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Volumn 269, Issue 18, 2002, Pages 4656-4665

Kinetics of violaxanthin de-epoxidation by violaxanthin de-epoxidase, a xanthophyll cycle enzyme, is regulated by membrane fluidity in model lipid bilayers

Author keywords

De epoxidation; Liposomes; Violaxanthin; Xanthophyll cycle; Zeaxanthin

Indexed keywords

VIOLAXANTHIN; XANTHOPHYLL; ZEAXANTHIN;

EID: 0036380814     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03166.x     Document Type: Article
Times cited : (77)

References (36)
  • 1
    • 0014910933 scopus 로고
    • The carotenoid pattern and the occurence of the light induced xanthophyll cycle in various classes of algae part 6 chemo systematic study
    • Stransky, H. & Hager, A. (1970) The carotenoid pattern and the occurence of the light induced xanthophyll cycle in various classes of algae part 6 chemo systematic study. Arch. Microbiol. 73, 315-323.
    • (1970) Arch. Microbiol. , vol.73 , pp. 315-323
    • Stransky, H.1    Hager, A.2
  • 3
    • 0031588952 scopus 로고    scopus 로고
    • Purification and properties of violaxanthin de-epoxidase from spinach
    • Havir, E.A., Tausta, L.S. & Peterson, R.B. (1997) Purification and properties of violaxanthin de-epoxidase from spinach. Plant Sci. 123, 57-66.
    • (1997) Plant Sci. , vol.123 , pp. 57-66
    • Havir, E.A.1    Tausta, L.S.2    Peterson, R.B.3
  • 4
    • 0030060496 scopus 로고    scopus 로고
    • Purification of a 43-kilodalton lumen protein from lettuce by lipid-affinity precipitation with monogalactosyldiacylglyceride
    • Rockholm, D.C. & Yamamoto, H.Y. (1996) Purification of a 43-kilodalton lumen protein from lettuce by lipid-affinity precipitation with monogalactosyldiacylglyceride. Plant Physiol. 110, 697-703.
    • (1996) Plant Physiol. , vol.110 , pp. 697-703
    • Rockholm, D.C.1    Yamamoto, H.Y.2
  • 5
    • 0010501804 scopus 로고
    • Partial purification of the violaxanthin de-epoxidase
    • P. Mathis, ed. Kluwer Academic Publishers, Dortrecht
    • Åkerlund, H.-E., Arvidson, P.-O., Bratt, C.E. & Carlsson, M. (1995) Partial purification of the violaxanthin de-epoxidase. In Photosynthesis from Light to Biosphere (P. Mathis, ed.), Vol. IV, pp. 103-106. Kluwer Academic Publishers, Dortrecht.
    • (1995) Photosynthesis from Light to Biosphere , vol.4 , pp. 103-106
    • Åkerlund, H.-E.1    Arvidson, P.-O.2    Bratt, C.E.3    Carlsson, M.4
  • 6
    • 0030011229 scopus 로고    scopus 로고
    • Molecular cloning of violaxanthin de-epoxidase from romaine lettuce and expression in Escherichia coli
    • Bugos, R.C. & Yamamoto, H.Y. (1996) Molecular cloning of violaxanthin de-epoxidase from romaine lettuce and expression in Escherichia coli. Proc. Natl Acad. Sci. USA 93, 6320-6325.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6320-6325
    • Bugos, R.C.1    Yamamoto, H.Y.2
  • 7
    • 0001227304 scopus 로고
    • Lichtbedingte pH-erniedringung in einem chloroplasten-kompartiment als ursache der enzymatichen violaxanthin-zu zeaxanthin - Umwandlung beziehungen zur photophosphorylierung
    • Hager. A. (1969) Lichtbedingte pH-Erniedringung in einem Chloroplasten-Kompartiment als Ursache der Enzymatichen Violaxanthin-zu Zeaxanthin - Umwandlung Beziehungen zur Photophosphorylierung. Planta 89, 224-243.
    • (1969) Planta , vol.89 , pp. 224-243
    • Hager, A.1
  • 8
    • 34249758236 scopus 로고
    • Regulation of violaxanthin de-epoxidase activity by pH and ascorbate concentration
    • Bratt, C.E., Arvidsson, P.-O., Carlsson, M. & Åkerlund, H.-E. (1995) Regulation of violaxanthin de-epoxidase activity by pH and ascorbate concentration. Photosynth. Res. 45, 169-175.
