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Volumn 64, Issue 6, 2003, Pages 1055-1060

Plastoquinones are effectively reduced by ferredoxin: NADP+ oxidoreductase in the presence of sodium cholate micelles Significance for cyclic electron transport and chlororespiration

Author keywords

Chlororespiration; Ferredoxin NADP+ oxidoreductase; Micelles; Plastoquinone; Sodium cholate

Indexed keywords

CHOLIC ACID; DETERGENT; DODECYL SULFATE SODIUM; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; OCTYL GLUCOSIDE; PLASTOQUINONE DERIVATIVE; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE; TETRADONIUM BROMIDE; TRITON X 100; UNCLASSIFIED DRUG;

EID: 0142026181     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0031-9422(03)00506-5     Document Type: Article
Times cited : (31)

References (38)
  • 2
    • 0031038029 scopus 로고    scopus 로고
    • + reductases: A basal structural framework and a multiplicity of functions
    • + reductases: a basal structural framework and a multiplicity of functions. FASEB J. 11, 133-140.
    • (1997) FASEB J. , vol.11 , pp. 133-140
    • Arakaki, A.K.1    Caccarelli, E.A.2    Carrillo, N.3
  • 3
    • 0028944579 scopus 로고
    • Cyclic photophosphorylation and electron transport
    • Bendall, D.S., Manasse, R.S., 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
  • 4
    • 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. U.S.A. 79, 4352-4356.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 4352-4356
    • Bennoun, P.1
  • 5
    • 0017578884 scopus 로고
    • + reductase in cyclic electron transport in spinach chloroplasts
    • + reductase in cyclic electron transport in spinach chloroplasts. Eur. J. Biochem. 72, 283-289.
    • (1977) Eur. J. Biochem. , vol.72 , pp. 283-289
    • Böhme, H.1
  • 6
    • 0028850963 scopus 로고
    • + oxidoreductase in the presence of dibromothymoquinone
    • + oxidoreductase in the presence of dibromothymoquinone. Phytochemistry 40, 661-665.
    • (1995) Phytochemistry , vol.40 , pp. 661-665
    • Bojko, M.1    Wiȩckowski, S.2
  • 7
    • 0032896141 scopus 로고    scopus 로고
    • + oxidoreductase-dependent reduction of quinones and their reoxidation
    • + oxidoreductase-dependent reduction of quinones and their reoxidation. Phytochemistry 50, 203-208.
    • (1999) Phytochemistry , vol.50 , pp. 203-208
    • Bojko, M.1    Wiȩckowski, S.2
  • 8
    • 0035560577 scopus 로고    scopus 로고
    • + oxidoreductase. Studies with selectively acting inhibitors
    • + oxidoreductase. Studies with selectively acting inhibitors. Photosynthetica 39, 553-556.
    • (2001) Photosynthetica , vol.39 , pp. 553-556
    • Bojko, M.1    Wiȩckowski, S.2
  • 11
    • 0031883125 scopus 로고    scopus 로고
    • Reduction of 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, H., Peltier, G., 1998. Reduction of 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, H.4    Peltier, G.5
  • 12
    • 0016743560 scopus 로고
    • 2 activity toward mixed micelles and its implication for the study of lipolytic enzymes
    • 2 activity toward mixed micelles and its implication for the study of lipolytic enzymes. J. Biol. Chem. 250, 9013-9020.
    • (1975) J. Biol. Chem. , vol.250 , pp. 9013-9020
    • Deems, R.A.1    Eaton, B.R.2    Dennis, E.A.3
  • 13
    • 0000229336 scopus 로고    scopus 로고
    • Donation of electrons to plastoquinone by NAD(P)H dehydrogenase and ferredoxin-quinone reductase in spinach chloroplasts
    • Endo, T., Mi, H., Shikanai, T., Asada, K., 1997. Donation of electrons to plastoquinone by NAD(P)H dehydrogenase and ferredoxin-quinone reductase in spinach chloroplasts. Plant Cell Physiol. 38, 1272-1277.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 1272-1277
    • Endo, T.1    Mi, H.2    Shikanai, T.3    Asada, K.4
  • 14
    • 0002676861 scopus 로고
