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Volumn 53, Issue , 2002, Pages 523-550

Chlororespiration

Author keywords

Alternative oxidase; Chloroplasts; Complex I; Photosynthesis; Respiration

Indexed keywords

CHLOROPLAST; ELECTRON TRANSPORT; OXIDATION REDUCTION REACTION; PHOTOSYNTHESIS; PHYSIOLOGY; REVIEW;

EID: 0037001968     PISSN: 15435008     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.arplant.53.100301.135242     Document Type: Review
Times cited : (342)

References (153)
  • 1
    • 36849155728 scopus 로고
    • Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems
    • Allen IF, Bennett J, Steinback KE, Amtzen CJ. 1981. Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems. Nature 291:25-29
    • (1981) Nature , vol.291 , pp. 25-29
    • Allen, I.F.1    Bennett, J.2    Steinback, K.E.3    Arntzen, C.J.4
  • 2
    • 0016809780 scopus 로고
    • Regulation of ferredoxin-catalyzed photosynthetic phosphorylations
    • Amon DI, Chain RK. 1975. Regulation of ferredoxin-catalyzed photosynthetic phosphorylations. Proc. Natl. Acad. Sci. USA 72:4961-65
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 4961-4965
    • Arnon, D.I.1    Chain, R.K.2
  • 4
    • 0026500778 scopus 로고
    • Identification of mitochondrial proteins in membrane preparations from Chlamydomonas reinhardtii
    • Atteia A, de Vitry C, Pierre Y, Popot J-L. 1992. Identification of mitochondrial proteins in membrane preparations from Chlamydomonas reinhardtii. J. Biol. Chem. 267:226-34
    • (1992) J. Biol. Chem. , vol.267 , pp. 226-234
    • Atteia, A.1    De Vitry, C.2    Pierre, Y.3    Popot, J.-L.4
  • 5
    • 0034730965 scopus 로고    scopus 로고
    • Flexibility in photosynthetic electron transport: A newly identified chloroplast oxidase involved in chlororespiration. Discussion
    • Barber J, Peltier G, Niyogi K, Foyer CH, Laisk A, Matthijs HCP. 2000. Flexibility in photosynthetic electron transport: a newly identified chloroplast oxidase involved in chlororespiration. Discussion. Philos. Trans. R. Soc. London Ser. B 355:1453-54
    • (2000) Philos. Trans. R. Soc. London Ser. B , vol.355 , pp. 1453-1454
    • Barber, J.1    Peltier, G.2    Niyogi, K.3    Foyer, C.H.4    Laisk, A.5    Matthijs, H.C.P.6
  • 6
    • 0028944579 scopus 로고
    • Cyclic photophosphorylation and electron transport
    • Bendall DS, Manasse RS. 1995. Cyclic photophosphorylation and electron transport. Biochim. Biophys. Acta 1229:23-38
    • (1995) Biochim. Biophys. Acta , vol.1229 , pp. 23-38
    • Bendall, D.S.1    Manasse, R.S.2
  • 7
    • 0001138725 scopus 로고
    • Protein phosphorylation in green plant chloroplasts
    • Bennett J. 1991. Protein phosphorylation in green plant chloroplasts. Annu. Rev. Plant Physiol. Plant Mol. Biol. 42:281-311
    • (1991) Annu. Rev. Plant Physiol. Plant Mol. Biol , vol.42 , pp. 281-311
    • Bennett, J.1
  • 8
    • 0000454893 scopus 로고
    • Evidence for a respiratory chain in the chloroplast
    • Bennoun P. 1982. Evidence for a respiratory chain in the chloroplast. Proc. Natl. Acad. Sci. USA 79:4352-56
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 4352-4356
    • Bennoun, P.1
  • 9
    • 0020514145 scopus 로고
    • Effects of mutations and of ionophore on chlororespiration in Chlamydomonas reinhardtii
    • Bennoun P. 1983. Effects of mutations and of ionophore on chlororespiration in Chlamydomonas reinhardtii. FEBS Lett. 156:363-65
    • (1983) FEBS Lett. , vol.156 , pp. 363-365
    • Bennoun, P.1
  • 10
    • 0028241770 scopus 로고
    • Chlororespiration revisited: Mitochondrial-plastid interactions in Chlamydomonas
    • Bennoun P. 1994. Chlororespiration revisited: mitochondrial-plastid interactions in Chlamydomonas. Biochim. Biophys. Acta 1186:59-66
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 59-66
    • Bennoun, P.1
  • 11
    • 0001180548 scopus 로고    scopus 로고
    • Chlororespiration, sixteen years later
    • ed. J-D Rochaix, M Goldschmidt-Clermont, S Merchant. Dordrecht, The Neth.: Kluwer
    • Bennoun P. 1998. Chlororespiration, sixteen years later. In The Molecular Biology of Chloroplasts and Mitochondria in Chlamydomonas, ed. J-D Rochaix, M Goldschmidt-Clermont, S Merchant, pp. 675-83. Dordrecht, The Neth.: Kluwer
    • (1998) The Molecular Biology of Chloroplasts and Mitochondria in Chlamydomonas , pp. 675-683
    • Bennoun, P.1
  • 12
    • 0002587507 scopus 로고
    • Studies on the expression of NDH-H, a subunit of the NAD(P) H-plastoquinone oxidoreductase of higher plant chloroplasts
    • Berger S, Ellersiek U, Westhoff P, Steinmuller K. 1993. Studies on the expression of NDH-H, a subunit of the NAD(P) H-plastoquinone oxidoreductase of higher plant chloroplasts. Planta 190:25-31
    • (1993) Planta , vol.190 , pp. 25-31
    • Berger, S.1    Ellersiek, U.2    Westhoff, P.3    Steinmuller, K.4
  • 13
    • 0032516058 scopus 로고    scopus 로고
    • Isolation of mutants of the Arabidopsis thaliana alternative oxidase (ubiquinol:oxygen oxidoreductase) resistant to salicylhydroxamic acid
    • Berthold DA. 1998. Isolation of mutants of the Arabidopsis thaliana alternative oxidase (ubiquinol:oxygen oxidoreductase) resistant to salicylhydroxamic acid. Biochim. Biophys. Acta 1364:73-83
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 73-83
    • Berthold, D.A.1
  • 14
    • 0028833998 scopus 로고
    • Evidence for the operation of a cyanide-sensitive oxidase in chlororespiration in the thylakoids of the chlorophyll c-containing alga Pleurochloris meiringensis (Xanthophyceae)
    • Büchel C, Garab G. 1995. Evidence for the operation of a cyanide-sensitive oxidase in chlororespiration in the thylakoids of the chlorophyll c-containing alga Pleurochloris meiringensis (Xanthophyceae). Planta 197:69-75
    • (1995) Planta , vol.197 , pp. 69-75
    • Büchel, C.1    Garab, G.2
  • 15
    • 0002634660 scopus 로고
    • Wavelength-independent state transitions and light-regulated chlororespiration as mechanisms to control the energy status in the chloroplast of Pleurochloris meiringensis
    • Büchel C, Wilhelm C. 1990. Wavelength-independent state transitions and light-regulated chlororespiration as mechanisms to control the energy status in the chloroplast of Pleurochloris meiringensis. Plant Physiol. Biochem. 28:307-14
    • (1990) Plant Physiol. Biochem. , vol.28 , pp. 307-314
    • Büchel, C.1    Wilhelm, C.2
  • 16
    • 0025169242 scopus 로고
    • ATP control on state transitions in vivo in Chlamydomonas reinhardtii
    • Bulté L, Gans P, Rebeille F, Wollman F-A. 1990. ATP control on state transitions in vivo in Chlamydomonas reinhardtii. Biochim. Biophys. Acta 1020:72-80
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 72-80
    • Bulté, L.1    Gans, P.2    Rebeille, F.3    Wollman, F.-A.4
  • 17
    • 0032481317 scopus 로고    scopus 로고
    • Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes
    • Burrows PA, Sazanov LA, Svab Z, Maliga P, Nixon PJ. 1998. Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes. EMBO J. 17:868-76
    • (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
  • 18
    • 0035211544 scopus 로고    scopus 로고
    • A plastid terminal oxidase comes to light: Implications for carotenoid biosynthesis and chlororespiration
    • Carol P, Kuntz M. 2001. A plastid terminal oxidase comes to light: implications for carotenoid biosynthesis and chlororespiration. Trends Plant Sci. 6:31-36