    • (1995) Photosynth. Res. , vol.45 , pp. 169-175
    • Bratt, C.E.1    Arvidsson, P.-O.2    Carlsson, M.3    Åkerlund, H.-E.4
  • 9
    • 0028004703 scopus 로고
    • Localization of the xanthophyll cycle enzyme violaxanthin de-epoxidase within the thylakoid lumen and abolition of its mobility by a (light-dependent) pH decrease
    • Hager, A. & Holocher, K. (1994) Localization of the xanthophyll cycle enzyme violaxanthin de-epoxidase within the thylakoid lumen and abolition of its mobility by a (light-dependent) pH decrease. Planta 192, 581-589.
    • (1994) Planta , vol.192 , pp. 581-589
    • Hager, A.1    Holocher, K.2
  • 11
    • 0000484207 scopus 로고
    • Reassembly of solubilized chlorophyll-protein complexes in proteolipid particles-comparison of monogalactosyldiacylglycerol and two phospholipids
    • Siefierman-Harms, D., Ninnemann, H. & Yamamoto, H.Y. (1987) Reassembly of solubilized chlorophyll-protein complexes in proteolipid particles-comparison of monogalactosyldiacylglycerol and two phospholipids. Biochim. Biophys. Acta 892, 303-313.
    • (1987) Biochim. Biophys. Acta , vol.892 , pp. 303-313
    • Siefierman-Harms, D.1    Ninnemann, H.2    Yamamoto, H.Y.3
  • 12
    • 0026008797 scopus 로고
    • Biochemical and biophysical properties of thylakoid acyl lipids
    • Webb, M. & Green, B. (1991) Biochemical and biophysical properties of thylakoid acyl lipids. Biochim. Biophys. Acta 1060, 133-158.
    • (1991) Biochim. Biophys. Acta , vol.1060 , pp. 133-158
    • Webb, M.1    Green, B.2
  • 13
    • 0016737865 scopus 로고
    • A model for the packing of lipids in bilayer membranes
    • Israelachvili, J.N. & Mitchell, D.J. (1975) A model for the packing of lipids in bilayer membranes. Biochim. Biophys. Acta. 389, 13-19.
    • (1975) Biochim. Biophys. Acta , vol.389 , pp. 13-19
    • Israelachvili, J.N.1    Mitchell, D.J.2
  • 14
    • 0001024136 scopus 로고
    • Different aspects of protective of the xanthophyll cycle under stress conditions
    • Gruszecki, W.I. (1995) Different aspects of protective of the xanthophyll cycle under stress conditions. Acta Physiol. Plant. 17, 145-152.
    • (1995) Acta Physiol. Plant. , vol.17 , pp. 145-152
    • Gruszecki, W.I.1
  • 15
    • 0030812109 scopus 로고    scopus 로고
    • Violaxanthin accessibility and temperature dependency for de-epoxidation in spinach thylakoid membranes
    • Arvidsson, P.-O., Carlsson, H., Stefansson, H., Albertsson, P.-A. & Åkerlund, H.-E. (1997) Violaxanthin accessibility and temperature dependency for de-epoxidation in spinach thylakoid membranes. Photosynth. Res. 52, 39-48.
    • (1997) Photosynth. Res. , vol.52 , pp. 39-48
    • Arvidsson, P.-O.1    Carlsson, H.2    Stefansson, H.3    Albertsson, P.-A.4    Åkerlund, H.-E.5
  • 16
    • 84957289476 scopus 로고
    • Organization of carotenoid-phospholipid bilayer systems incorporation of zeaxanthin and their C-50 homologues into dimyristoylphosphatidylcholine vesicles
    • Milton, A., Wolff, G., Ourisson, G. & Nakatani, Y. (1986) Organization of carotenoid-phospholipid bilayer systems incorporation of zeaxanthin and their C-50 homologues into dimyristoylphosphatidylcholine vesicles. Helv. Chim. Acta 69, 12-24.
    • (1986) Helv. Chim. Acta , vol.69 , pp. 12-24
    • Milton, A.1    Wolff, G.2    Ourisson, G.3    Nakatani, Y.4
  • 17
    • 0034470076 scopus 로고    scopus 로고
    • Effect of monogalactosyldiacylglycerol and other thylakoid lipids on violaxanthin de-epoxidation in liposomes
