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Volumn 13, Issue 5, 2008, Pages 201-207

Molecular crowding and order in photosynthetic membranes

Author keywords

[No Author keywords available]

Indexed keywords

PLASTOQUINONE;

EID: 43049156431     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tplants.2008.03.001     Document Type: Article
Times cited : (99)

References (36)
  • 1
    • 10044254637 scopus 로고    scopus 로고
    • The complex architecture of oxygenic photosynthesis
    • Nelson N., and Ben-Shem A. The complex architecture of oxygenic photosynthesis. Nat. Rev. Mol. Cell Biol. 5 (2004) 971-982
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 971-982
    • Nelson, N.1    Ben-Shem, A.2
  • 2
    • 33644687594 scopus 로고    scopus 로고
    • Three-dimensional organization of higher plant chloroplast thylakoid membranes revealed by electron tomography
    • Shimoni E., et al. Three-dimensional organization of higher plant chloroplast thylakoid membranes revealed by electron tomography. Plant Cell 17 (2005) 2580-2586
    • (2005) Plant Cell , vol.17 , pp. 2580-2586
    • Shimoni, E.1
  • 3
    • 0035214910 scopus 로고    scopus 로고
    • A quantitative model of the domain structure of the photosynthetic membrane
    • Albertsson P. A quantitative model of the domain structure of the photosynthetic membrane. Trends Plant Sci. 6 (2001) 349-358
    • (2001) Trends Plant Sci. , vol.6 , pp. 349-358
    • Albertsson, P.1
  • 5
    • 0037423884 scopus 로고    scopus 로고
    • State transitions - a question of balance
    • Allen J.F. State transitions - a question of balance. Science 299 (2003) 1530-1532
    • (2003) Science , vol.299 , pp. 1530-1532
    • Allen, J.F.1
  • 6
    • 0000055138 scopus 로고
    • Function of the two cytochrome components in chloroplasts - a working hypothesis
    • Hill R., and Bendall F. Function of the two cytochrome components in chloroplasts - a working hypothesis. Nature 186 (1960) 136-137
    • (1960) Nature , vol.186 , pp. 136-137
    • Hill, R.1    Bendall, F.2
  • 7
    • 77957083058 scopus 로고
    • Lateral diffusion in membranes
    • Lipowsky R., and Sackmann E. (Eds), Elsevier
    • Almeida P.F.F., and Vaz W.L.C. Lateral diffusion in membranes. In: Lipowsky R., and Sackmann E. (Eds). Handbook of biological physics Vol. 1 (1995), Elsevier 305-357
    • (1995) Handbook of biological physics , vol.1 , pp. 305-357
    • Almeida, P.F.F.1    Vaz, W.L.C.2
  • 8
    • 0037117740 scopus 로고    scopus 로고
    • Molecular architecture of the thylakoid membrane: Lipid diffusion space for plastoquinone
    • Kirchhoff H., et al. Molecular architecture of the thylakoid membrane: Lipid diffusion space for plastoquinone. Biochemistry 41 (2002) 4872-4882
    • (2002) Biochemistry , vol.41 , pp. 4872-4882
    • Kirchhoff, H.1
  • 9
    • 3142776351 scopus 로고    scopus 로고
    • Supramolecular photosystem II organization in grana thylakoid membranes: evidence for a structured arrangement
    • Kirchhoff H., et al. Supramolecular photosystem II organization in grana thylakoid membranes: evidence for a structured arrangement. Biochemistry 43 (2004) 9204-9213
    • (2004) Biochemistry , vol.43 , pp. 9204-9213
    • Kirchhoff, H.1
  • 10
    • 0015209679 scopus 로고
    • Enzymic characterization and lipid composition of rat liver subcellular membranes
    • Colbeau A., et al. Enzymic characterization and lipid composition of rat liver subcellular membranes. Biochim. Biophys. Acta 249 (1971) 462-492
    • (1971) Biochim. Biophys. Acta , vol.249 , pp. 462-492
    • Colbeau, A.1
  • 11
    • 0025013378 scopus 로고
    • Mitochondrial contact sites. Lipid composition and dynamics
    • Ardail D., et al. Mitochondrial contact sites. Lipid composition and dynamics. J. Biol. Chem. 265 (1990) 18797-18802
    • (1990) J. Biol. Chem. , vol.265 , pp. 18797-18802
    • Ardail, D.1
  • 13
    • 84935354375 scopus 로고
    • Experimentelle und theortische Untersuchungen des zwischenmolekularen Übergangs von Elektronenanregungsenergie
    • Förster V.T. Experimentelle und theortische Untersuchungen des zwischenmolekularen Übergangs von Elektronenanregungsenergie. Z. Naturforsch. 4 (1949) 321-327
    • (1949) Z. Naturforsch. , vol.4 , pp. 321-327
    • Förster, V.T.1
  • 14
    • 37749034529 scopus 로고    scopus 로고
