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Volumn 41, Issue 1, 2000, Pages 49-59

Identification of the Ndh (NAD(P)H-plastoquinone-oxidoreductase) complex in etioplast membranes of barley: Changes during photomorphogenesis of chloroplasts

Author keywords

Barley (Hordeum vulgare); Etioplasts; NAD(P)H plastoquinone oxidoreductase complex (Ndh complex); Ndh genes; Peroxidase; Photomorphogenesis

Indexed keywords

BARLEY; CHLOROPLAST; ENZYME ACTIVITY; ENZYME SPECIFICITY; ETIOPLAST; MORPHOGENESIS; PHOTOMORPHOGENESIS; PLANT CELL CULTURE; PLASTOQUINONE OXIDOREDUCTASE; POLYACRYLAMIDE GEL ELECTROPHORESIS; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDOREDUCTASE; THYLAKOID; WESTERN BLOTTING;

EID: 0033966275     PISSN: 00320781     EISSN: None     Source Type: Journal    
DOI: 10.1093/pcp/41.1.49     Document Type: Article
Times cited : (41)

References (49)
  • 1
    • 0001155586 scopus 로고    scopus 로고
    • Photosynthetic and heterotrophic ferredoxin isoproteins are colocalized in fruit plastids of tomato
    • Aoki, K., Yamamoto, M. and Wada, K. (1998) Photosynthetic and heterotrophic ferredoxin isoproteins are colocalized in fruit plastids of tomato. Plant Physiol. 118: 439-449.
    • (1998) Plant Physiol. , vol.118 , pp. 439-449
    • Aoki, K.1    Yamamoto, M.2    Wada, K.3
  • 2
    • 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: 4352-4356.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 4352-4356
    • Bennoun, P.1
  • 3
    • 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
  • 4
    • 0002587507 scopus 로고
    • Studies on the expression of NDH-H, a subunit of the NAD(P)H-plasto-quinone-oxidoreductase of higher plant chloroplasts
    • Berger, S., Ellersiek, U., Westhoff, P. and SteinmuÌller, K. (1993) Studies on the expression of NDH-H, a subunit of the NAD(P)H-plasto-quinone-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    SteinmuÌller, K.4
  • 5
    • 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. and Nixon, P.J. (1998) Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes. EMBO J. 17: 868-876.
    • (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
  • 6
    • 0033978632 scopus 로고    scopus 로고
    • Chlororespiration and poising of cyclic electron transport: Plastoquinone as electron transporter between thylakoid NADH dehydrogenase and peroxidase
    • in press
    • Casano, L.M., Zapata, J.M., MartiÌn, M. and Sabater, B. (2000) Chlororespiration and poising of cyclic electron transport: plastoquinone as electron transporter between thylakoid NADH dehydrogenase and peroxidase. J. Biol. Chem. 275: (in press).
    • (2000) J. Biol. Chem. , vol.275
    • Casano, L.M.1    Zapata, J.M.2    MartiÌn, M.3    Sabater, B.4
  • 7
    • 0031440186 scopus 로고    scopus 로고
    • Expression of the plastid ndhF gene product in photosynthetic and non-photosynthetic tissues of developing barley seedlings
    • CatalaÌ R., Sabater, B. and GueÌra, A. (1997) Expression of the plastid ndhF gene product in photosynthetic and non-photosynthetic tissues of developing barley seedlings. Plant Cell Physiol. 38: 1382-1388.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 1382-1388
    • CatalaÌ, R.1    Sabater, B.2    GueÌra, A.3
  • 8
    • 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. and 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
  • 9
    • 0029142099 scopus 로고
    • Properties of a large complex with NADH dehydrogenase activity from barley chloroplasts
    • Cuello, J., Quiles, M.J., Albacete, M.E. and Sabater, B. (1995) Properties of a large complex with NADH dehydrogenase activity from barley chloroplasts. Plant Cell Physiol. 36: 265-271.
    • (1995) Plant Cell Physiol. , vol.36 , pp. 265-271
    • Cuello, J.1    Quiles, M.J.2    Albacete, M.E.3    Sabater, B.4
  • 10
    • 0028248841 scopus 로고
    • Modifications of etioplasts in cotyledons during prolonged dark growth of sugar beet seedlings
    • El Amrani, A., CoueÌe, I., Carde, J.P., GaudilleÌre, J.P. and Raymond, P. (1994) Modifications of etioplasts in cotyledons during prolonged dark growth of sugar beet seedlings. Plant Physiol. 106: 1555-1565.