    • Latowski, D., Kostecka, A. & Strzalka, K. (2000) Effect of monogalactosyldiacylglycerol and other thylakoid lipids on vio-laxanthin de-epoxidation in liposomes. Bioch. Soc. Trans., Vol. 28 Part. 6, 810-812.
    • (2000) Bioch. Soc. Trans. , vol.28 , Issue.PART 6 , pp. 810-812
    • Latowski, D.1    Kostecka, A.2    Strzalka, K.3
  • 18
    • 0011071824 scopus 로고
    • Formation and properties of 1000 Å-diameter, single-bilayer phospholipidvesicles
    • Enoch, H.G. & Stritmatter, P. (1979) Formation and properties of 1000 Å-diameter, single-bilayer phospholipidvesicles. Proc. Natl Acad. Sci. USA 76, 145-149.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 145-149
    • Enoch, H.G.1    Stritmatter, P.2
  • 19
    • 0000523021 scopus 로고
    • Carotenoids
    • Goodwin, T.W., ed. Academic Press, London New York San Francisco
    • Davies, B.H. (1976) Carotenoids. In Chemistry and Biochemistry of Plant Pigments (Goodwin, T.W., ed.), pp. 65-66. Academic Press, London New York San Francisco.
    • (1976) Chemistry and Biochemistry of Plant Pigments , pp. 65-66
    • Davies, B.H.1
  • 20
    • 0000171640 scopus 로고
    • Xanthophyll cycle
    • Yamamoto, H.Y. (1995) Xanthophyll cycle. Meth Enzymol. 110, 303-312.
    • (1995) Meth. Enzymol. , vol.110 , pp. 303-312
    • Yamamoto, H.Y.1
  • 21
    • 0025869235 scopus 로고
    • 18 high-performance liquid chromatographic column
    • 18 high-performance liquid chromatographic column. J. Chrom. 543, 137-145.
    • (1991) J. Chrom. , vol.543 , pp. 137-145
    • Gilmore, A.M.1    Yamamoto, H.Y.2
  • 22
    • 0034699782 scopus 로고    scopus 로고
    • A mathematical model describing kinetics of conversion of violaxanthin to zeaxanthin via intermediate antheraxanthin by the xanthophyll cycle enzyme violaxanthin de-epoxidase
    • Latowski, D., Burda, K. & Strzalka, K. (2000) A mathematical model describing kinetics of conversion of violaxanthin to zeaxanthin via intermediate antheraxanthin by the xanthophyll cycle enzyme violaxanthin de-epoxidase. J. Theor. Biol. 206, 507-514.
    • (2000) J. Theor. Biol. , vol.206 , pp. 507-514
    • Latowski, D.1    Burda, K.2    Strzalka, K.3
  • 23
    • 0001673390 scopus 로고
    • Effect of reconstitution method on the structural organization of isolated chloroplast membrane lipids
    • Sprague, G.S. & Staehelin, L.A. (1984) Effect of Reconstitution Method on the structural organization of isolated chloroplast membrane lipids. Biochim. Biophys. Acta 777, 306-322.
    • (1984) Biochim. Biophys. Acta , vol.777 , pp. 306-322
    • Sprague, G.S.1    Staehelin, L.A.2
  • 24
    • 0032993865 scopus 로고    scopus 로고
    • Light-induced formation of 13-cis violaxanthin in leaves of Hordeum vulgarum
    • Phillip, D., Molnar, P., Toth, G. & Young, A.J. (1999) Light-induced formation of 13-cis violaxanthin in leaves of Hordeum vulgarum. J. Photochem. Photobiol. B: Biol. 49, 89-95.
    • (1999) J. Photochem. Photobiol. B: Biol. , vol.49 , pp. 89-95
    • Phillip, D.1    Molnar, P.2    Toth, G.3    Young, A.J.4
  • 25
    • 0034684163 scopus 로고    scopus 로고
    • Plant lipocalins: Violaxanthin de-epoxidase and zeaxanthin epoxidase
    • Hieber, A.D., Bugos, R.C. & Yamamoto, H.Y. (2000) Plant lipocalins: violaxanthin de-epoxidase and zeaxanthin epoxidase. Biochim. Biophys. Acta. 1482, 84-91.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 84-91
    • Hieber, A.D.1    Bugos, R.C.2    Yamamoto, H.Y.3
  • 28
    • 0019885231 scopus 로고
    • Analysis of the hexagonal II phase and its relations to lipidic particles and the lamellar phase. A freeze-fracture study
