CEF-PSI) in tobacco leaves - relative electron fluxes through PSI and PSII determine the magnitude of non-photochemical quenching (NPQ) of Chl fluorescence
    • 2 response of cyclic electron flow around PSI (CEF-PSI) in tobacco leaves - relative electron fluxes through PSI and PSII determine the magnitude of non-photochemical quenching (NPQ) of Chl fluorescence. Plant Cell Physiol. 2005, 46:629-637.
    • (2005) Plant Cell Physiol. , vol.46 , pp. 629-637
    • Miyake, C.1    Miyata, M.2    Shinzaki, Y.3    Tomizawa, K.4
  • 95
    • 33845939598 scopus 로고    scopus 로고
    • HCF164 receives reducing equivalents from stromal thioredoxin across the thylakoid membrane and mediates reduction of target proteins in the thylakoid lumen
    • Motohashi K., Hisabori T. HCF164 receives reducing equivalents from stromal thioredoxin across the thylakoid membrane and mediates reduction of target proteins in the thylakoid lumen. J. Biol. Chem. 2006, 281:35039-35047.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35039-35047
    • Motohashi, K.1    Hisabori, T.2
  • 96
    • 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., Shikanai T. PGR5 is involved in cyclic electron flow around photosystem I and is essential for photoprotection in Arabidopsis. Cell 2002, 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
  • 98
    • 20444443144 scopus 로고    scopus 로고
    • A spontaneous tRNA suppressor of a mutation in the Chlamydomonas reinhardtii nuclear MCD1 gene required for stability of the chloroplast petD mRNA
    • Murakami S., Kuehnle K., Stern D.B. A spontaneous tRNA suppressor of a mutation in the Chlamydomonas reinhardtii nuclear MCD1 gene required for stability of the chloroplast petD mRNA. Nucleic Acids Res. 2005, 33:3372-3380.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 3372-3380
    • Murakami, S.1    Kuehnle, K.2    Stern, D.B.3
  • 99
    • 0033868211 scopus 로고    scopus 로고
    • Assembly of chloroplast cytochromes b and c
    • Nakamoto S.S., Hamel P., Merchant S. Assembly of chloroplast cytochromes b and c. Biochimie 2000, 82:603-614.
    • (2000) Biochimie , vol.82 , pp. 603-614
    • Nakamoto, S.S.1    Hamel, P.2    Merchant, S.3
  • 100
    • 0142088891 scopus 로고    scopus 로고
    • RNA-binding properties of HCF152, an Arabidopsis PPR protein involved in the processing of chloroplast RNA
    • Nakamura T., Meierhoff K., Westhoff P., Schuster G. RNA-binding properties of HCF152, an Arabidopsis PPR protein involved in the processing of chloroplast RNA. Eur. J. Biochem. 2003, 270:4070-4081.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4070-4081
    • Nakamura, T.1    Meierhoff, K.2    Westhoff, P.3    Schuster, G.4
  • 101
    • 15444378936 scopus 로고    scopus 로고
    • 6 arginine 214 of Synechococcus sp. PCC 7002, a key residue for quinone-reductase site function and turnover of the cytochrome bf complex
    • 6 arginine 214 of Synechococcus sp. PCC 7002, a key residue for quinone-reductase site function and turnover of the cytochrome bf complex. J. Biol. Chem. 2005, 280:10395-10402.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10395-10402
    • Nelson, M.E.1    Finazzi, G.2    Wang, Q.J.3    Middleton-Zarka, K.A.4    Whitmarsh, J.5    Kallas, T.6
  • 102
    • 0025845648 scopus 로고
    • A gene homologous to the subunit-2 gene of NADH dehydrogenase is essential to inorganic carbon transport of Synechocystis PCC6803
    • Ogawa T. A gene homologous to the subunit-2 gene of NADH dehydrogenase is essential to inorganic carbon transport of Synechocystis PCC6803. Proc. Natl. Acad. Sci. U. S. A. 1991, 88:4275-4279.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 4275-4279
    • Ogawa, T.1
  • 104
    • 0031153994 scopus 로고    scopus 로고
    • Light-stimulated degradation of an unassembled Rieske FeS protein by a thylakoid-bound protease: The possible role of the FtsH protease
    • Ostersetzer O., Adam Z. Light-stimulated degradation of an unassembled Rieske FeS protein by a thylakoid-bound protease: The possible role of the FtsH protease. Plant Cell 1997, 9:957-965.