    • (1994) Plant Physiol. , vol.106 , pp. 1555-1565
    • El Amrani, A.1    CoueÌe, I.2    Carde, J.P.3    GaudilleÌre, J.P.4    Raymond, P.5
  • 11
    • 0000792290 scopus 로고    scopus 로고
    • Nonphotochemical reduction of the plastoquinone pool in sunflower leaves originates from chlororespiration
    • Feild, T.S., Nedbal, L. and Ort, D.R. (1998) Nonphotochemical reduction of the plastoquinone pool in sunflower leaves originates from chlororespiration. Plant Physiol. 116: 1209-1218.
    • (1998) Plant Physiol. , vol.116 , pp. 1209-1218
    • Feild, T.S.1    Nedbal, L.2    Ort, D.R.3
  • 12
    • 84987038916 scopus 로고
    • 4-methoxy-�-naphthol as a specific substrate for kinetic, zymographyc and cytochemical studies on plant peroxidase activities
    • Ferrer, M.A., CalderoÌn, A.A., MunÌ�oz, R. and Ros BarceloÌ A. (1990) 4-methoxy-�-naphthol as a specific substrate for kinetic, zymographyc and cytochemical studies on plant peroxidase activities. Phytochem. Anal. 1: 63.
    • (1990) Phytochem. Anal. , vol.1 , pp. 63
    • Ferrer, M.A.1    CalderoÌn, A.A.2    MunÌ�oz, R.3    Ros BarceloÌ, A.4
  • 13
    • 0030850950 scopus 로고    scopus 로고
    • The expression of subunits of the mitochondrial complex 1-homologous NAD(P)H-plastoquinone oxidoreductase during plastid development
    • Fischer, M., Funk, E. and SteinmuÌller, K. (1997) The expression of subunits of the mitochondrial complex 1-homologous NAD(P)H-plastoquinone oxidoreductase during plastid development. Z. Naturforsch. 52c: 481-486.
    • (1997) Z. Naturforsch. , vol.52 C , pp. 481-486
    • Fischer, M.1    Funk, E.2    SteinmuÌller, K.3
  • 14
    • 0029059910 scopus 로고
    • The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts
    • Friedrich, T., SteinmuÌller, K. and Weiss, H. (1995) The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts. FEBS Lett. 367: 107-111.
    • (1995) FEBS Lett. , vol.367 , pp. 107-111
    • Friedrich, T.1    SteinmuÌller, K.2    Weiss, H.3
  • 15
    • 0001036383 scopus 로고
    • Respiratory control over photosynthetic electron transport in chloroplasts of higher-plant cells: Evidence for chlororespiration
    • Garab, G., LajkoÌ F., MustaÌrdy, L. and MaÌrton, L. (1989) Respiratory control over photosynthetic electron transport in chloroplasts of higher-plant cells: evidence for chlororespiration. Planta 179: 349-358.
    • (1989) Planta , vol.179 , pp. 349-358
    • Garab, G.1    LajkoÌ, F.2    MustaÌrdy, L.3    MaÌrton, L.4
  • 16
    • 0026411481 scopus 로고
    • Ferredoxin and ferredoxin-NADP reductase from photosynthetic and nonphotosynthetic tissues of tomato
    • Green, L.S., Yee, B.C., Buchanan, B.B., Kamide, K., Sanada, Y. and Wada, K. (1991) Ferredoxin and ferredoxin-NADP reductase from photosynthetic and nonphotosynthetic tissues of tomato. Plant Physiol. 96: 1207-1213.
    • (1991) Plant Physiol. , vol.96 , pp. 1207-1213
    • Green, L.S.1    Yee, B.C.2    Buchanan, B.B.3    Kamide, K.4    Sanada, Y.5    Wada, K.6
  • 17
    • 0030043480 scopus 로고    scopus 로고
    • Evidence for an association of ndh B, ndh J gene products and ferredoxin-NADP-reductase as components of a chloroplastic NAD(P)H dehydrogenase complex
    • Guedeney, G., Corneille, S., CuineÌ S. and Peltier, G. (1996) Evidence for an association of ndh B, ndh J gene products and ferredoxin-NADP-reductase as components of a chloroplastic NAD(P)H dehydrogenase complex. FEBS Lett. 378: 277-280.