    • Venetië, R.V. & Verkleij, A.J. (1981) Analysis of the hexagonal II phase and its relations to lipidic particles and the lamellar phase. A freeze-fracture study. Biochim. Biophys. Acta. 645, 262-269.
    • (1981) Biochim. Biophys. Acta , vol.645 , pp. 262-269
    • Venetië, R.V.1    Verkleij, A.J.2
  • 29
    • 0010462322 scopus 로고
    • 31P-NMR observation of the temperature and glycerol induced non-lamellar phase formation in wheat thylakoid membranes
    • 31P-NMR observation of the temperature and glycerol induced non-lamellar phase formation in wheat thylakoid membranes. J. Biol. Phys. 21, 125-139.
    • (1995) J. Biol. Phys. , vol.21 , pp. 125-139
    • Harañczyk, H.1    Strzalka, K.2    Dietrich, W.3    Blicharski, J.S.4
  • 30
    • 48749149633 scopus 로고
    • The structural role of lipids in photosynthetic membranes
    • Quinn, P.J. & Williams, W.P. (1983) The structural role of lipids in photosynthetic membranes. Biochim. Biophys. Acta. 737, 223-266.
    • (1983) Biochim. Biophys. Acta , vol.737 , pp. 223-266
    • Quinn, P.J.1    Williams, W.P.2
  • 31
    • 0003096624 scopus 로고
    • The formation of non-bilayer structures in total polar lipid extracts of chloroplast membranes
    • Gounaris, K., Sen, A., Brain, A.P.R., Quinn, P. & Williams, W.P. (1983) The formation of non-bilayer structures in total polar lipid extracts of chloroplast membranes. Biochim. Biophys. Acta. 728, 129-139.
    • (1983) Biochim. Biophys. Acta , vol.728 , pp. 129-139
    • Gounaris, K.1    Sen, A.2    Brain, A.P.R.3    Quinn, P.4    Williams, W.P.5
  • 32
    • 0018129919 scopus 로고
    • Violaxanthin de-epoxidase. Lipid composition and substrate specifity
    • Yamamoto, H.Y. & Higashi, R.M. (1978) Violaxanthin de-epoxidase. Lipid composition and substrate specifity. Arch. Bioch. Biophys. 190, 514-522.
    • (1978) Arch. Bioch. Biophys. , vol.190 , pp. 514-522
    • Yamamoto, H.Y.1    Higashi, R.M.2
  • 33
    • 0027987397 scopus 로고
    • The protective function of the xanthophyll cycle in photosynthesis
    • Sarry, J.-E., Montillet, J.-L., Sauvaire, Y. & Havaux, M. (1994) The protective function of the xanthophyll cycle in photosynthesis. FEBS Lett. 353, 147-150.
    • (1994) FEBS Lett. , vol.353 , pp. 147-150
    • Sarry, J.-E.1    Montillet, J.-L.2    Sauvaire, Y.3    Havaux, M.4
  • 34
    • 0026062916 scopus 로고
    • Does the xanthophyll cycle take part in the regulation of fluidity of the thylakoid membrane?
    • Gruszecki, W.I. & Strzalka, K. (1991) Does the xanthophyll cycle take part in the regulation of fluidity of the thylakoid membrane? Biochim. Biophys. Acta. 1060, 310-314.
    • (1991) Biochim. Biophys. Acta , vol.1060 , pp. 310-314
    • Gruszecki, W.I.1    Strzalka, K.2
  • 35
    • 0030807802 scopus 로고    scopus 로고
    • Thylakoid membrane fluidity and thermostability during the operation of the xanthophyll cycle in higher-plant chloroplasts
    • Tardy, F. & Havaux, H. (1997) Thylakoid membrane fluidity and thermostability during the operation of the xanthophyll cycle in higher-plant chloroplasts. Biochim. Biophys. Acta 1330, 179-193.
    • (1997) Biochim. Biophys. Acta , vol.1330 , pp. 179-193
    • Tardy, F.1    Havaux, H.2
  • 36
    • 0001329893 scopus 로고    scopus 로고
    • Modulation of thylakoid membrane fluidity by exogenously added carotenoids
    • Strzalka, K. & Gruszecki, W. (1997) Modulation of thylakoid membrane fluidity by exogenously added carotenoids. J. Biochem. Mol. Biol. Biophys. 1, 103-108.
    • (1997) J. Biochem. Mol. Biol. Biophys. , vol.1 , pp. 103-108
    • Strzalka, K.1    Gruszecki, W.2


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