    • Significance of molecular crowding in grana membranes of higher plants for light harvesting by photosystem II
    • Haferkamp S., and Kirchhoff H. Significance of molecular crowding in grana membranes of higher plants for light harvesting by photosystem II. Photosynth. Res. 95 (2008) 129-134
    • (2008) Photosynth. Res. , vol.95 , pp. 129-134
    • Haferkamp, S.1    Kirchhoff, H.2
  • 15
    • 0345170107 scopus 로고    scopus 로고
    • Dependence of plastoquinone diffusion on the shape, size and density of integral thylakoid proteins
    • Tremmel I.G., et al. Dependence of plastoquinone diffusion on the shape, size and density of integral thylakoid proteins. Biochim. Biophys. Acta 1607 (2003) 97-109
    • (2003) Biochim. Biophys. Acta , vol.1607 , pp. 97-109
    • Tremmel, I.G.1
  • 16
    • 0026766411 scopus 로고
    • Plastoquinone compartimentation in chloroplasts. I. Evidence for domains with different rates of photo-reduction
    • Joliot P., et al. Plastoquinone compartimentation in chloroplasts. I. Evidence for domains with different rates of photo-reduction. Biochim. Biophys. Acta 1101 (1992) 1-12
    • (1992) Biochim. Biophys. Acta , vol.1101 , pp. 1-12
    • Joliot, P.1
  • 17
    • 0026631287 scopus 로고
    • Plastoquinone compartimentation in chloroplasts. II. Theoretical aspects
    • Lavergne J., et al. Plastoquinone compartimentation in chloroplasts. II. Theoretical aspects. Biochim. Biophys. Acta. 1101 (1992) 13-22
    • (1992) Biochim. Biophys. Acta. , vol.1101 , pp. 13-22
    • Lavergne, J.1
  • 18
    • 33846968150 scopus 로고    scopus 로고
    • Supramolecular structure of the mitochondrial oxidative phosphorylation system
    • Boekema E.J., and Braun H.-P. Supramolecular structure of the mitochondrial oxidative phosphorylation system. J. Biol. Chem. 282 (2007) 1-4
    • (2007) J. Biol. Chem. , vol.282 , pp. 1-4
    • Boekema, E.J.1    Braun, H.-P.2
  • 19
    • 0028295574 scopus 로고
    • Electron microscopic structural analysis of photosystem I, photosystem II, and the cytochrome b6/f complex from green plants and cyanobacteria
    • Boekema E.J., et al. Electron microscopic structural analysis of photosystem I, photosystem II, and the cytochrome b6/f complex from green plants and cyanobacteria. J. Bioenerg. Biomembr. 26 (1994) 17-29
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 17-29
    • Boekema, E.J.1
  • 20
    • 4344704617 scopus 로고    scopus 로고
    • The native architecture of a photosynthetic membrane
    • Bahatyrova S., et al. The native architecture of a photosynthetic membrane. Nature 430 (2004) 1058-1062
    • (2004) Nature , vol.430 , pp. 1058-1062
    • Bahatyrova, S.1
  • 21
    • 0002276039 scopus 로고
    • Photoregulation of the composition, function, and structure of thylakoid membranes
    • Anderson J.M. Photoregulation of the composition, function, and structure of thylakoid membranes. Annu. Rev. Plant Physiol. 37 (1986) 93-136
    • (1986) Annu. Rev. Plant Physiol. , vol.37 , pp. 93-136
    • Anderson, J.M.1
  • 22
    • 34848816208 scopus 로고    scopus 로고
    • Low-light formation of semicrystalline photosystem II arrays on higher plant chloroplasts
    • Kirchhoff H., et al. Low-light formation of semicrystalline photosystem II arrays on higher plant chloroplasts. Biochemistry 46 (2007) 11169-11176
    • (2007) Biochemistry , vol.46 , pp. 11169-11176
    • Kirchhoff, H.1
  • 23
    • 0037267882 scopus 로고    scopus 로고
    • Chloroplast redox signals: how photosynthesis controls its own genes
    • Pfannschmidt T. Chloroplast redox signals: how photosynthesis controls its own genes. Trends Plant Sci. 8 (2003) 33-41
    • (2003) Trends Plant Sci. , vol.8 , pp. 33-41
    • Pfannschmidt, T.1
  • 24
    • 43049166553 scopus 로고    scopus 로고
    • Protein diffusion and macromolecular crowding in thylakoid membranes
    • Kirchhoff H., et al. Protein diffusion and macromolecular crowding in thylakoid membranes. Plant Physiol. 146 (2008) 1571-1578
    • (2008) Plant Physiol. , vol.146 , pp. 1571-1578
    • Kirchhoff, H.1
  • 25
    • 11044234285 scopus 로고    scopus 로고
    • Supramolecular organization of thylakoid membrane proteins in green plants
    • Dekker J.P., and Boekema E.J. Supramolecular organization of thylakoid membrane proteins in green plants. Biochim. Biophys. Acta 1706 (2005) 12-39
    • (2005) Biochim. Biophys. Acta , vol.1706 , pp. 12-39