    • Purification of membrane proteins
    • Harris E.L.V., Angal, S. (Eds.). IRL Press, Oxford
    • Findlay, J.B.C., 1989. Purification of membrane proteins. In: Harris E.L.V., Angal, S. (Eds.), Protein Purification Methods: A Practical Approach. IRL Press, Oxford, pp. 59-82.
    • (1989) Protein Purification Methods: A Practical Approach , pp. 59-82
    • Findlay, J.B.C.1
  • 16
    • 0007719698 scopus 로고
    • ndhB, and ndhI gene products are associated to FNR as components of a chloroplastic NAD(P)H dehydrogenase complex
    • Mathis, P. (Ed.). Kluwer Academic, Dordrecht
    • Guedeney, G., Corneille, S., Cuine, S., Peltier, G., 1995. ndhB, and ndhI gene products are associated to FNR as components of a chloroplastic NAD(P)H dehydrogenase complex. In: Mathis, P. (Ed.), Photosynthesis from Light to Biosphere, Vol. 2. Kluwer Academic, Dordrecht, pp. 883-886.
    • (1995) Photosynthesis from Light to Biosphere , vol.2 , pp. 883-886
    • Guedeney, G.1    Corneille, S.2    Cuine, S.3    Peltier, G.4
  • 17
    • 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, 277-280.
    • (1996) FEBS Lett. , vol.378 , pp. 277-280
    • Guedeney, G.1    Corneille, S.2    Cuine, S.3    Peltier, G.4
  • 18
    • 0032494283 scopus 로고
    • Interdependence between chloroplasts and mitochondria in the light and the dark
    • Hoefnagel, M.H.N., Atkin, O.K., Wiskich, J.T., 1988. Interdependence between chloroplasts and mitochondria in the light and the dark. Biochim. Biophys. Acta 1366, 235-255.
    • (1988) Biochim. Biophys. Acta , vol.1366 , pp. 235-255
    • Hoefnagel, M.H.N.1    Atkin, O.K.2    Wiskich, J.T.3
  • 19
    • 0002598737 scopus 로고
    • Evidence for two cyclic photophosphorylation reactions concurrent with ferredoxin catalyzed noncyclic electron transport
    • Hosler, J.P., Yocum, C.F., 1985. Evidence for two cyclic photophosphorylation reactions concurrent with ferredoxin catalyzed noncyclic 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
  • 20
    • 0030049879 scopus 로고    scopus 로고
    • Location of ubiquinone homologues in liposome membranes studied by fluorescence anisotropy of diphenylhexatriene and trimethyl-ammoniumdiphenylhexatriene
    • Jemioła-Rzemińska, M., Kruk, J., Skowronek, M., Strzałka, K., 1996. Location of ubiquinone homologues in liposome membranes studied by fluorescence anisotropy of diphenylhexatriene and trimethyl-ammoniumdiphenylhexatriene. Chem. Phys. Lipids 79, 55-63.
    • (1996) Chem. Phys. Lipids , vol.79 , pp. 55-63
    • Jemioła-Rzemińska, M.1    Kruk, J.2    Skowronek, M.3    Strzałka, K.4
  • 21
    • 0001244149 scopus 로고
    • Charge-transfer complexes of plastoquinone and α-tocopherol quinone in vitro
    • Kruk, J., 1988. Charge-transfer complexes of plastoquinone and α-tocopherol quinone in vitro. Biophys. Chem. 30, 143-149.
    • (1988) Biophys. Chem. , vol.30 , pp. 143-149
    • Kruk, J.1
  • 22
    • 0343618724 scopus 로고    scopus 로고
    • Dark reoxidation of the PQ-pool proceeds via the low-potential form of cytochrome b-559 in spinach thylakoids
    • Kruk, J., Strzałka, K., 1999. Dark reoxidation of the PQ-pool proceeds via the low-potential form of cytochrome b-559 in spinach thylakoids. Photosynth. Res. 62, 273-279.
    • (1999) Photosynth. Res. , vol.62 , pp. 273-279
    • Kruk, J.1    Strzałka, K.2
  • 23
    • 0027275011 scopus 로고
    • Fluorescence properties of plastoquinol, ubiquinol and α-tocopherol quinol in solution and liposome membranes
    • Kruk, J., Strzałka, K., Leblanc, R.M., 1993. Fluorescence properties of plastoquinol, ubiquinol and α-tocopherol quinol in solution and liposome membranes. J. Photochem. Photobiol. B 19, 23-38.
    • (1993) J. Photochem. Photobiol. B , vol.19 , pp. 23-38
    • Kruk, J.1    Strzałka, K.2    Leblanc, R.M.3
  • 25