    • (2001) Trends Plant Sci. , vol.6 , pp. 31-36
    • Carol, P.1    Kuntz, M.2
  • 19
    • 0032697005 scopus 로고    scopus 로고
    • Mutations in the Arabidopsis gene immutans cause a variegated phenotype by inactivating a chloroplast terminal oxidase associated with phytoene desaturation
    • Carol R Stevenson D, Bisanz C, Breitenbach J, Sandmann G, et al. 1999. Mutations in the Arabidopsis gene immutans cause a variegated phenotype by inactivating a chloroplast terminal oxidase associated with phytoene desaturation. Plant Cell 11:57-68
    • (1999) Plant Cell , vol.11 , pp. 57-68
    • Carol, R.1    Stevenson, D.2    Bisanz, C.3    Breitenbach, J.4    Sandmann, G.5
  • 20
    • 0035099626 scopus 로고    scopus 로고
    • Hydrogen peroxide mediates the induction of chloroplastic Ndh complex under photooxidative stress in barley
    • Casano LM, Martin M, Sabater B. 2001. Hydrogen peroxide mediates the induction of chloroplastic Ndh complex under photooxidative stress in barley. Plant Physiol. 125:1450-58
    • (2001) Plant Physiol. , vol.125 , pp. 1450-1458
    • Casano, L.M.1    Martin, M.2    Sabater, B.3
  • 21
    • 0033550215 scopus 로고    scopus 로고
    • Leaf age- and paraquat concentration-dependent effects on the levels of enzymes protecting against photooxidative stress
    • Casano LM, Martin M, Zapata JM, Sabater B. 1999. Leaf age- and paraquat concentration-dependent effects on the levels of enzymes protecting against photooxidative stress. Plant Sci. 149:13-22
    • (1999) Plant Sci. , vol.149 , pp. 13-22
    • Casano, L.M.1    Martin, M.2    Zapata, J.M.3    Sabater, B.4
  • 22
    • 0033978632 scopus 로고    scopus 로고
    • Chlororespiration and poising of cyclic electron transport - Plastoquinone as electron transporter between thylakoid NADH dehydrogenase and peroxidase
    • Casano LM, Zapata JM, Martin M, Sabater B. 2000. Chlororespiration and poising of cyclic electron transport - plastoquinone as electron transporter between thylakoid NADH dehydrogenase and peroxidase. J. Biol. Chem. 275:942-48
    • (2000) J. Biol. Chem. , vol.275 , pp. 942-948
    • Casano, L.M.1    Zapata, J.M.2    Martin, M.3    Sabater, B.4
  • 23
    • 0031440186 scopus 로고    scopus 로고
    • Expression of the plastid ndhF gene product in photosynthetic and non-photosynthetic tissues of developing barley seedlings
    • Catala R, Sabater B, Guera A. 1997. Expression of the plastid ndhF gene product in photosynthetic and non-photosynthetic tissues of developing barley seedlings. Plant Cell Physiol. 38:1382-88
    • (1997) Plant Cell Physiol. , vol.38 , pp. 1382-1388
    • Catala, R.1    Sabater, B.2    Guera, A.3
  • 24
    • 0013356214 scopus 로고
    • Glucose respiration in the intact chloroplast of Chlamydomonas reinhardtii
    • Chen CG, Gibbs M. 1991. Glucose respiration in the intact chloroplast of Chlamydomonas reinhardtii. Plant Physiol. 95:82-87
    • (1991) Plant Physiol. , vol.95 , pp. 82-87
    • Chen, C.G.1    Gibbs, M.2
  • 25
    • 0000914341 scopus 로고
    • Photosystern I cyclic electron transport - Measurement of ferredoxin-plastoquinone reductase activity
    • Cleland RE, Bendall DS. 1992. Photosystern I cyclic electron transport - measurement of ferredoxin-plastoquinone reductase activity. Photosynth. Res. 34:409-18
    • (1992) Photosynth. Res. , vol.34 , pp. 409-418
    • Cleland, R.E.1    Bendall, D.S.2
  • 26
    • 0033978251 scopus 로고    scopus 로고
    • Succinate: Quinol oxidoreductases in the cyanobacterium Synechocystis sp. strain PCC 6803: Presence and function in metabolism and electron transport
    • Cooley JW, Howitt CA, Vermaas WF. 2000. Succinate: quinol oxidoreductases in the cyanobacterium Synechocystis sp. strain PCC 6803: presence and function in metabolism and electron transport. J. Bacteriol. 182:714-22
    • (2000) J. Bacteriol. , vol.182 , pp. 714-722
    • Cooley, J.W.1    Howitt, C.A.2    Vermaas, W.F.3
  • 27
    • 0034977905 scopus 로고    scopus 로고
    • Succinate dehydrogenase and other respiratory pathways in thylakoid membranes of Synechocystis sp. strain PCC 6803: Capacity comparisons and physiological function
    • Cooley JW, Vermaas WFJ. 2001. Succinate dehydrogenase and other respiratory pathways in thylakoid membranes of Synechocystis sp. strain PCC 6803: capacity comparisons and physiological function. J. Bacteriol. 183:4251-58
    • (2001) J. Bacteriol. , vol.183 , pp. 4251-4258
    • Cooley, J.W.1    Vermaas, W.F.J.2
  • 28
    • 0031883125 scopus 로고    scopus 로고
    • Reduction of the plastoquinone pool by exogenous NADH and NADPH in higher plant chloroplasts - Characterization of a NAD(P)H-plastoquinone oxidoreductase activity
    • Corneille S, Cournac L, Guedeney G, Havaux M, Peltier G. 1998. Reduction of the plastoquinone pool by exogenous NADH and NADPH in higher plant chloroplasts - characterization of a NAD(P)H-plastoquinone oxidoreductase activity. Biochim. Biophys. Acta 1363:59-69
    • (1998) Biochim. Biophys. Acta , vol.1363 , pp. 59-69
    • Corneille, S.1    Cournac, L.2    Guedeney, G.3    Havaux, M.4    Peltier, G.5
  • 29
    • 0001865346 scopus 로고    scopus 로고
    • Non-photochemical reduction of intersystem electron carriers in chloroplasts of higher plants and algae
    • ed. G Garab. Dordrecht, The Neth.: Kluwer
    • Cournac L, Guedeney G, Joët T, Rumeau D, Latouche G, et al. 1998. Non-photochemical reduction of intersystem electron carriers in chloroplasts of higher plants and algae. In Photosynthesis: Mechanism and Effects, ed. G Garab, pp. 1877-82. Dordrecht, The Neth.: Kluwer
    • (1998) Photosynthesis: Mechanism and Effects , pp. 1877-1882
    • Cournac, L.1    Guedeney, G.2    Joët, T.3    Rumeau, D.4    Latouche, G.5
  • 30
    • 0034730965 scopus 로고    scopus 로고
    • Flexibility in photosynthetic electron transport: A newly identified chloroplast oxidase involved in chlororespiration
    • Cournac L, Josse EM, Joët T, Rumeau D, Redding K, et al. 2000. Flexibility in photosynthetic electron transport: a newly identified chloroplast oxidase involved in chlororespiration. Philos. Trans. R. Soc. London Ser. B 355:1447-53
    • (2000) Philos. Trans. R. Soc. London Ser. B , vol.355 , pp. 1447-1453
    • Cournac, L.1    Josse, E.M.2    Joët, T.3    Rumeau, D.4    Redding, K.5
  • 32
    • 0034625412 scopus 로고    scopus 로고
    • Electron flow between photosystem II and oxygen in chloroplasts of photosystem I-deficient algae is mediated by a quinol oxidase involved in chlororespiration
    • Cournac L, Redding K, Ravenel J, Rumeau D, Josse EM, et al. 2000. Electron flow between photosystem II and oxygen in chloroplasts of photosystem I-deficient algae is mediated by a quinol oxidase involved in chlororespiration. J. Biol. Chem. 275:17256-62
    • (2000) J. Biol. Chem. , vol.275 , pp. 17256-17262
    • Cournac, L.1    Redding, K.2    Ravenel, J.3    Rumeau, D.4    Josse, E.M.5
  • 33
    • 0029142099 scopus 로고
    • Properties of a large complex with NADH dehydrogenase activity from barley thylakoids
    • Cuello J, Quiles MJ, Albacete ME, Sabater B. 1995. Properties of a large complex with NADH dehydrogenase activity from barley thylakoids. Plant Cell Physiol. 36:265-71
    • (1995) Plant Cell Physiol. , vol.36 , pp. 265-271
    • Cuello, J.1    Quiles, M.J.2    Albacete, M.E.3    Sabater, B.4
  • 34
    • 0025712978 scopus 로고
