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Volumn 1777, Issue 4, 2008, Pages 351-361

Photosystem I complexes associated with fucoxanthin-chlorophyll-binding proteins from a marine centric diatom, Chaetoceros gracilis

Author keywords

Chaetoceros gracilis; Diatom; Fucoxanthin chlorophyll binding protein; Photosystem I; Time resolved fluorescence spectra

Indexed keywords

BINDING PROTEIN; CHLOROPHYLL; FUCOXANTHIN; MENATETRENONE; PHYTOMENADIONE;

EID: 40949140065     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2008.01.011     Document Type: Article
Times cited : (75)

References (64)
  • 2
    • 0029540174 scopus 로고
    • Production and dissolution of biogenic silica in the ocean: revised global estimates, comparison with regional data and relationship to biogenic silica sedimentation
    • Nelson D.M., Tréguer P., Brzezinski M.A., Leynaert A., and Quéguiner B. Production and dissolution of biogenic silica in the ocean: revised global estimates, comparison with regional data and relationship to biogenic silica sedimentation. Global Biogeochem. Cycles 9 (1995) 359-372
    • (1995) Global Biogeochem. Cycles , vol.9 , pp. 359-372
    • Nelson, D.M.1    Tréguer, P.2    Brzezinski, M.A.3    Leynaert, A.4    Quéguiner, B.5
  • 3
    • 0032503986 scopus 로고    scopus 로고
    • Primary production of the biosphere: integrating terrestrial and oceanic components
    • Field C.B., Behrenfeld M.J., Randerson J.T., and Falkowski P. Primary production of the biosphere: integrating terrestrial and oceanic components. Science 281 (1998) 237-240
    • (1998) Science , vol.281 , pp. 237-240
    • Field, C.B.1    Behrenfeld, M.J.2    Randerson, J.T.3    Falkowski, P.4
  • 4
    • 6044271639 scopus 로고    scopus 로고
    • Photosynthetic architecture differs in coastal and oceanic diatoms
    • Strzepek R.F., and Harrison P.J. Photosynthetic architecture differs in coastal and oceanic diatoms. Nature 431 (2004) 689-692
    • (2004) Nature , vol.431 , pp. 689-692
    • Strzepek, R.F.1    Harrison, P.J.2
  • 6
    • 33947414878 scopus 로고    scopus 로고
    • Chloroplast genomes of the diatoms Phaeodactylum tricornutum and Thalassiosira pseudonana: comparison with other plastid genomes of the red lineage
    • Oudot-Le Secq M.P., Grimwood J., Shapiro H., Armbrust E.V., Bowler C., and Green B.R. Chloroplast genomes of the diatoms Phaeodactylum tricornutum and Thalassiosira pseudonana: comparison with other plastid genomes of the red lineage. Mol. Genet. Genomics 277 (2007) 427-439
    • (2007) Mol. Genet. Genomics , vol.277 , pp. 427-439
    • Oudot-Le Secq, M.P.1    Grimwood, J.2    Shapiro, H.3    Armbrust, E.V.4    Bowler, C.5    Green, B.R.6
  • 8
    • 40949154902 scopus 로고
    • Regulation of photosystem stoichiometry in oxygenic photosynthesis
    • Miyachi S., Kanai R., and Katoh S. (Eds), The Botanical Society of Japan, Tokyo
    • Melis A. Regulation of photosystem stoichiometry in oxygenic photosynthesis. In: Miyachi S., Kanai R., and Katoh S. (Eds). Regulation of Photosynthetic Processes (1991), The Botanical Society of Japan, Tokyo 9-28
    • (1991) Regulation of Photosynthetic Processes , pp. 9-28
    • Melis, A.1
  • 9
    • 0009814432 scopus 로고
    • Photochemical apparatus organization in the diatom Cylindrotheca fusiformis: photosystem stoichiometry and excitation distribution in cells grown under high and low irradiance
    • Smith B.M., and Melis A. Photochemical apparatus organization in the diatom Cylindrotheca fusiformis: photosystem stoichiometry and excitation distribution in cells grown under high and low irradiance. Plant Cell Physiol. 29 (1988) 761-769
    • (1988) Plant Cell Physiol. , vol.29 , pp. 761-769
    • Smith, B.M.1    Melis, A.2
  • 10
    • 0000046689 scopus 로고
    • Effects of growth irradiance levels on the ratio of reaction centers in two species of marine phytoplankton
    • Falkowski P.G., Owens T.G., Ley A.C., and Mauzerall D.C. Effects of growth irradiance levels on the ratio of reaction centers in two species of marine phytoplankton. Plant Physiol. 68 (1981) 969-973