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • LeMaire, M., Champeil, P., Møller, J.V., 2000. Interaction of membrane proteins and lipids with solubilizing detergents. Biochim. Biophys. Acta 1508, 86-111.
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 86-111
    • LeMaire, M.1    Champeil, P.2    Møller, J.V.3
  • 26
    • 0022929856 scopus 로고
    • + oxidoreductase from thylakoid membranes, rebinding to depleted membranes and identification of the binding site
    • + oxidoreductase from thylakoid membranes, rebinding to depleted membranes and identification of the binding site. J. Biol. Chem. 261, 12154-12158.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12154-12158
    • Matthijs, H.C.P.1    Coughlan, S.J.2    Hind, G.3
  • 27
    • 34547115717 scopus 로고
    • Cyclic electron transport in chloroplasts. The Q-cycle and the site of action of antimycin
    • Moss, D.A., Bendall, D.S., 1984. Cyclic electron transport in chloroplasts. The Q-cycle and the site of action of antimycin. Biochim. Biophys. Acta 767 389-395.
    • (1984) Biochim. Biophys. Acta , vol.767 , pp. 389-395
    • Moss, D.A.1    Bendall, D.S.2
  • 31
    • 0034043661 scopus 로고    scopus 로고
    • Separation by blue-native PAGE and identification of the whole NAD(P)H dehydrogenase complex from barley stroma thylakoids
    • Quilles, M.J., Garcia, A., Cuello, J., 2000. Separation by blue-native PAGE and identification of the whole NAD(P)H dehydrogenase complex from barley stroma thylakoids. Plant Physiol. Biochem. 38, 225-232.
    • (2000) Plant Physiol. Biochem. , vol.38 , pp. 225-232
    • Quilles, M.J.1    Garcia, A.2    Cuello, J.3
  • 32
    • 0025195184 scopus 로고
    • + distributions in the headgroup regions of binary membranes of phosphatidylcholine and phosphatidylserine as seen by the deuterium NMR
    • + distributions in the headgroup regions of binary membranes of phosphatidylcholine and phosphatidylserine as seen by the deuterium NMR. Biochemistry 29, 7077-7089.
    • (1990) Biochemistry , vol.29 , pp. 7077-7089
    • Roux, M.1    Bloom, M.2
  • 34
    • 0014686224 scopus 로고
    • Studies of simple and mixed bile salt micelles by nuclear magnetic resonance spectroscopy
    • Small, D.M., Penkett, S.A., Chapman, D., 1969. Studies of simple and mixed bile salt micelles by nuclear magnetic resonance spectroscopy. Biochim. Biophys. Acta 176, 178-189.
    • (1969) Biochim. Biophys. Acta , vol.176 , pp. 178-189
    • Small, D.M.1    Penkett, S.A.2    Chapman, D.3
  • 35
    • 0031659943 scopus 로고    scopus 로고
    • Micelle formation of sodium cholate and solubilization into micelle
    • Sugioka, H., Moroi, Y., 1998. Micelle formation of sodium cholate and solubilization into micelle. Biochim. Biophys. Acta 1394, 99-110.
    • (1998) Biochim. Biophys. Acta , vol.1394 , pp. 99-110
    • Sugioka, H.1    Moroi, Y.2
  • 36
    • 0034707088 scopus 로고    scopus 로고
    • The vesicle-to-micelle transition of phosphatidylcholine vesicles induced by nonionic detergents: Effects of sodium chloride, sucrose and urea
    • Walter, A., Kuehl, G., Barnes, K., Vandwaerdt, G., 2000. The vesicle-to-micelle transition of phosphatidylcholine vesicles induced by nonionic detergents: effects of sodium chloride, sucrose and urea. Biochim. Biophys. Acta 1508, 20-33.
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 20-33
    • Walter, A.1    Kuehl, G.2    Barnes, K.3    Vandwaerdt, G.4
  • 37
    • 0031291196 scopus 로고    scopus 로고
    • The NADPH-dependent electron flow in chloroplasts of the higher plants
    • Wiȩckowski, S., Bojko, M., 1997. The NADPH-dependent electron flow in chloroplasts of the higher plants. Photosynthetica 34, 481-496.
    • (1997) Photosynthetica , vol.34 , pp. 481-496
    • Wiȩckowski, S.1    Bojko, M.2


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