    • Loss of photosynthetic and chlororespiratory genes from the plastid genome of a parasitic flowering plant
    • dePamphilis CW, Palmer JD. 1990. Loss of photosynthetic and chlororespiratory genes from the plastid genome of a parasitic flowering plant. Nature 348:337-39
    • (1990) Nature , vol.348 , pp. 337-339
    • DePamphilis, C.W.1    Palmer, J.D.2
  • 35
    • 0015846699 scopus 로고
    • Feedback controlling oxygen production in a cross-reaction between two photosystems in photosynthesis
    • Diner B, Mauzerall D. 1973. Feedback controlling oxygen production in a cross-reaction between two photosystems in photosynthesis. Biochim. Biophys. Acta 305:329-52
    • (1973) Biochim. Biophys. Acta , vol.305 , pp. 329-352
    • Diner, B.1    Mauzerall, D.2
  • 36
    • 0029850499 scopus 로고    scopus 로고
    • Dark induction of the non-photochemical quenching of chlorophyll fluorescence by acetate in Chlamydomonas reinhardtii
    • Endo T, Asada K. 1996. Dark induction of the non-photochemical quenching of chlorophyll fluorescence by acetate in Chlamydomonas reinhardtii. Plant Cell Physiol. 37:551-55
    • (1996) Plant Cell Physiol. , vol.37 , pp. 551-555
    • Endo, T.1    Asada, K.2
  • 37
    • 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 HL, Shikanai T, Asada K. 1997. Donation of electrons to plastoquinone by NAD(P)H dehydrogenase and by ferredoxin-quinone reductase in spinach chloroplasts. Plant Cell Physiol. 38:1272-77
    • (1997) Plant Cell Physiol. , vol.38 , pp. 1272-1277
    • Endo, T.1    Mi, H.L.2    Shikanai, T.3    Asada, K.4
  • 38
    • 0029189429 scopus 로고
    • Suppression of quantum yield of photosystern II by hyperosmotic stress in Chlamydomonas reinhardtii
    • Endo T, Schreiber U, Asada K. 1995. Suppression of quantum yield of photosystern II by hyperosmotic stress in Chlamydomonas reinhardtii. Plant Cell Physiol. 36:1253-58
    • (1995) Plant Cell Physiol. , vol.36 , pp. 1253-1258
    • Endo, T.1    Schreiber, U.2    Asada, K.3
  • 39
    • 0001657280 scopus 로고    scopus 로고
    • NAD(P)H dehydrogenase-dependent, antimycin A-sensitive electron donation to plastoquinone in tobacco chloroplasts
    • Endo T, Shikanai T, Sato F, Asada K. 1998. NAD(P)H dehydrogenase-dependent, antimycin A-sensitive electron donation to plastoquinone in tobacco chloroplasts. Plant Cell Physiol. 39:1226-31
    • (1998) Plant Cell Physiol. , vol.39 , pp. 1226-1231
    • Endo, T.1    Shikanai, T.2    Sato, F.3    Asada, K.4
  • 40
    • 0032790755 scopus 로고    scopus 로고
    • The role of chloroplastic NAD(P)H dehydrogenase in photoprotection
    • Endo T, Shikanai T, Takabayashi A, Asada K, Sato F. 1999. The role of chloroplastic NAD(P)H dehydrogenase in photoprotection. FEBS Lett. 457:5-8
    • (1999) FEBS Lett. , vol.457 , pp. 5-8
    • Endo, T.1    Shikanai, T.2    Takabayashi, A.3    Asada, K.4    Sato, F.5
  • 41
    • 0028865421 scopus 로고
    • Light intensity regulation of cab gene transcription is signaled by the redox state of the plastoquinone pool
    • Escoubas JM, Lomas M, LaRoche J, Falkowski PG. 1995. Light intensity regulation of cab gene transcription is signaled by the redox state of the plastoquinone pool. Proc. Natl. Acad. Sci. USA 92:10237-41
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10237-10241
    • Escoubas, J.M.1    Lomas, M.2    LaRoche, J.3    Falkowski, P.G.4
  • 42
    • 0000792290 scopus 로고    scopus 로고
    • Non-photochemical reduction of the plastoquinone pool in sunflower leaves originates from chlororespiration
    • Feild TS, Nedbal L, Ort DR. 1998. Non-photochemical reduction of the plastoquinone pool in sunflower leaves originates from chlororespiration. Plant Physiol. 116:1209-18
    • (1998) Plant Physiol. , vol.116 , pp. 1209-1218
    • Feild, T.S.1    Nedbal, L.2    Ort, D.R.3
  • 43
    • 0035933863 scopus 로고    scopus 로고
    • Photoinhibition of Chlamydomonas reinhardtii in state 1 and state 2 - Damages to the photosynthetic apparatus under linear and cyclic electron flow
    • Finazzi G, Barbagallo RP, Bergo E, Barbato R, Forti G. 2001. Photoinhibition of Chlamydomonas reinhardtii in state 1 and state 2 - damages to the photosynthetic apparatus under linear and cyclic electron flow. J. Biol. Chem. 276:22251-57
    • (2001) J. Biol. Chem. , vol.276 , pp. 22251-22257
    • Finazzi, G.1    Barbagallo, R.P.2    Bergo, E.3    Barbato, R.4    Forti, G.5
  • 44
    • 0030850950 scopus 로고    scopus 로고
    • The expression of subunits of the mitochondrial complex I-homologous NAD(P)H-plastoquinone-oxidoreductase during plastid development
    • Fischer M, Funk E, Steinmüller K. 1997. The expression of subunits of the mitochondrial complex I-homologous NAD(P)H-plastoquinone-oxidoreductase during plastid development. Z. Naturforsch. Teil C 52:481-86
    • (1997) Z. Naturforsch. Teil C , vol.52 , pp. 481-486
    • Fischer, M.1    Funk, E.2    Steinmüller, K.3
  • 45
    • 0029059910 scopus 로고
    • The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts
    • Friedrich T, Steinmuller K, Weiss H. 1995. The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts. FEBS Len. 367:107-11
    • (1995) FEBS Lett. , vol.367 , pp. 107-111
    • Friedrich, T.1    Steinmuller, K.2    Weiss, H.3
  • 46
    • 84941787599 scopus 로고
    • Fermentative and photochemical production of hydrogen in algae
    • Gaffron H, Rubin J. 1942. Fermentative and photochemical production of hydrogen in algae. J. Gen. Physiol. 26:219-40
    • (1942) J. Gen. Physiol. , vol.26 , pp. 219-240
    • Gaffron, H.1    Rubin, J.2
  • 47
    • 0025117511 scopus 로고
    • Control in the dark of the plastoquinone redox state by mitochondrial activity in Chlamydomonas reinhardtii
    • Gans P, Rebeillé F. 1990. Control in the dark of the plastoquinone redox state by mitochondrial activity in Chlamydomonas reinhardtii. Biochim. Biophys. Acta 1015:150-55
    • (1990) Biochim. Biophys. Acta , vol.1015 , pp. 150-155
    • Gans, P.1    Rebeillé, F.2
  • 48
    • 0001036383 scopus 로고
    • Respiratory control over photosynthetic electron transport in chloroplasts of higher plant cells - Evidence for chlororespiration
    • Garab G, Lajko F, Mustardy L, Marton L. 1989. Respiratory control over photosynthetic electron transport in chloroplasts of higher plant cells - evidence for chlororespiration. Planta 179:349-58
    • (1989) Planta , vol.179 , pp. 349-358
    • Garab, G.1    Lajko, F.2    Mustardy, L.3    Marton, L.4
  • 49
    • 0028845652 scopus 로고
    • The contribution of mitochondria to energetic metabolism in photosynthetic cells
    • Gardestrom P, Lernmark U. 1995. The contribution of mitochondria to energetic metabolism in photosynthetic cells. J. Bioenerg. Biomembr. 27:415-21
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 415-421
    • Gardestrom, P.1    Lernmark, U.2
  • 50
    • 0000099721 scopus 로고
    • Fermentative metabolism of Chlamydomonas reinhardtii. 2. Role of plastoquinone
    • Gfeller RP, Gibbs M. 1985. Fermentative metabolism of Chlamydomonas reinhardtii. 2. Role of plastoquinone. Plant Physiol. 77:509-11
    • (1985) Plant Physiol. , vol.77 , pp. 509-511
    • Gfeller, R.P.1    Gibbs, M.2
  • 51
    • 0019974543 scopus 로고
    • Evidence for a membrane-bound NADH-plastoquinone oxidoreductase in Chlamydomonas reinhardtii CW-15
    • Godde D. 1982. Evidence for a membrane-bound NADH-plastoquinone oxidoreductase in Chlamydomonas reinhardtii CW-15. Arch. Microbiol. 131:197-202