    • (1981) Plant Physiol. , vol.68 , pp. 969-973
    • Falkowski, P.G.1    Owens, T.G.2    Ley, A.C.3    Mauzerall, D.C.4
  • 12
    • 0000840060 scopus 로고
    • Light-shade adaptation: tow strategies in marine phytoplankton
    • Falkowski P.G., and Owens T.G. Light-shade adaptation: tow strategies in marine phytoplankton. Plant Physiol. 66 (1980) 592-595
    • (1980) Plant Physiol. , vol.66 , pp. 592-595
    • Falkowski, P.G.1    Owens, T.G.2
  • 13
    • 33644901283 scopus 로고    scopus 로고
    • Comparative analysis of photosynthetic properties in ice algae and phytoplankton inhabiting Franklin Bay, the Canadian Arctic, with those in mesophilic diatoms during CASES 03-04
    • Ban A., Aikawa S., Hattori H., Sasaki H., Sampei M., Kudoh S., Fukuchi M., Satoh K., and Kashino Y. Comparative analysis of photosynthetic properties in ice algae and phytoplankton inhabiting Franklin Bay, the Canadian Arctic, with those in mesophilic diatoms during CASES 03-04. Polar Biosci. 19 (2006) 11-28
    • (2006) Polar Biosci. , vol.19 , pp. 11-28
    • Ban, A.1    Aikawa, S.2    Hattori, H.3    Sasaki, H.4    Sampei, M.5    Kudoh, S.6    Fukuchi, M.7    Satoh, K.8    Kashino, Y.9
  • 14
    • 24644509316 scopus 로고    scopus 로고
    • The light-harvesting antenna of the diatom Phaeodactylum tricornutum. Evidence for a diadinoxanthin-binding subcomplex
    • Guglielmi G., Lavaud J., Rousseau B., Etienne A.L., Houmard J., and Ruban A.V. The light-harvesting antenna of the diatom Phaeodactylum tricornutum. Evidence for a diadinoxanthin-binding subcomplex. FEBS J. 272 (2005) 4339-4348
    • (2005) FEBS J. , vol.272 , pp. 4339-4348
    • Guglielmi, G.1    Lavaud, J.2    Rousseau, B.3    Etienne, A.L.4    Houmard, J.5    Ruban, A.V.6
  • 15
    • 0025187594 scopus 로고
    • Carotenoids and photoprotection in plants: a role for the xanthophyll zeaxanthin
    • Demmig-Adams B. Carotenoids and photoprotection in plants: a role for the xanthophyll zeaxanthin. Biochim. Biophys. Acta 1020 (1990) 1-24
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 1-24
    • Demmig-Adams, B.1
  • 16
    • 0028150127 scopus 로고
    • Short-term response of the diadinoxanthin cycle and fluorescence yield to high irradiance in Chaetoceros muelleri (Bacillariophyceae)
    • Olaizola M., and Yamamoto H.Y. Short-term response of the diadinoxanthin cycle and fluorescence yield to high irradiance in Chaetoceros muelleri (Bacillariophyceae). J. Phycol. 30 (1994) 606-612
    • (1994) J. Phycol. , vol.30 , pp. 606-612
    • Olaizola, M.1    Yamamoto, H.Y.2
  • 17
    • 0028035657 scopus 로고
    • Influence of the pool size of the xanthophyll cycle on the effects of light stress in a diatom: competition between photoprotection and photoinhibition
    • Arsalane W., Rousseau B., and Duval J.-C. Influence of the pool size of the xanthophyll cycle on the effects of light stress in a diatom: competition between photoprotection and photoinhibition. Photochem. Photobiol. 60 (1994) 237-243
    • (1994) Photochem. Photobiol. , vol.60 , pp. 237-243
    • Arsalane, W.1    Rousseau, B.2    Duval, J.-C.3
  • 18
    • 0141836158 scopus 로고    scopus 로고
    • Concerted response of xanthophyll-cycle pigments in a marine diatom, Chaetoceros gracilis, to the sifts of light condition
    • Kashino Y., and Kudoh S. Concerted response of xanthophyll-cycle pigments in a marine diatom, Chaetoceros gracilis, to the sifts of light condition. Phycol. Res. 51 (2003) 168-172
    • (2003) Phycol. Res. , vol.51 , pp. 168-172
    • Kashino, Y.1    Kudoh, S.2
  • 19
    • 0000212967 scopus 로고
    • Subunit organization of PSI particles from brown algae and diatoms: polypeptide and pigment analysis
    • Berkaloff C., Caron L., and Rousseau B. Subunit organization of PSI particles from brown algae and diatoms: polypeptide and pigment analysis. Photosynth. Res. 23 (1990) 181-193
    • (1990) Photosynth. Res. , vol.23 , pp. 181-193
    • Berkaloff, C.1    Caron, L.2    Rousseau, B.3
  • 21
    • 33749639074 scopus 로고    scopus 로고