    • (1996) FEBS Lett. , vol.378 , pp. 277-280
    • Guedeney, G.1    Corneille, S.2    CuineÌ, S.3    Peltier, G.4
  • 18
    • 0023664103 scopus 로고
    • Control of gene expression during higher plant chloroplast biogenesis
    • Klein, R.R. and Mullet, J.E. (1987) Control of gene expression during higher plant chloroplast biogenesis. J. Biol. Chem. 262: 4341-4348.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4341-4348
    • Klein, R.R.1    Mullet, J.E.2
  • 20
    • 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 polyethilene glycol-mediated plastome transformation
    • Kofer, W., Koop, H.-U., Wanner, G. and SteimuÌller, 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 polyethilene glycol-mediated plastome transformation. Mol. Gen. Genet. 258: 166-173.
    • (1998) Mol. Gen. Genet. , vol.258 , pp. 166-173
    • Kofer, W.1    Koop, H.-U.2    Wanner, G.3    SteimuÌller, K.4
  • 21
    • 85047693604 scopus 로고
    • Coproporphyrinogen III oxidase from barley and tobacco-sequence analysis and initial expression studies
    • Kruse, E., Mock, H.P. and Grimm, B. (1995) Coproporphyrinogen III oxidase from barley and tobacco-sequence analysis and initial expression studies. Planta 196: 796-803.
    • (1995) Planta , vol.196 , pp. 796-803
    • Kruse, E.1    Mock, H.P.2    Grimm, B.3
  • 22
    • 0029740614 scopus 로고    scopus 로고
    • 4 plant shorgum bicolor indicates that the complex I-homologous NAD(P)H-plastoquinone oxidoreductase is involved in cyclic electron transport
    • 4 plant Shorgum bicolor indicates that the complex I-homologous NAD(P)H-plastoquinone oxidoreductase is involved in cyclic electron transport. Planta 199: 276-281.
    • (1996) Planta , vol.199 , pp. 276-281
    • Kubicki, A.1    Funk, E.2    Westhoff, P.3    SteinmuÌller, K.4
  • 23
    • 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
    • LajkoÌ F., Kadioglu, A., BorbeÌly, G. and 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: 217-226.
    • (1997) Photosynthetica , vol.33 , pp. 217-226
    • LajkoÌ, F.1    Kadioglu, A.2    BorbeÌly, G.3    Garab, G.4
  • 24
    • 0027435638 scopus 로고
    • Higher plant mitochondria encode an homologue of the nuclear-encoded 30-kDa subunit of bovine mitochondrial complex I
    • Lamattina, L., GonzaÌlez, D., Gualberto, J. and Grienenberger, J.M. (1993) Higher plant mitochondria encode an homologue of the nuclear-encoded 30-kDa subunit of bovine mitochondrial complex I. Eur. J. Biochem. 217: 831-838.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 831-838
    • Lamattina, L.1    GonzaÌlez, D.2    Gualberto, J.3    Grienenberger, J.M.4
  • 25
    • 0030738530 scopus 로고    scopus 로고
    • Cloning and characterization of a plastidial and a mitochondrial isophorm of tobacco protoporphyrinogen IX oxidase
    • Lermontova, I., Kruse, E., Mock, H.P. and Grimm, B. (1997) Cloning and characterization of a plastidial and a mitochondrial isophorm of tobacco protoporphyrinogen IX oxidase. Proc. Natl. Acad. Sci. USA 94: 8895-8900.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8895-8900
    • Lermontova, I.1    Kruse, E.2    Mock, H.P.3    Grimm, B.4
  • 26
    • 77957068711 scopus 로고
    • Chlorophylls and carotenoids pigment of photosynthetic biomembranes
    • Lichtenthaler, H.K. (1987) Chlorophylls and carotenoids pigment of photosynthetic biomembranes. Methods Enzymol. 148: 350-382.
    • (1987) Methods Enzymol. , vol.148 , pp. 350-382
    • Lichtenthaler, H.K.1
  • 28
    • 0030116960 scopus 로고    scopus 로고
    • Identification of the product of ndh A gene as a thylakoid protein synthesized in response to photooxidative treatment
    • MartiÌn, M., Casano, L.M. and Sabater, B. (1996) Identification of the product of ndh A gene as a thylakoid protein synthesized in response to photooxidative treatment. Plant Cell Physiol. 37: 293-298.
    • (1996) Plant Cell Physiol. , vol.37 , pp. 293-298
    • MartiÌn, M.1    Casano, L.M.2    Sabater, B.3
  • 29
    • 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 ndh A and ndhB pre-mRNAs
    • Matsubayashi, T., Wakasugi, T., Shinozaki, K., Yamaguchi-Shinozaki, K., Zaita, N., Hidaka, T., Meng, B.Y., Ohto, C., Tanaka, M., Kato, A., Maruyama, T. and Sugiura, M. (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 ndh A and ndhB pre-mRNAs. Mol. Gen. Genet. 210: 385-393.