    • (1982) Arch. Microbiol. , vol.131 , pp. 197-202
    • Godde, D.1
  • 52
    • 0019126116 scopus 로고
    • NADH as electron donor for the photosynthetic membrane of Chlamydomonas reinhardtii
    • Godde D, Trebst A. 1980. NADH as electron donor for the photosynthetic membrane of Chlamydomonas reinhardtii. Arch. Microbiol. 127:245-52
    • (1980) Arch. Microbiol. , vol.127 , pp. 245-252
    • Godde, D.1    Trebst, A.2
  • 53
    • 0002428235 scopus 로고
    • A cooperation of two-pigment systems and respiration in photosynthetic luminescence
    • Goedheer JC. 1963. A cooperation of two-pigment systems and respiration in photosynthetic luminescence. Biochim. Biophys. Acta 66:61-71
    • (1963) Biochim. Biophys. Acta , vol.66 , pp. 61-71
    • Goedheer, J.C.1
  • 54
    • 0030295294 scopus 로고    scopus 로고
    • The NADH-binding subunit of respiratory chain complex I is nuclear-encoded in plants and identified only in mitochondria
    • Grohmann L, Rasmusson AG, Heiser V, Thieck O, 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
    • (1996) Plant J. , vol.10 , pp. 793-803
    • Grohmann, L.1    Rasmusson, A.G.2    Heiser, V.3    Thieck, O.4    Brennicke, A.5
  • 56
    • 0030043480 scopus 로고    scopus 로고
    • Evidence for an association of ndhB, ndhJ gene products and ferredoxin-NADP-reductase as components of a chloroplastic NAD(P)H dehydrogenase complex
    • Guedeney G, Corneille S, Cuine S, Peltier G. 1996. Evidence for an association of ndhB, ndhJ gene products and ferredoxin-NADP-reductase as components of a chloroplastic NAD(P)H dehydrogenase complex. FEBS Lett. 378:277-80
    • (1996) FEBS Lett. , vol.378 , pp. 277-280
    • Guedeney, G.1    Corneille, S.2    Cuine, S.3    Peltier, G.4
  • 58
    • 0000353641 scopus 로고
    • Effects of anaerobiosis on chlorophyll fluorescence yield in spinach (Spinacia oleracea) leaf discs
    • Harris GC, Heber U. 1993. Effects of anaerobiosis on chlorophyll fluorescence yield in spinach (Spinacia oleracea) leaf discs. Plant Physiol. 101:1169-73
    • (1993) Plant Physiol. , vol.101 , pp. 1169-1173
    • Harris, G.C.1    Heber, U.2
  • 59
    • 0030032608 scopus 로고    scopus 로고
    • Short-term responses of photosystem I to heat stress. Induction of a PSII-independent electron transport through PSI fed by stromal components
    • Havaux M. 1996. Short-term responses of photosystem I to heat stress. Induction of a PSII-independent electron transport through PSI fed by stromal components. Photosynth. Res. 47:85-97
    • (1996) Photosynth. Res. , vol.47 , pp. 85-97
    • Havaux, M.1
  • 60
    • 0001411962 scopus 로고
    • Metabolite exchange between chloroplasts and cytoplasm
    • Heber U. 1974. Metabolite exchange between chloroplasts and cytoplasm. Annu. Rev. Plant Physiol. Plant Mol. Biol. 25:393-421
    • (1974) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.25 , pp. 393-421
    • Heber, U.1
  • 61
    • 0002054893 scopus 로고
    • Regulation of photosynthetic electron transport and phosphorylation in intact chloroplasts and leaves of Spinacia oleracea
    • Heber U, Egneus H, Hanck U, Jensen M, Köster S. 1978. Regulation of photosynthetic electron transport and phosphorylation in intact chloroplasts and leaves of Spinacia oleracea. Planta 143:41-49
    • (1978) Planta , vol.143 , pp. 41-49
    • Heber, U.1    Egneus, H.2    Hanck, U.3    Jensen, M.4    Köster, S.5
  • 62
    • 0001391899 scopus 로고
    • Concerning a dual function of coupled cyclic electron transport in leaves
    • Heber U, Walker D. 1992. Concerning a dual function of coupled cyclic electron transport in leaves. Plant Physiol. 100:1621-26
    • (1992) Plant Physiol. , vol.100 , pp. 1621-1626
    • Heber, U.1    Walker, D.2
  • 63
    • 0002463354 scopus 로고
    • Transfer of redox equivalents between subcellular compartments of a leaf cell
    • ed. M Batscheffsky. Dordrecht, The Neth.: Kluwer
    • Heldt HW, Heineke D, Heupel R, Krömer S, Riens B. 1990. Transfer of redox equivalents between subcellular compartments of a leaf cell. In Current Research in Photosynthesis, ed. M Batscheffsky, pp. 15.1-5.7. Dordrecht, The Neth.: Kluwer
    • (1990) Current Research in Photosynthesis , pp. 115-157
    • Heldt, H.W.1    Heineke, D.2    Heupel, R.3    Krömer, S.4    Riens, B.5
  • 64
    • 0024674380 scopus 로고
    • The complete sequence of the rice (Oryza sativa) chloroplast genome - Intermolecular recombination between distinct transfer-RNA genes accounts for a major plastid DNA inversion during the evolution of the cereals
    • Hiratsuka J, Shimada H, Whittier R, Ishibashi T, Sakamoto M, et al. 1989. The complete sequence of the rice (Oryza sativa) chloroplast genome - intermolecular recombination between distinct transfer-RNA genes accounts for a major plastid DNA inversion during the evolution of the cereals. Mol. Gen. Genet. 217:185-94
    • (1989) Mol. Gen. Genet. , vol.217 , pp. 185-194
    • Hiratsuka, J.1    Shimada, H.2    Whittier, R.3    Ishibashi, T.4    Sakamoto, M.5
  • 65
    • 0032494283 scopus 로고    scopus 로고
    • Interdependence between chloroplasts and mitochondria in the light and the dark
    • Hoefnagel MHN, Atkin OK, Wiskich JT. 1998. Interdependence between chloroplasts and mitochondria in the light and the dark. Biochim. Biophys. Acta 1366:235-55
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 235-255
    • Hoefnagel, M.H.N.1    Atkin, O.K.2    Wiskich, J.T.3
  • 66
    • 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
    • Horvath EM, Peter SO, Joët T, Rumeau D, Cournac L, 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. 123:1337-49
    • (2000) Plant Physiol. , vol.123 , pp. 1337-1349
    • Horvath, E.M.1    Peter, S.O.2    Joët, T.3    Rumeau, D.4    Cournac, L.5
  • 67
    • 0002598737 scopus 로고
    • Evidence for two cyclic photophosphorylation reactions concurrent with ferredoxin-catalyzed non-cyclic electron transport
    • Hosler JP, Yocum CF. 1985. Evidence for two cyclic photophosphorylation reactions concurrent with ferredoxin-catalyzed non-cyclic electron transport. Biochim. Biophys. Acta 808:21-31
    • (1985) Biochim. Biophys. Acta , vol.808 , pp. 21-31
    • Hosler, J.P.1    Yocum, C.F.2
  • 68
    • 0032988011 scopus 로고    scopus 로고
    • Type 2 NADH dehydrogenases in the cyanobacterium Synechocystis sp. strain PCC 6803 are involved in regulation rather than respiration
    • Howitt CA, Udall PK, Vermaas WFJ. 1999. Type 2 NADH dehydrogenases in the cyanobacterium Synechocystis sp. strain PCC 6803 are involved in regulation rather than respiration. J. Bacteriol. 181:3994-4003
    • (1999) J. Bacteriol. , vol.181 , pp. 3994-4003
    • Howitt, C.A.1    Udall, P.K.2    Vermaas, W.F.J.3
  • 69
    • 0035033776 scopus 로고    scopus 로고
    • Increased sensitivity of photosynthesis to antimycin A induced by inactivation of the chloroplast ndhB gene. Evidence for a participation of the NADH-dehydrogenase complex to cyclic electron flow around photosystem I
    • Joët T, Cournac L, Horvath EM, Medgyesy P, Peltier G. 2001. Increased sensitivity of photosynthesis to antimycin A induced by inactivation of the chloroplast ndhB gene. Evidence for a participation of the NADH-dehydrogenase complex to cyclic electron flow around photosystem I. Plant Physiol. 125:1919-29