    • Association of fucoxanthin chlorophyll a/c-binding polypeptides with photosystems and phosphorylation in the centric diatom Cyclotella cryptica
    • Brakemann T., Schlörmann W., Marquardt J., Nolte M., and Rhiel E. Association of fucoxanthin chlorophyll a/c-binding polypeptides with photosystems and phosphorylation in the centric diatom Cyclotella cryptica. Protist 157 (2006) 463-475
    • (2006) Protist , vol.157 , pp. 463-475
    • Brakemann, T.1    Schlörmann, W.2    Marquardt, J.3    Nolte, M.4    Rhiel, E.5
  • 22
    • 0348148910 scopus 로고    scopus 로고
    • Crystal structure of plant photosystem I
    • Ben-Shem A., Frolow F., and Nelson N. Crystal structure of plant photosystem I. Nature 426 (2003) 630-635
    • (2003) Nature , vol.426 , pp. 630-635
    • Ben-Shem, A.1    Frolow, F.2    Nelson, N.3
  • 23
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
    • Jordan P., Fromme P., Witt H.T., Klukas O., Saenger W., and Krauß N. Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 411 (2001) 909-917
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauß, N.6
  • 24
    • 73049174685 scopus 로고
    • Studies of marine planktonic diatoms. I. Cyclotella nana Hustedt, and Detonula confervacea (cleve) Gran
    • Guillard R.R., and Ryther J.H. Studies of marine planktonic diatoms. I. Cyclotella nana Hustedt, and Detonula confervacea (cleve) Gran. Can. J. Microbiol. 8 (1962) 229-239
    • (1962) Can. J. Microbiol. , vol.8 , pp. 229-239
    • Guillard, R.R.1    Ryther, J.H.2
  • 25
    • 0037172810 scopus 로고    scopus 로고
    • Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides
    • Kashino Y., Lauber W.M., Carroll J.A., Wang Q., Whitmarsh J., Satoh K., and Pakrasi H.B. Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides. Biochemistry 41 (2002) 8004-8012
    • (2002) Biochemistry , vol.41 , pp. 8004-8012
    • Kashino, Y.1    Lauber, W.M.2    Carroll, J.A.3    Wang, Q.4    Whitmarsh, J.5    Satoh, K.6    Pakrasi, H.B.7
  • 27
    • 0035030294 scopus 로고    scopus 로고
    • An improved sodium dodecyl sulfate-polyacrylamide gel electrophoresis system for the analysis of membrane protein complexes
    • Kashino Y., Koike H., and Satoh K. An improved sodium dodecyl sulfate-polyacrylamide gel electrophoresis system for the analysis of membrane protein complexes. Electrophoresis 22 (2001) 1004-1007
    • (2001) Electrophoresis , vol.22 , pp. 1004-1007
    • Kashino, Y.1    Koike, H.2    Satoh, K.3
  • 28
    • 0001105949 scopus 로고
    • Immunological cross-reactivity among corresponding proteins of photosystems I and II from widely divergent photosynthetic organisms
    • Kashino Y., Enami I., Satoh K., and Katoh S. Immunological cross-reactivity among corresponding proteins of photosystems I and II from widely divergent photosynthetic organisms. Plant Cell Physiol. 31 (1990) 479-488
    • (1990) Plant Cell Physiol. , vol.31 , pp. 479-488
    • Kashino, Y.1    Enami, I.2    Satoh, K.3    Katoh, S.4
  • 29
    • 4444347536 scopus 로고    scopus 로고
    • Blue native electrophoresis
    • Hunte C., von Jagow G., and Schägger H. (Eds), Academic Press, Amsterdam
    • Schägger H. Blue native electrophoresis. In: Hunte C., von Jagow G., and Schägger H. (Eds). Membrane Protein Purification and Crystallization: A Practical Guide (2002), Academic Press, Amsterdam 105-130
    • (2002) Membrane Protein Purification and Crystallization: A Practical Guide , pp. 105-130
    • Schägger, H.1
  • 30
    • 0031878965 scopus 로고    scopus 로고
    • HPLC determination of phytoplankton pigments using N,N-dimethylformamide
    • Furuya K., Hayashi M., and Yabushita Y. HPLC determination of phytoplankton pigments using N,N-dimethylformamide. J. Oceanogr. 54 (1998) 199-203
    • (1998) J. Oceanogr. , vol.54 , pp. 199-203
    • Furuya, K.1    Hayashi, M.2    Yabushita, Y.3
  • 31
    • 77956989125 scopus 로고
    • The structure and function of quinones in respiratory metabolism
    • Vitamins and Coenzymes, Part C. McCormick D.B., and Wright L.D. (Eds), Academic Press, New York