    • Dekker, J.P.1    Boekema, E.J.2
  • 26
    • 0001532210 scopus 로고
    • Photosynthetic acclimation of Alocasia macrorrhiza (L.) G. don to growth irradiance: structure, function and composition of chloroplasts
    • Chow W.S., et al. Photosynthetic acclimation of Alocasia macrorrhiza (L.) G. don to growth irradiance: structure, function and composition of chloroplasts. Aust. J. Plant Physiol. 15 (1988) 107-122
    • (1988) Aust. J. Plant Physiol. , vol.15 , pp. 107-122
    • Chow, W.S.1
  • 27
    • 0036097272 scopus 로고    scopus 로고
    • A large population of small chloroplasts in tobacco leaf cells allows more efficient chloroplast movement than a few enlarged chloroplasts
    • Jeong W.J., et al. A large population of small chloroplasts in tobacco leaf cells allows more efficient chloroplast movement than a few enlarged chloroplasts. Plant Physiol. 129 (2002) 112-121
    • (2002) Plant Physiol. , vol.129 , pp. 112-121
    • Jeong, W.J.1
  • 28
    • 16344363252 scopus 로고    scopus 로고
    • Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 Å resolution
    • Standfuss J., et al. Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 Å resolution. EMBO J. 24 (2005) 919-928
    • (2005) EMBO J. , vol.24 , pp. 919-928
    • Standfuss, J.1
  • 29
    • 22144439716 scopus 로고    scopus 로고
    • The influence of protein-protein interations on the organization of proteins within thylakoid membranes
    • Tremmel I.G., et al. The influence of protein-protein interations on the organization of proteins within thylakoid membranes. Biophys. J. 88 (2005) 2650-2660
    • (2005) Biophys. J. , vol.88 , pp. 2650-2660
    • Tremmel, I.G.1
  • 30
    • 8544240147 scopus 로고    scopus 로고
    • Transversal and lateral exciton energy transfer in grana thylakoids of spinach
    • Kirchhoff H., et al. Transversal and lateral exciton energy transfer in grana thylakoids of spinach. Biochemistry 43 (2004) 14508-14516
    • (2004) Biochemistry , vol.43 , pp. 14508-14516
    • Kirchhoff, H.1
  • 31
    • 7244244196 scopus 로고    scopus 로고
    • Lipids do influence protein function - the hydrophobic matching hypothesis revisited
    • Jensen M.O., and Mouritsen O.G. Lipids do influence protein function - the hydrophobic matching hypothesis revisited. Biochim. Biophys. Acta 1666 (2004) 205-226
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 205-226
    • Jensen, M.O.1    Mouritsen, O.G.2
  • 32
    • 7044232102 scopus 로고    scopus 로고
    • Nonbilayer lipids affect peripheral and integral membrane proteins via changes in the lateral pressure profile
    • van den Brinck-van der Laan E., et al. Nonbilayer lipids affect peripheral and integral membrane proteins via changes in the lateral pressure profile. Biochim. Biophys. Acta. 1666 (2004) 275-288
    • (2004) Biochim. Biophys. Acta. , vol.1666 , pp. 275-288
    • van den Brinck-van der Laan, E.1
  • 33
    • 0028239502 scopus 로고
    • Structural characteristics of thylakoid membranes of Arabidopsis mutants deficient in lipid fatty acid desaturation
    • Tsvetkova N.M., et al. Structural characteristics of thylakoid membranes of Arabidopsis mutants deficient in lipid fatty acid desaturation. Biochim. Biophys. Acta 1192 (1994) 263-271
    • (1994) Biochim. Biophys. Acta , vol.1192 , pp. 263-271
    • Tsvetkova, N.M.1
  • 34
    • 38349033143 scopus 로고    scopus 로고
    • Protein shape and crowding drive domain formation and curvature in biological membranes
    • Frese R.N., et al. Protein shape and crowding drive domain formation and curvature in biological membranes. Biophys. J. 94 (2008) 640-647
    • (2008) Biophys. J. , vol.94 , pp. 640-647
    • Frese, R.N.1
  • 35
    • 27644537088 scopus 로고    scopus 로고
    • Function and evolution of grana
    • Mullineaux C.W. Function and evolution of grana. Trends Plant Sci. 10 (2005) 521-525
    • (2005) Trends Plant Sci. , vol.10 , pp. 521-525
    • Mullineaux, C.W.1
  • 36
    • 37849002062 scopus 로고    scopus 로고
    • Probing the organization of photosystem II in photosynthetic membranes by atomic force microscopy
    • Kirchhoff H., et al. Probing the organization of photosystem II in photosynthetic membranes by atomic force microscopy. Biochemistry 47 (2008) 431-440
    • (2008) Biochemistry , vol.47 , pp. 431-440
    • Kirchhoff, H.1


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