    • (2001) Plant Physiol. , vol.125 , pp. 1919-1929
    • Joët, T.1    Cournac, L.2    Horvath, E.M.3    Medgyesy, P.4    Peltier, G.5
  • 70
    • 0000888058 scopus 로고
    • Dependence of delayed luminescence upon adenosine-triphosphatase activity in Chlorella
    • Joliot P, Joliot A. 1980. Dependence of delayed luminescence upon adenosine-triphosphatase activity in Chlorella. Plant Physiol. 65:691-96
    • (1980) Plant Physiol. , vol.65 , pp. 691-696
    • Joliot, P.1    Joliot, A.2
  • 71
    • 0026766411 scopus 로고
    • Plastoquinone compartmentation in chloroplasts. 1. Evidence for domains with different rates of photoreduction
    • Joliot P, Lavergne J, Beal D. 1992. Plastoquinone compartmentation in chloroplasts. 1. Evidence for domains with different rates of photoreduction. Biochim. Biophys. Acta 1101:1-12
    • (1992) Biochim. Biophys. Acta , vol.1101 , pp. 1-12
    • Joliot, P.1    Lavergne, J.2    Beal, D.3
  • 72
    • 0033841024 scopus 로고    scopus 로고
    • A plastid terminal oxidase associated with carotenoid desaturation during chromoplast differentiation
    • Josse EM, Simkin AJ, Gaffe J, Laboure AM, Kuntz M, Carol P. 2000. A plastid terminal oxidase associated with carotenoid desaturation during chromoplast differentiation. Plant Physiol. 123:1427-36
    • (2000) Plant Physiol. , vol.123 , pp. 1427-1436
    • Josse, E.M.1    Simkin, A.J.2    Gaffe, J.3    Laboure, A.M.4    Kuntz, M.5    Carol, P.6
  • 73
    • 0034739889 scopus 로고    scopus 로고
    • Complete structure of the chloroplast genome of a legume, Lotus japonicus
    • Kato T, Kaneko T, Sato S, Nakamura Y, Tabata S. 2000. Complete structure of the chloroplast genome of a legume, Lotus japonicus. DNA Res. 7:323-30
    • (2000) DNA Res. , vol.7 , pp. 323-330
    • Kato, T.1    Kaneko, T.2    Sato, S.3    Nakamura, Y.4    Tabata, S.5
  • 74
    • 0013356469 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 75
    • 0013359057 scopus 로고
    • + reduction
    • ed. RK Clayton, WR Sistrom. New York: Plenum
    • + reduction. In The Photosynthetic Bacteria, ed. RK Clayton, WR Sistrom, pp. 629-40. New York: Plenum
    • (1978) The Photosynthetic Bacteria , pp. 629-640
    • Knaff, D.B.1
  • 76
    • 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 HU, Wanner G, 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. 258:166-73
    • (1998) Mol. Gen. Genet. , vol.258 , pp. 166-173
    • Kofer, W.1    Koop, H.U.2    Wanner, G.3    Steinmüller, K.4
  • 77
    • 0343618724 scopus 로고    scopus 로고
    • Dark reoxidation of the plastoquinone pool is mediated by the low-potential form of cytochrome b-559 in spinach thylakoids
    • Kruk J, Strzalka K. 1999. Dark reoxidation of the plastoquinone pool is mediated by the low-potential form of cytochrome b-559 in spinach thylakoids. Photosynth. Res. 62:273-79
    • (1999) Photosynth. Res. , vol.62 , pp. 273-279
    • Kruk, J.1    Strzalka, K.2
  • 78
    • 0029740614 scopus 로고    scopus 로고
    • 4 plant Sorghum bicolor indicates that the complex I-homologous NAD(P)H-plastoquinone oxidoreductase is involved in cyclic electron transport
    • 4 plant Sorghum bicolor indicates that the complex I-homologous NAD(P)H-plastoquinone oxidoreductase is involved in cyclic electron transport. Planta 199:276-81
    • (1996) Planta , vol.199 , pp. 276-281
    • Kubicki, A.1    Funk, E.2    Westhoff, P.3    Steinmüller, K.4
  • 79
    • 0030969742 scopus 로고    scopus 로고
    • Competition between the photosynthetic and the (chloro)respiratory electron transport chains in cyanobacteria, green algae and higher plants. Effect of heat stress
    • Lajko F, Kadioglu A, Borbely G, Garab G. 1997. Competition between the photosynthetic and the (chloro)respiratory electron transport chains in cyanobacteria, green algae and higher plants. Effect of heat stress. Photosynthetica 33:217-26
    • (1997) Photosynthetica , vol.33 , pp. 217-226
    • Lajko, F.1    Kadioglu, A.2    Borbely, G.3    Garab, G.4
  • 80
    • 0029075136 scopus 로고
    • Isolation and characterization of the proton-translocating NADH: Ubiquinone oxidoreductase from Escherichia coli
    • Leif H, Sled VD, Ohnishi T, Weiss H, Friedrich T. 1995. Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli. Eur. J. Biochem. 230:538-48
    • (1995) Eur. J. Biochem. , vol.230 , pp. 538-548
    • Leif, H.1    Sled, V.D.2    Ohnishi, T.3    Weiss, H.4    Friedrich, T.5
  • 81
    • 0034628462 scopus 로고    scopus 로고
    • Ancestral chloroplast genome in Mesostigma viride reveals an early branch of green plant evolution
    • Lemieux C, Otis C, Turmel M. 2000. Ancestral chloroplast genome in Mesostigma viride reveals an early branch of green plant evolution. Nature 403:649-52
    • (2000) Nature , vol.403 , pp. 649-652
    • Lemieux, C.1    Otis, C.2    Turmel, M.3
  • 82
    • 0029160870 scopus 로고
    • Complete sequence of the maize chloroplast genome - Gene content, hotspots of divergence and fine tuning of genetic information by transcript editing
    • Maier RM, Neckermann K, Igloi GL, Kossel H. 1995. Complete sequence of the maize chloroplast genome - gene content, hotspots of divergence and fine tuning of genetic information by transcript editing. J. Mol. Biol. 251:614-28
    • (1995) J. Mol. Biol. , vol.251 , pp. 614-628
    • Maier, R.M.1    Neckermann, K.2    Igloi, G.L.3    Kossel, H.4
  • 83
    • 0000688294 scopus 로고
    • Association of the chloroplastic respiratory and photosynthetic electron transport chains of Chlamydomonas reinhardtii with photoreduction and the oxyhydrogen reaction
    • Maione TE, Gibbs M. 1986. Association of the chloroplastic respiratory and photosynthetic electron transport chains of Chlamydomonas reinhardtii with photoreduction and the oxyhydrogen reaction. Plant Physiol. 80:364-68
    • (1986) Plant Physiol. , vol.80 , pp. 364-368
    • Maione, T.E.1    Gibbs, M.2
  • 84
    • 0000572642 scopus 로고
    • Hydrogenase-mediated activities in isolated chloroplasts of Chlamydomonas reinhardtii
    • Maione TE, Gibbs M. 1986. Hydrogenase-mediated activities in isolated chloroplasts of Chlamydomonas reinhardtii. Plant Physiol. 80:360-63
    • (1986) Plant Physiol. , vol.80 , pp. 360-363
    • Maione, T.E.1    Gibbs, M.2
  • 85
    • 0031660755 scopus 로고    scopus 로고
    • Judging the homoplastomic state of plastid transformants
    • Maliga P, Nixon PJ. 1998. Judging the homoplastomic state of plastid transformants. Trends Plant Sci. 3:376-77
    • (1998) Trends Plant Sci. , vol.3 , pp. 376-377
    • Maliga, P.1    Nixon, P.J.2
  • 86
    • 0030116960 scopus 로고    scopus 로고
    • Identification of the product of ndhA gene as a thylakoid protein synthesized in response to photooxidative treatment
    • Martin M, Casano LM, Sabater B. 1996. Identification of the product of ndhA gene as a thylakoid protein synthesized in response to photooxidative treatment. Plant Cell Physiol. 37:293-98
    • (1996) Plant Cell Physiol. , vol.37 , pp. 293-298
    • Martin, M.1    Casano, L.M.2    Sabater, B.3
  • 87
    • 0013452671 scopus 로고
    • Three iron-sulfur proteins encoded by three ORFs in chloroplasts and cyanobacteria
    • Matsubara H, Oh OH, Takahashi Y, Fujita Y. 1995. Three iron-sulfur proteins encoded by three ORFs in chloroplasts and cyanobacteria. Photosynth. Res. 46:107-15
    • (1995) Photosynth. Res. , vol.46 , pp. 107-115
    • Matsubara, H.1    Oh, O.H.2    Takahashi, Y.3    Fujita, Y.4