    • (1997) Plant Cell , vol.9 , pp. 957-965
    • Ostersetzer, O.1    Adam, Z.2
  • 110
    • 33846234254 scopus 로고    scopus 로고
    • Heme concentration dependence and metalloporphyrin inhibition of the system I and II cytochrome c assembly pathways
    • Richard-Fogal C.L., Frawley E.R., Feissner R.E., Kranz R.G. Heme concentration dependence and metalloporphyrin inhibition of the system I and II cytochrome c assembly pathways. J. Bacteriol. 2007, 189:455-463.
    • (2007) J. Bacteriol. , vol.189 , pp. 455-463
    • Richard-Fogal, C.L.1    Frawley, E.R.2    Feissner, R.E.3    Kranz, R.G.4
  • 111
    • 0035929632 scopus 로고    scopus 로고
    • In vitro reconstitution of insertion and processing of cytochrome f in a homologous chloroplast translation system
    • Rohl T., van Wijk K.J. In vitro reconstitution of insertion and processing of cytochrome f in a homologous chloroplast translation system. J. Biol. Chem. 2001, 276:35465-35472.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35465-35472
    • Rohl, T.1    van Wijk, K.J.2
  • 112
    • 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
    • Rumeau D., Becuwe-Linka N., Beyly A., Louwagie M., Garin J., Peltier G. New subunits NDH-M, -N, and -O, encoded by nuclear genes, are essential for plastid Ndh complex functioning in higher plants. Plant Cell 2005, 17:219-232.
    • (2005) Plant Cell , vol.17 , pp. 219-232
    • Rumeau, D.1    Becuwe-Linka, N.2    Beyly, A.3    Louwagie, M.4    Garin, J.5    Peltier, G.6
  • 113
    • 33645664198 scopus 로고    scopus 로고
    • Nuclear suppressors define three factors that participate in both 5′ and 3′ end processing of mRNAs in Chlamydomonas chloroplasts
    • Rymarquis L.A., Higgs D.C., Stern D.B. Nuclear suppressors define three factors that participate in both 5′ and 3′ end processing of mRNAs in Chlamydomonas chloroplasts. Plant J. 2006, 46:448-461.
    • (2006) Plant J. , vol.46 , pp. 448-461
    • Rymarquis, L.A.1    Higgs, D.C.2    Stern, D.B.3
  • 114
    • 0032477715 scopus 로고    scopus 로고
    • The plastid ndh genes code for an NADH-specific dehydrogenase: Isolation of a complex I analogue from pea thylakoid membranes
    • Sazanov L.A., Burrows P.A., Nixon P.J. The plastid ndh genes code for an NADH-specific dehydrogenase: Isolation of a complex I analogue from pea thylakoid membranes. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:1319-1324.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 1319-1324
    • Sazanov, L.A.1    Burrows, P.A.2    Nixon, P.J.3
  • 120
    • 33745955558 scopus 로고    scopus 로고
    • 6f complex prevent light-induced expression of nuclear genes involved in chlorophyll biosynthesis
    • 6f complex prevent light-induced expression of nuclear genes involved in chlorophyll biosynthesis. Plant Physiol. 2006, 141:1128-1137.