    • (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    Hidaka, T.6    Meng, B.Y.7    Ohto, C.8    Tanaka, M.9    Kato, A.10    Maruyama, T.11    Sugiura, M.12
  • 30
    • 0028814979 scopus 로고
    • Thylakoid membrane-bound, NADPH-specific pyridine nucleotide dehydrogenase complex mediates cyclic electron transport in the cyanobacterium Synechocystis sp. PCC 6803
    • Mi, H., Endo, T., Ogawa, T. and Asada, K. (1995) Thylakoid membrane-bound, NADPH-specific pyridine nucleotide dehydrogenase complex mediates cyclic electron transport in the cyanobacterium Synechocystis sp. PCC 6803. Plant Cell Physiol. 36: 661-668.
    • (1995) Plant Cell Physiol. , vol.36 , pp. 661-668
    • Mi, H.1    Endo, T.2    Ogawa, T.3    Asada, K.4
  • 31
    • 0000977339 scopus 로고
    • Purification and characterization of a ferredoxin-NADP oxidoreductase-like enzyme from radish root tissues
    • Morigasaki, S., Takata, K., Suzuki, T. and Wada, K. (1990) Purification and characterization of a ferredoxin-NADP oxidoreductase-like enzyme from radish root tissues. Plant Physiol. 93: 896-901.
    • (1990) Plant Physiol. , vol.93 , pp. 896-901
    • Morigasaki, S.1    Takata, K.2    Suzuki, T.3    Wada, K.4
  • 33
    • 0016711037 scopus 로고
    • High resolution two-dimensional gel electrophoresis of protein
    • O'Farrel, P.M. (1975) High resolution two-dimensional gel electrophoresis of protein. J. Biol. Chem. 250: 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrel, P.M.1
  • 34
  • 35
    • 0030424671 scopus 로고    scopus 로고
    • Isolation and partial characterization of the NADH dehydrogenase complex from barley chloroplast thylakoids
    • Quiles, M.J., Albacete, M.E., Sabater, B. and Cuello, J. (1996) Isolation and partial characterization of the NADH dehydrogenase complex from barley chloroplast thylakoids. Plant Cell Physiol. 37; 1134-1142.
    • (1996) Plant Cell Physiol. , vol.37 , pp. 1134-1142
    • Quiles, M.J.1    Albacete, M.E.2    Sabater, B.3    Cuello, J.4
  • 36
    • 0000662076 scopus 로고    scopus 로고
    • Association of ferredoxin-NADP oxidoreductase with the chloroplastic pyridine nucleotide dehydrogenase complex in barley leaves
    • Quiles, M.J. and Cuello, J. (1998). Association of ferredoxin-NADP oxidoreductase with the chloroplastic pyridine nucleotide dehydrogenase complex in barley leaves. Plant Physiol. 117: 235-244.
    • (1998) Plant Physiol. , vol.117 , pp. 235-244
    • Quiles, M.J.1    Cuello, J.2
  • 37
    • 0000448607 scopus 로고    scopus 로고
    • PORA and PORB, two light-dependent protochlorophyllide-reducing enzymes of angiosperm chlorophyll biosynthesis
    • Reinbothe, S., Reinbothe, C., Lebedev, N. and Apel, K. (1996) PORA and PORB, two light-dependent protochlorophyllide-reducing enzymes of angiosperm chlorophyll biosynthesis. Plant Cell 8: 763-769.
    • (1996) Plant Cell , vol.8 , pp. 763-769
    • Reinbothe, S.1    Reinbothe, C.2    Lebedev, N.3    Apel, K.4
  • 38
    • 0003047177 scopus 로고
    • Localization of manganese superoxide dismutase in peroxisomes isolated from Pisum sativum L
    • Sandalio, L.M., Palma, J.M. and Del Rio, L.A. (1987) Localization of manganese superoxide dismutase in peroxisomes isolated from Pisum sativum L. Plant Sci. 51: 1-8.
    • (1987) Plant Sci. , vol.51 , pp. 1-8
    • Sandalio, L.M.1    Palma, J.M.2    Del Rio, L.A.3
  • 39
    • 0032477715 scopus 로고    scopus 로고
    • The plastid ndh genes code for an NADH-specific dehydrogenase: Isolation of a complex 1 analogue from pea thylakoid membranes
    • Sazanov, L.A., Burrows, P.A. and Nixon, P.J. (1998a) The plastid ndh genes code for an NADH-specific dehydrogenase: isolation of a complex 1 analogue from pea thylakoid membranes. Proc. Natl. Acad. Sci. USA 95: 1319-1324.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1319-1324
    • Sazanov, L.A.1    Burrows, P.A.2    Nixon, P.J.3
  • 40
    • 0032486451 scopus 로고    scopus 로고
    • The chloroplast Ndh complex mediates the dark reduction of the plastoquinone pool in response to heat stress in tobaco leaves
    • Sazanov, L.A., Burrows, P.A. and Nixon, P.J. (1998b) The chloroplast Ndh complex mediates the dark reduction of the plastoquinone pool in response to heat stress in tobaco leaves. FEBS Lett. 429: 115-118.