  • 88
    • 0023476294 scopus 로고
    • Six chloroplast genes (ndhA-F) homologous to human mitochondrial genes encoding components of the respiratory chain NADH dehydrogenase are actively expressed: Determination of the splice sites in ndhA and ndhB premRNAs
    • Matsubayashi T, Wakasugi T, Shinozaki K, Yamaguchi-Shinozaki K, Zaita N, et al. 1987. Six chloroplast genes (ndhA-F) homologous to human mitochondrial genes encoding components of the respiratory chain NADH dehydrogenase are actively expressed: determination of the splice sites in ndhA and ndhB premRNAs. Mol. Gen. Genet. 210:385-93
    • (1987) Mol. Gen. Genet. , vol.210 , pp. 385-393
    • Matsubayashi, T.1    Wakasugi, T.2    Shinozaki, K.3    Yamaguchi-Shinozaki, K.4    Zaita, N.5
  • 89
    • 0033759410 scopus 로고    scopus 로고
    • Sustained photobiological hydrogen gas production upon reversible inactivation of oxygen evolution in the green alga Chlamydomonas reinhardtii
    • Melis A, Zhang LP, Forestier M, Ghirardi ML, Seibert M. 2000. Sustained photobiological hydrogen gas production upon reversible inactivation of oxygen evolution in the green alga Chlamydomonas reinhardtii. Plant Physiol. 122:127-35
    • (2000) Plant Physiol. , vol.122 , pp. 127-135
    • Melis, A.1    Zhang, L.P.2    Forestier, M.3    Ghirardi, M.L.4    Seibert, M.5
  • 90
    • 0018786935 scopus 로고
    • Electron transport pathways in spinach chloroplasts. Reduction of the primary acceptor of photosystem II by reduced nicotinamide adenine dinucleotide phosphate in the dark
    • Mills JD, Crowther D, Slovacek RE, Hind G, McCarty RE. 1979. Electron transport pathways in spinach chloroplasts. Reduction of the primary acceptor of photosystem II by reduced nicotinamide adenine dinucleotide phosphate in the dark. Biochim. Biophys. Acta 547:127-37
    • (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.E.5
  • 91
    • 34547115717 scopus 로고
    • Cyclic electron transport in chloroplasts. The Q-cycle and the site of action of antimycin
    • Moss DA, Bendall DS. 1984. Cyclic electron transport in chloroplasts. The Q-cycle and the site of action of antimycin. Biochim. Biophys. Acta 767:389-95
    • (1984) Biochim. Biophys. Acta , vol.767 , pp. 389-395
    • Moss, D.A.1    Bendall, D.S.2
  • 92
    • 0029854243 scopus 로고    scopus 로고
    • The ndhF chloroplast gene detected in all vascular plant divisions
    • Neyland R, Urbatsch LE. 1996. The ndhF chloroplast gene detected in all vascular plant divisions. Planta 200:273-77
    • (1996) Planta , vol.200 , pp. 273-277
    • Neyland, R.1    Urbatsch, L.E.2
  • 93
    • 0001325378 scopus 로고
    • Protein-DNA interaction within one cloned chloroplast DNA replication origin of Chlamydomonas
    • Nie ZQ, Chang DY, Wu M. 1987. Protein-DNA interaction within one cloned chloroplast DNA replication origin of Chlamydomonas. Mol. Gen. Genet. 209:265-69
    • (1987) Mol. Gen. Genet. , vol.209 , pp. 265-269
    • Nie, Z.Q.1    Chang, D.Y.2    Wu, M.3
  • 94
    • 0028884857 scopus 로고
    • Carotene desaturation is linked to a respiratory redox pathway in Narcissus pseudonarcissus chromoplast membranes. Involvement of a 23-kDa oxygen-evolving-complex-like protein
    • Nievelstein V, Vandekerchove J, Tadros MH, Lintig JV, Nitschke W, Beyer P. 1995. Carotene desaturation is linked to a respiratory redox pathway in Narcissus pseudonarcissus chromoplast membranes. Involvement of a 23-kDa oxygen-evolving-complex-like protein. Eur. J. Biochem. 233:864-72
    • (1995) Eur. J. Biochem. , vol.233 , pp. 864-872
    • Nievelstein, V.1    Vandekerchove, J.2    Tadros, M.H.3    Lintig, J.V.4    Nitschke, W.5    Beyer, P.6
  • 97
    • 0033709566 scopus 로고    scopus 로고
    • Safety valves for photosynthesis
    • Niyogi KK. 2000. Safety valves for photosynthesis. Curr. Opin. Plant Biol. 3:455-60
    • (2000) Curr. Opin. Plant Biol. , vol.3 , pp. 455-460
    • Niyogi, K.K.1
  • 98
    • 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. 1991. A gene homologous to the subunit-2 gene of NADH dehydrogenase is essential to inorganic carbon transport of Synechocystis PCC6803. Proc. Natl. Acad. Sci. USA 88:4275-79
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4275-4279
    • Ogawa, T.1
  • 99
    • 0034664042 scopus 로고    scopus 로고
    • Redox signaling: Globalization of gene expression
    • Oh JI, Kaplan S. 2000. Redox signaling: globalization of gene expression. EMBO J. 19:4237-47
    • (2000) EMBO J. , vol.19 , pp. 4237-4247
    • Oh, J.I.1    Kaplan, S.2
  • 100
    • 0022546644 scopus 로고
    • Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA
    • Ohyama K, Fukuzawa H, Kohchi T, Shirai H, Sano T, et al. 1986. Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA. Nature 322:572-74
    • (1986) Nature , vol.322 , pp. 572-574
    • Ohyama, K.1    Fukuzawa, H.2    Kohchi, T.3    Shirai, H.4    Sano, T.5
  • 102
    • 0027602859 scopus 로고
    • Chloroplast transformation in plants: Polyethylene glycol (PEG) treatment of protoplasts is an alternative to biolistic delivery systems
    • O'Neill C, Horvath GV, Horvath E, Dix PJ, Medgyesy P. 1993. Chloroplast transformation in plants: polyethylene glycol (PEG) treatment of protoplasts is an alternative to biolistic delivery systems. Plant J. 3:729-38
    • (1993) Plant J. , vol.3 , pp. 729-738
    • O'Neill, C.1    Horvath, G.V.2    Horvath, E.3    Dix, P.J.4    Medgyesy, P.5
  • 103
    • 0002379651 scopus 로고
    • Photorespiration and photoinhibition. Some implications for the energetics of photosynthesis
    • Osmond CB. 1981. Photorespiration and photoinhibition. Some implications for the energetics of photosynthesis. Biochim. Biophys. Acta 639:77-98
    • (1981) Biochim. Biophys. Acta , vol.639 , pp. 77-98
    • Osmond, C.B.1
  • 104
    • 0031016902 scopus 로고    scopus 로고
    • Organelle genomes: Going, going, gone
    • Palmer JD. 1997. Organelle genomes: going, going, gone. Science 275:790-91
    • (1997) Science , vol.275 , pp. 790-791
    • Palmer, J.D.1
  • 105
    • 0001279866 scopus 로고
    • Characterization of starch breakdown in intact spinach chloroplast
    • Peavey DG, Steup M, Gibbs M. 1977. Characterization of starch breakdown in intact spinach chloroplast. Plant Physiol. 60:305-8
    • (1977) Plant Physiol. , vol.60 , pp. 305-308
    • Peavey, D.G.1    Steup, M.2    Gibbs, M.3
  • 106
    • 0001638522 scopus 로고
    • Chlororespiration in unicellular green algae. Studies with mitochondrial respiration deficient mutants
    • ed. P. Mathis. Dordrecht, The Neth.: Kluwer
    • Peltier G, Havaux M, Ravenel J. 1995. Chlororespiration in unicellular green algae. Studies with mitochondrial respiration deficient mutants. In Photosynthesis: From Light to Biosphere, ed. P. Mathis, pp. 887-90. Dordrecht, The Neth.: Kluwer
    • (1995) Photosynthesis: From Light to Biosphere , pp. 887-890
    • Peltier, G.1    Havaux, M.2    Ravenel, J.3
  • 107
    • 0002070827 scopus 로고
    • Inhibition of a respiratory activity by short saturating flashes in Chlamydomonas: Evidence for a chlororespiration
    • Peltier G, Ravenel J, Verméglio A. 1987. Inhibition of a respiratory activity by short saturating flashes in Chlamydomonas: evidence for a chlororespiration. Biochim. Biophys. Acta 893:83-90
    • (1987) Biochim. Biophys. Acta , vol.893 , pp. 83-90
    • Peltier, G.1    Ravenel, J.2    Verméglio, A.3