    • (2006) Plant Physiol. , vol.141 , pp. 1128-1137
    • Shao, N.1    Vallon, O.2    Dent, R.3    Niyogi, K.K.4    Beck, C.F.5
  • 122
    • 4143054902 scopus 로고    scopus 로고
    • Cytochrome bc complexes: A common core of structure and function surrounded by diversity in the outlying provinces
    • Smith J.L., Zhang H., Yan J., Kurisu G., Cramer W.A. Cytochrome bc complexes: A common core of structure and function surrounded by diversity in the outlying provinces. Curr. Opin. Struct. Biol. 2004, 14:432-439.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 432-439
    • Smith, J.L.1    Zhang, H.2    Yan, J.3    Kurisu, G.4    Cramer, W.A.5
  • 127
    • 10944268718 scopus 로고    scopus 로고
    • Function of a PscD subunit in a homodimeric reaction center complex of the photosynthetic green sulfur bacterium Chlorobium tepidum studied by insertional gene inactivation. Regulation of energy transfer and ferredoxin-mediated NADP+ reduction on the cytoplasmic side
    • Tsukatani Y., Miyamoto R., Itoh S., Oh-Oka H. Function of a PscD subunit in a homodimeric reaction center complex of the photosynthetic green sulfur bacterium Chlorobium tepidum studied by insertional gene inactivation. Regulation of energy transfer and ferredoxin-mediated NADP+ reduction on the cytoplasmic side. J. Biol. Chem. 2004, 279:51122-51130.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51122-51130
    • Tsukatani, Y.1    Miyamoto, R.2    Itoh, S.3    Oh-Oka, H.4
  • 132
    • 0007691921 scopus 로고    scopus 로고
    • 6f complexes
    • Kluwer Academic Publishers, The Netherlands, J.D. Rochaix, M. Goldschmidt-Clermont, S. Merchant (Eds.)
    • 6f complexes. The Molecular Biology of Chloroplasts and Mitochondria in Chlamydomonas 1998, 459-476. Kluwer Academic Publishers, The Netherlands. J.D. Rochaix, M. Goldschmidt-Clermont, S. Merchant (Eds.).
    • (1998) The Molecular Biology of Chloroplasts and Mitochondria in Chlamydomonas , pp. 459-476
    • Wollman, F.A.1
  • 133
    • 0035898532 scopus 로고    scopus 로고
    • State transitions reveal the dynamics and flexibility of the photosynthetic apparatus
    • Wollman F.A. State transitions reveal the dynamics and flexibility of the photosynthetic apparatus. EMBO J. 2001, 20:3623-3630.
    • (2001) EMBO J. , vol.20 , pp. 3623-3630
    • Wollman, F.A.1
  • 134
    • 0002827118 scopus 로고
    • 6f mutants from Chlamydomonas reinhardtii which lack quinone-binding proteins
    • 6f mutants from Chlamydomonas reinhardtii which lack quinone-binding proteins. Biochim. Biophys. Acta 1988, 933:85-94.
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 85-94
    • Wollman, F.A.1    Lemaire, C.2
  • 135
    • 0032910388 scopus 로고    scopus 로고
    • The biogenesis and assembly of photosynthetic proteins in thylakoid membranes
    • Wollman F.A., Minai L., Nechustai R. The biogenesis and assembly of photosynthetic proteins in thylakoid membranes. Biochim. Biophys. Acta 1999, 1411:21-85.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 21-85
    • Wollman, F.A.1    Minai, L.2    Nechustai, R.3
  • 136
    • 0034810970 scopus 로고    scopus 로고
    • TCA1, a single nuclear-encoded translational activator specific for petA mRNA in Chlamydomonas reinhardtii chloroplast
    • Wostrikoff K., Choquet Y., Wollman F.A., Girard-Bascou J. TCA1, a single nuclear-encoded translational activator specific for petA mRNA in Chlamydomonas reinhardtii chloroplast. Genetics 2001, 159:119-132.