    • (1998) FEBS Lett. , vol.429 , pp. 115-118
    • Sazanov, L.A.1    Burrows, P.A.2    Nixon, P.J.3
  • 41
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane complexes by two dimensional native electrophoresis
    • SchaÌgger, H., Cramer, W.A. and von Jagow, G. (1994) Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane complexes by two dimensional native electrophoresis. Anal. Biochem. 199: 220-230.
    • (1994) Anal. Biochem. , vol.199 , pp. 220-230
    • SchaÌgger, H.1    Cramer, W.A.2    Von Jagow, G.3
  • 42
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrilamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • SchaÌgger, H. and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrilamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166: 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • SchaÌgger, H.1    Von Jagow, G.2
  • 43
    • 0032567253 scopus 로고    scopus 로고
    • Chlorophyll a formation in the chlorophyll b reductase reaction requires reduced ferredoxin
    • Scheumann, V., Schoch, S. and Rudiger, W. (1998) Chlorophyll a formation in the chlorophyll b reductase reaction requires reduced ferredoxin. J. Biol. Chem. 273: 35102-35108.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35102-35108
    • Scheumann, V.1    Schoch, S.2    Rudiger, W.3
  • 44
    • 0000545202 scopus 로고
    • Purification of peroxisomes and mitochondria from spinach leaf by percoll gradient centrifugation
    • Schwitzguebel, J.-P. and Siegenthaler, P.-A. (1984) Purification of peroxisomes and mitochondria from spinach leaf by percoll gradient centrifugation. Plant Physiol. 75: 670-674.
    • (1984) Plant Physiol. , vol.75 , pp. 670-674
    • Schwitzguebel, J.-P.1    Siegenthaler, P.-A.2
  • 45
    • 0032483030 scopus 로고    scopus 로고
    • Directed disruption of the tobacco ndhB gene impairs cyclic electron flow around photosystem I
    • Shikanai, T., Endo, T., Hashimoto, T., Yamada, Y., Asada, K. and Yokota, A. (1998) Directed disruption of the tobacco ndhB gene impairs cyclic electron flow around photosystem I. Proc. Natl. Acad. Sci. USA 95: 9705-9709.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9705-9709
    • Shikanai, T.1    Endo, T.2    Hashimoto, T.3    Yamada, Y.4    Asada, K.5    Yokota, A.6
  • 46
    • 0026860017 scopus 로고
    • The chloroplast genome
    • Sugiura, M. (1992) The chloroplast genome. Plant Mol. Biol. 19: 149-168.
    • (1992) Plant Mol. Biol. , vol.19 , pp. 149-168
    • Sugiura, M.1
  • 47
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrilamide gels to nitocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrilamide gels to nitocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76: 4350-4353.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4353
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 48
    • 0030792395 scopus 로고    scopus 로고
    • Isomerization of 3,4-dialkyl-1,3,4-thiadiazolines and 3,4-alkylene-1,3,4-thiadizolidines by gluthatione S-transferase
    • Uchida, A., Iida, T., Sato, Y., Boeger, P. and Wakabayasi, K. (1997) Isomerization of 3,4-dialkyl-1,3,4-thiadiazolines and 3,4-alkylene-1,3,4-thiadizolidines by gluthatione S-transferase. Z. Naturforsch.52c: 345-350.
    • (1997) Z. Naturforsch. , vol.52 C , pp. 345-350
    • Uchida, A.1    Iida, T.2    Sato, Y.3    Boeger, P.4    Wakabayasi, K.5
  • 49
    • 0032146623 scopus 로고    scopus 로고
    • Identification of a thylakoid peroxidase of barley which oxidizes hydroquinone
    • Zapata, J.M., Sabater, B. and MartiÌn, M. (1998) Identification of a thylakoid peroxidase of barley which oxidizes hydroquinone. Phytochemistry 48: 1119-1123.
    • (1998) Phytochemistry , vol.48 , pp. 1119-1123
    • Zapata, J.M.1    Sabater, B.2    MartiÌn, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.