  • 108
    • 0025819203 scopus 로고
    • Chlororespiration: An adaptation to nitrogen deficiency in Chlamydomonas reinhardtii
    • Peltier G, Schmidt GW. 1991. Chlororespiration: an adaptation to nitrogen deficiency in Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA 88:4791-95
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4791-4795
    • Peltier, G.1    Schmidt, G.W.2
  • 109
    • 0000360875 scopus 로고
    • Oxygen exchange studies in Chlamydomonas mutants deficient in photosynthetic electron transport: Evidence for a photosystem II-dependent oxygen uptake in vivo
    • Peltier G, Thibault P. 1988. Oxygen exchange studies in Chlamydomonas mutants deficient in photosynthetic electron transport: evidence for a photosystem II-dependent oxygen uptake in vivo. Biochim. Biophys. Acta 936:319-24
    • (1988) Biochim. Biophys. Acta , vol.936 , pp. 319-324
    • Peltier, G.1    Thibault, P.2
  • 110
    • 48749147999 scopus 로고
    • Studies on well-coupled photosystem I-enriched subchloroplast vesicles - Optimization of ferredoxin-mediated cyclic photophosphorylation and electric potential generation
    • Peters F, Vanspanning R, Kraayenhof R. 1983. Studies on well-coupled photosystem I-enriched subchloroplast vesicles - optimization of ferredoxin-mediated cyclic photophosphorylation and electric potential generation. Biochim. Biophys. Acta 724:159-65
    • (1983) Biochim. Biophys. Acta , vol.724 , pp. 159-165
    • Peters, F.1    Vanspanning, R.2    Kraayenhof, R.3
  • 111
    • 0033580325 scopus 로고    scopus 로고
    • Photosynthetic control of chloroplast gene expression
    • Pfannschmidt T, Nilsson A, Allen JF. 1999. Photosynthetic control of chloroplast gene expression. Nature 397:625-28
    • (1999) Nature , vol.397 , pp. 625-628
    • Pfannschmidt, T.1    Nilsson, A.2    Allen, J.F.3
  • 113
    • 0000662076 scopus 로고    scopus 로고
    • Association of ferredoxin-NADP oxidoreductase with the chloroplastic pyridine nucleotide dehydrogenase complex in barley leaves
    • Quiles MJ, Cuello J. 1998. Association of ferredoxin-NADP oxidoreductase with the chloroplastic pyridine nucleotide dehydrogenase complex in barley leaves. Plant Physiol. 117:235-44
    • (1998) Plant Physiol. , vol.117 , pp. 235-244
    • Quiles, M.J.1    Cuello, J.2
  • 114
    • 0028086766 scopus 로고
    • Interdependence of photosynthesis and respiration in plant cells - Interactions between chloroplasts and mitochondria
    • Raghavendra AS, Padmasree K, Saradadevi K. 1994. Interdependence of photosynthesis and respiration in plant cells - interactions between chloroplasts and mitochondria. Plant Sci. 97:1-14
    • (1994) Plant Sci. , vol.97 , pp. 1-14
    • Raghavendra, A.S.1    Padmasree, K.2    Saradadevi, K.3
  • 115
    • 0033573842 scopus 로고    scopus 로고
    • A new electrochemical gradient generator in thylakoid membranes of green algae
    • Rappaport F, Finazzi G, Pierre Y, Bennoun P. 1999. A new electrochemical gradient generator in thylakoid membranes of green algae. Biochemistry 38:2040-47
    • (1999) Biochemistry , vol.38 , pp. 2040-2047
    • Rappaport, F.1    Finazzi, G.2    Pierre, Y.3    Bennoun, P.4
  • 116
    • 0026723731 scopus 로고
    • Stimulation of the chlororespiratory electron flow by photosystem II activity in Chlamydomonas reinhardtii
    • Ravenel J, Peltier G. 1992. Stimulation of the chlororespiratory electron flow by photosystem II activity in Chlamydomonas reinhardtii. Biochim. Biophys. Acta 1101:57-63
    • (1992) Biochim. Biophys. Acta , vol.1101 , pp. 57-63
    • Ravenel, J.1    Peltier, G.2
  • 117
    • 0028110631 scopus 로고
    • The cyclic electron pathways around photosystem I in Chlamydomonas reinhardtii as determined in vivo by photoacoustic measurements of energy storage
    • Ravenel J, Peltier G, Havaux M. 1994. The cyclic electron pathways around photosystem I in Chlamydomonas reinhardtii as determined in vivo by photoacoustic measurements of energy storage. Planta 193:251-59
    • (1994) Planta , vol.193 , pp. 251-259
    • Ravenel, J.1    Peltier, G.2    Havaux, M.3
  • 118
    • 0000331434 scopus 로고
    • Interaction between chloroplasts and mitochondria in microalgae
    • Rebeillé F, Gans P. 1988. Interaction between chloroplasts and mitochondria in microalgae. Plant Physiol. 88:973-75
    • (1988) Plant Physiol. , vol.88 , pp. 973-975
    • Rebeillé, F.1    Gans, P.2
  • 120
    • 51649139576 scopus 로고
    • Complete nucleotide sequence of the Porphyra purpurea chloroplast genome
    • Reith M, Munholland J. 1995. Complete nucleotide sequence of the Porphyra purpurea chloroplast genome. Plant Mol. Biol. 13:327-32
    • (1995) Plant Mol. Biol. , vol.13 , pp. 327-332
    • Reith, M.1    Munholland, J.2
  • 121
    • 0013357678 scopus 로고    scopus 로고
    • An assessment of the pathways of dark reduction and oxidation of the plastoquinone pool in thylakoid membranes of higher plants and green algae
    • Victoria, Aust.: CSIRO
    • Rich PR, Fisher N, Lennon A, Prommeenate P, Purton S, et al. 2001. An assessment of the pathways of dark reduction and oxidation of the plastoquinone pool in thylakoid membranes of higher plants and green algae. Proc. Int. Congr. Photosynth., 12th, Brisbane, Aust. Victoria, Aust.: CSIRO. http://www.publish.csiro.au/ps2001/cf/home/index.cfm
    • (2001) Proc. Int. Congr. Photosynth., 12th, Brisbane, Aust.
    • Rich, P.R.1    Fisher, N.2    Lennon, A.3    Prommeenate, P.4    Purton, S.5
  • 122
    • 0013405965 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 123
    • 0033615372 scopus 로고    scopus 로고
    • Complete structure of the chloroplast genome of Arabidopsis thaliana
    • Sato S, Nakamura Y, Kaneko T, Asamizu E, Tabata S. 1999. Complete structure of the chloroplast genome of Arabidopsis thaliana. DNA Res. 6:283-90
    • (1999) DNA Res. , vol.6 , pp. 283-290
    • Sato, S.1    Nakamura, Y.2    Kaneko, T.3    Asamizu, E.4    Tabata, S.5
  • 124
    • 0029792224 scopus 로고    scopus 로고
    • Detection and characterization of a complex I-like NADH-specific dehydrogenase from pea thylakoids
    • Sazanov LA, Burrows P, Nixon PJ. 1996. Detection and characterization of a complex I-like NADH-specific dehydrogenase from pea thylakoids. Biochem. Soc. Trans. 24:739-43
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 739-743
    • Sazanov, L.A.1    Burrows, P.2    Nixon, P.J.3
  • 125
    • 0032486451 scopus 로고    scopus 로고
    • The chloroplast Ndh complex mediates the dark reduction of the plastoquinone pool in response to heat stress in tobacco leaves
    • Sazanov LA, Burrows PA, Nixon PJ. 1998. The chloroplast Ndh complex mediates the dark reduction of the plastoquinone pool in response to heat stress in tobacco leaves. FEBS Lett. 429:115-18
    • (1998) FEBS Lett. , vol.429 , pp. 115-118
    • Sazanov, L.A.1    Burrows, P.A.2    Nixon, P.J.3
  • 126
    • 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 LA, Burrows PA, Nixon PJ. 1998. The plastid ndh genes code for an NADH-specific dehydrogenase: isolation of a complex I analogue from pea thylakoid membranes. Proc. Natl. Acad. Sci. USA 95:1319-24
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1319-1324
    • Sazanov, L.A.1    Burrows, P.A.2    Nixon, P.J.3
  • 127
    • 0025254644 scopus 로고
    • Do photosynthetic and respiratory electron transport chains share redox proteins?