    • (2001) Genetics , vol.159 , pp. 119-132
    • Wostrikoff, K.1    Choquet, Y.2    Wollman, F.A.3    Girard-Bascou, J.4
  • 139
    • 0029867910 scopus 로고    scopus 로고
    • The plastid-encoded ccsA gene is required for heme attachment to chloroplast c-type cytochromes
    • Xie Z., Merchant S. The plastid-encoded ccsA gene is required for heme attachment to chloroplast c-type cytochromes. J. Biol. Chem. 1996, 271:4632-4639.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4632-4639
    • Xie, Z.1    Merchant, S.2
  • 140
    • 0032311168 scopus 로고    scopus 로고
    • A novel pathway for cytochrome c biogenesis in chloroplasts
    • Xie Z., Merchant S. A novel pathway for cytochrome c biogenesis in chloroplasts. Biochim. Biophys. Acta 1998, 1365:309-318.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 309-318
    • Xie, Z.1    Merchant, S.2
  • 141
    • 0031951970 scopus 로고    scopus 로고
    • Genetic analysis of chloroplast c-type cytochrome assembly in Chlamydomonas reinhardtii: One chloroplast locus and at least four nuclear loci are required for heme attachment
    • Xie Z., Culler D., Dreyfuss B.W., Kuras R., Wollman F.A., Girard-Bascou J., Merchant S. Genetic analysis of chloroplast c-type cytochrome assembly in Chlamydomonas reinhardtii: One chloroplast locus and at least four nuclear loci are required for heme attachment. Genetics 1998, 148:681-692.
    • (1998) Genetics , vol.148 , pp. 681-692
    • Xie, Z.1    Culler, D.2    Dreyfuss, B.W.3    Kuras, R.4    Wollman, F.A.5    Girard-Bascou, J.6    Merchant, S.7
  • 142
    • 33750601493 scopus 로고    scopus 로고
    • Ferredoxin limits cyclic electron flow around PSI (CEF-PSI) in higher plants stimulation of CEF-PSI enhances non-photochemical quenching of Chl fluorescence in transplastomic tobacco
    • Yamamoto H., Kato H., Shinzaki Y., Horiguchi S., Shikanai T., Hase T., Endo T., Nishioka M., Makino A., Tomizawa K., Miyake C. Ferredoxin limits cyclic electron flow around PSI (CEF-PSI) in higher plants stimulation of CEF-PSI enhances non-photochemical quenching of Chl fluorescence in transplastomic tobacco. Plant Cell Physiol. 2006, 47:1355-1371.
    • (2006) Plant Cell Physiol. , vol.47 , pp. 1355-1371
    • Yamamoto, H.1    Kato, H.2    Shinzaki, Y.3    Horiguchi, S.4    Shikanai, T.5    Hase, T.6    Endo, T.7    Nishioka, M.8    Makino, A.9    Tomizawa, K.10    Miyake, C.11
  • 145
    • 0032502756 scopus 로고    scopus 로고
    • Studies of the cytochrome subunits of menaquinone:cytochrome c reductase (bc complex) of Bacillus subtilis. Evidence for the covalent attachment of heme to the cytochrome b subunit
    • Yu J., Le Brun N.E. Studies of the cytochrome subunits of menaquinone:cytochrome c reductase (bc complex) of Bacillus subtilis. Evidence for the covalent attachment of heme to the cytochrome b subunit. J. Biol. Chem. 1998, 273:8860-8866.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8860-8866
    • Yu, J.1    Le Brun, N.E.2
  • 148
    • 0033556297 scopus 로고    scopus 로고
    • 6f complex of oxygenic photosynthesis protects against oxygen damage
    • 6f complex of oxygenic photosynthesis protects against oxygen damage. J. Biol. Chem. 1999, 274:1581-1587.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1581-1587
    • Zhang, H.1    Huang, D.2    Cramer, W.A.3
  • 152
    • 0037023743 scopus 로고    scopus 로고
    • 6f complex of Chlamydomonas reinhardtii: Structural implications and consequences on state transitions
    • 6f complex of Chlamydomonas reinhardtii: Structural implications and consequences on state transitions. J. Biol. Chem. 2002, 277:12446-12455.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12446-12455
    • Zito, F.1    Vinh, J.2    Popot, J.L.3    Finazzi, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.