    • Scherer S. 1990. Do photosynthetic and respiratory electron transport chains share redox proteins? Trends Biochem. Sci. 15:458-62
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 458-462
    • Scherer, S.1
  • 130
    • 0002591836 scopus 로고    scopus 로고
    • Physiological function of a respiratory complex, NAD(P)H dehydrogenase in chloroplasts: Dissection by chloroplast reverse genetics
    • Shikanai T, Endo T. 2000. Physiological function of a respiratory complex, NAD(P)H dehydrogenase in chloroplasts: dissection by chloroplast reverse genetics. Plant Biotechnol. 17:79-86
    • (2000) Plant Biotechnol. , vol.17 , pp. 79-86
    • Shikanai, T.1    Endo, T.2
  • 132
    • 84968989005 scopus 로고
    • The complete nucleotide sequence of the tobacco chloroplast genome: Its gene organization and expression
    • Shinozaki K, Ohme M, Tanaka M, Wakasugi T, Hayashida N, et al. 1986. The complete nucleotide sequence of the tobacco chloroplast genome: its gene organization and expression. EMBO J. 5:2043-49
    • (1986) EMBO J. , vol.5 , pp. 2043-2049
    • Shinozaki, K.1    Ohme, M.2    Tanaka, M.3    Wakasugi, T.4    Hayashida, N.5
  • 133
    • 0001065061 scopus 로고
    • Characterization of an electron transport pathway associated with glucose and fructose respiration in the intact chloroplasts of Chlamydomonas reinhardtii and spinach
    • Singh KK, Chen C, Gibbs M. 1992. Characterization of an electron transport pathway associated with glucose and fructose respiration in the intact chloroplasts of Chlamydomonas reinhardtii and spinach. Plant Physiol. 100:327-33
    • (1992) Plant Physiol. , vol.100 , pp. 327-333
    • Singh, K.K.1    Chen, C.2    Gibbs, M.3
  • 134
    • 0019327356 scopus 로고
    • Carbohydrate breakdown by chloroplasts of Pisum sativum
    • Stitt M, Rees TA. 1980. Carbohydrate breakdown by chloroplasts of Pisum sativum. Biochim. Biophys. Acta 627:131-43
    • (1980) Biochim. Biophys. Acta , vol.627 , pp. 131-143
    • Stitt, M.1    Rees, T.A.2
  • 135
    • 0026860017 scopus 로고
    • The chloroplast genome
    • Sugiura M. 1992. The chloroplast genome. Plant Mol. Biol. 19:149-68
    • (1992) Plant Mol. Biol. , vol.19 , pp. 149-168
    • Sugiura, M.1
  • 136
    • 0013448136 scopus 로고
    • + reductase
    • ed. M Edelman, RB Hallick, N-H Chua. Amsterdam, The Neth.: Elsevier Biomed. Press
    • + reductase. In Methods in Chloroplast Molecular Biology, ed. M Edelman, RB Hallick, N-H Chua, pp. 957-71. Amsterdam, The Neth.: Elsevier Biomed. Press
    • (1982) Methods in Chloroplast Molecular Biology , pp. 957-971
    • Süss, K.H.1
  • 137
    • 0027398358 scopus 로고
    • High-frequency plastid transformation in tobacco by selection for a chimeric aadA gene
    • Svab Z, Maliga P. 1993. High-frequency plastid transformation in tobacco by selection for a chimeric aadA gene. Proc. Natl. Acad. Sci. USA 90:913-17
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 913-917
    • Svab, Z.1    Maliga, P.2
  • 138
    • 0001414438 scopus 로고
    • Role of chloroplast ferredoxin in energy conversion process of photosynthesis
    • Tagawa K, Arnon DI, Tsujimoto HY. 1963. Role of chloroplast ferredoxin in energy conversion process of photosynthesis. Proc. Natl. Acad. Sci. USA 49:567-72
    • (1963) Proc. Natl. Acad. Sci. USA , vol.49 , pp. 567-572
    • Tagawa, K.1    Arnon, D.I.2    Tsujimoto, H.Y.3
  • 139
    • 0000960255 scopus 로고
    • Photochemical and nonphotochemical fluorescence quenching processes in the diatom Phaeodactylum tricornutum
    • Ting CS, Owens TG. 1993. Photochemical and nonphotochemical fluorescence quenching processes in the diatom Phaeodactylum tricornutum. Plant Physiol. 101:1323-30
    • (1993) Plant Physiol. , vol.101 , pp. 1323-1330
    • Ting, C.S.1    Owens, T.G.2
  • 140
    • 0033621040 scopus 로고    scopus 로고
    • The complete chloroplast DNA sequence of the green alga Nephroselmis olivacea: Insights into the architecture of ancestral chloroplast genomes
    • Turmel M, Otis C, Lemieux C. 1999. The complete chloroplast DNA sequence of the green alga Nephroselmis olivacea: insights into the architecture of ancestral chloroplast genomes. Proc. Natl. Acad. Sci. USA 96:10248-53
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10248-10253
    • Turmel, M.1    Otis, C.2    Lemieux, C.3
  • 142
    • 0018791105 scopus 로고
    • Quenching of the system II chlorophyll fluorescence by the plastoquinone pool
    • Vernotte C, Etienne A-L, Briantais J-M. 1979. Quenching of the system II chlorophyll fluorescence by the plastoquinone pool. Biochim. Biophys. Acta 545:519-27
    • (1979) Biochim. Biophys. Acta , vol.545 , pp. 519-527
    • Vernotte, C.1    Etienne, A.-L.2    Briantais, J.-M.3
  • 143
    • 12644284525 scopus 로고    scopus 로고
    • Complete nucleotide sequence of the chloroplast genome from the green alga Chlorella vulgaris: The existence of genes possibly involved in chloroplast division
    • Wakasugi T, Nagai T, Kapoor M, Sugita M, Ito M, et al. 1997. Complete nucleotide sequence of the chloroplast genome from the green alga Chlorella vulgaris: the existence of genes possibly involved in chloroplast division. Proc. Natl. Acad. Sci. USA 94:5967-72
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5967-5972
    • Wakasugi, T.1    Nagai, T.2    Kapoor, M.3    Sugita, M.4    Ito, M.5
  • 144
    • 0028043489 scopus 로고
    • Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii
    • Wakasugi T, Tsudzuki J, Ito S, Nakashima K, Tsudzuki T, Sugiura M. 1994. Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii. Proc. Natl. Acad. Sci. USA 91:9794-98
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9794-9798
    • Wakasugi, T.1    Tsudzuki, J.2    Ito, S.3    Nakashima, K.4    Tsudzuki, T.5    Sugiura, M.6
  • 145
    • 0027022870 scopus 로고
    • Cloning of ndhK from soybean chloroplasts using antibodies raised to mitochondrial complex I
    • Whelan J, Young S, Day DA. 1992. Cloning of ndhK from soybean chloroplasts using antibodies raised to mitochondrial complex I. Plant Mol. Biol. 20:887-95
    • (1992) Plant Mol. Biol. , vol.20 , pp. 887-895
    • Whelan, J.1    Young, S.2    Day, D.A.3
  • 146
    • 0025343435 scopus 로고
    • Fluorescence induction kinetics as a tool to detect a chlororespiratory activity in the prasinophycean alga, Mantoniella squamata
    • Wilhelm C, Duval J-C. 1990. Fluorescence induction kinetics as a tool to detect a chlororespiratory activity in the prasinophycean alga, Mantoniella squamata. Biochim. Biophys. Acta 1016:197-202
    • (1990) Biochim. Biophys. Acta , vol.1016 , pp. 197-202
    • Wilhelm, C.1    Duval, J.-C.2
  • 147
    • 0000020862 scopus 로고
    • Evidence for chloroplastic succinate dehydrogenase participating in the chloroplastic respiratory and photosynthetic electron transport chains of Chlamydomonas reinhardtii
    • Willeford KO, Gombos Z, Gibbs M. 1989. Evidence for chloroplastic succinate dehydrogenase participating in the chloroplastic respiratory and photosynthetic electron transport chains of Chlamydomonas reinhardtii. Plant Physiol. 90:1084-87
    • (1989) Plant Physiol. , vol.90 , pp. 1084-1087
    • Willeford, K.O.1    Gombos, Z.2    Gibbs, M.3
  • 148
    • 0026447426 scopus 로고
    • Function and evolution of a minimal plastid genome form a nonphotosynthetic parasitic plant
    • Wolfe KH, Morden CW, Palmer JD. 1992. Function and evolution of a minimal plastid genome form a nonphotosynthetic parasitic plant. Proc. Natl. Acad. Sci. USA 89:10648-52
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10648-10652
    • Wolfe, K.H.1    Morden, C.W.2    Palmer, J.D.3
  • 149
    • 0032910388 scopus 로고    scopus 로고
    • The biogenesis and assembly of photosynthetic proteins in thylakoid membranes
    • Wollman FA, Minai L, Nechushtai R. 1999. The biogenesis and assembly of photosynthetic proteins in thylakoid membranes. Biochim. Biophys. Acta 1411:21-85
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 21-85
    • Wollman, F.A.1    Minai, L.2    Nechushtai, R.3
  • 150
    • 0032741833 scopus 로고    scopus 로고
    • The immutans variegation locus of Arabidopsis defines a mitochondrial alternative oxidase homolog that functions during early chloroplast biogenesis
    • Wu DY, Wright DA, Wetzel C, Voytas DF, Rodermel S. 1999. The immutans variegation locus of Arabidopsis defines a mitochondrial alternative oxidase homolog that functions during early chloroplast biogenesis. Plant Cell 11:43-55
    • (1999) Plant Cell , vol.11 , pp. 43-55
    • Wu, D.Y.1    Wright, D.A.2    Wetzel, C.3    Voytas, D.F.4    Rodermel, S.5
  • 151
    • 0024656031 scopus 로고
    • The 18-kD protein that binds to the chloroplast DNA replicative origin is an iron-sulfur protein related to a subunit of NADH dehydrogenase
    • Wu M, Nie ZQ, Yang J. 1989. The 18-kD protein that binds to the chloroplast DNA replicative origin is an iron-sulfur protein related to a subunit of NADH dehydrogenase. Plant Cell 1:551-57
    • (1989) Plant Cell , vol.1 , pp. 551-557
    • Wu, M.1    Nie, Z.Q.2    Yang, J.3
  • 152
    • 0034051467 scopus 로고    scopus 로고
    • Reduction of Q(A) in the dark: Another cause of fluorescence Fo increases by high temperatures in higher plants
    • Yamane Y, Shikanai T, Kashino Y, Koike H, Satoh K. 2000. Reduction of Q(A) in the dark: another cause of fluorescence Fo increases by high temperatures in higher plants. Photosynth. Res. 63:23-34
    • (2000) Photosynth. Res , vol.63 , pp. 23-34
    • Yamane, Y.1    Shikanai, T.2    Kashino, Y.3    Koike, H.4    Satoh, K.5


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