    • Dunphy P.J., and Brodie A.F. The structure and function of quinones in respiratory metabolism. In: McCormick D.B., and Wright L.D. (Eds). Vitamins and Coenzymes, Part C. Methods in Enzymology vol. 18 (1971), Academic Press, New York 407-461
    • (1971) Methods in Enzymology , vol.18 , pp. 407-461
    • Dunphy, P.J.1    Brodie, A.F.2
  • 32
    • 0015516862 scopus 로고
    • Difference spectra and extinction coefficients of P700
    • Hiyama T., and Ke B. Difference spectra and extinction coefficients of P700. Biochim. Biophys. Acta 267 (1972) 160-171
    • (1972) Biochim. Biophys. Acta , vol.267 , pp. 160-171
    • Hiyama, T.1    Ke, B.2
  • 33
    • 0001396452 scopus 로고
    • New spectroscopic equations for determining chlorophylls a, b, c1 and c2 in higher plants, algae and natural phytoplankton
    • Jeffrey S.W., and Humphrey G.F. New spectroscopic equations for determining chlorophylls a, b, c1 and c2 in higher plants, algae and natural phytoplankton. Biochem. Physiol. Pflanzen 167 (1975) 191-194
    • (1975) Biochem. Physiol. Pflanzen , vol.167 , pp. 191-194
    • Jeffrey, S.W.1    Humphrey, G.F.2
  • 34
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: verification of the concentration of chlorophyll standards by atomic absorption spectroscopy
    • Porra R.J., Thompson W.A., and Kriedemann P.E. Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: verification of the concentration of chlorophyll standards by atomic absorption spectroscopy. Biochim. Biophys. Acta 975 (1989) 384-394
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 384-394
    • Porra, R.J.1    Thompson, W.A.2    Kriedemann, P.E.3
  • 35
    • 33751517686 scopus 로고    scopus 로고
    • A new fluorescence band F689 in photosystem II revealed by picosecond analysis at 4-77 K: function of two terminal energy sinks F689 and F695 in PS II
    • Komura M., Shibata Y., and Itoh S. A new fluorescence band F689 in photosystem II revealed by picosecond analysis at 4-77 K: function of two terminal energy sinks F689 and F695 in PS II. Biochim. Biophys. Acta 1757 (2006) 1657-1668
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1657-1668
    • Komura, M.1    Shibata, Y.2    Itoh, S.3
  • 36
    • 24644510206 scopus 로고    scopus 로고
    • PsbU provides a stable architecture for the oxygen-evolving system in cyanobacterial photosystem II
    • Inoue-Kashino N., Kashino Y., Satoh K., Terashima I., and Pakrasi H.B. PsbU provides a stable architecture for the oxygen-evolving system in cyanobacterial photosystem II. Biochemistry 44 (2005) 12214-12228
    • (2005) Biochemistry , vol.44 , pp. 12214-12228
    • Inoue-Kashino, N.1    Kashino, Y.2    Satoh, K.3    Terashima, I.4    Pakrasi, H.B.5
  • 38
    • 0036286172 scopus 로고    scopus 로고
    • Light harvesting in photosystem I: modeling based on the 2.5-Å structure of photosystem I from Synechococcus elongatus
    • Byrdin M., Jordan P., Krauss N., Fromme P., Stehlik D., and Schlodder E. Light harvesting in photosystem I: modeling based on the 2.5-Å structure of photosystem I from Synechococcus elongatus. Biophys. J. 83 (2002) 433-457
    • (2002) Biophys. J. , vol.83 , pp. 433-457
    • Byrdin, M.1    Jordan, P.2    Krauss, N.3    Fromme, P.4    Stehlik, D.5    Schlodder, E.6
  • 39
    • 0242663865 scopus 로고    scopus 로고
    • Separation methods in the analysis of protein membrane complexes
    • Kashino Y. Separation methods in the analysis of protein membrane complexes. J. Chromatogr. B 797 (2003) 191-216
    • (2003) J. Chromatogr. B , vol.797 , pp. 191-216
    • Kashino, Y.1
  • 40
    • 34548286317 scopus 로고    scopus 로고
    • Spectroscopic and molecular characterization of the oligomeric antenna of the diatom Phaeodactylum tricornutum
    • Lepetit B., Volke D., Szabo M., Hoffmann R., Garab G., Wilhelm C., and Goss R. Spectroscopic and molecular characterization of the oligomeric antenna of the diatom Phaeodactylum tricornutum. Biochemistry 46 (2007) 9813-9822
    • (2007) Biochemistry , vol.46 , pp. 9813-9822
    • Lepetit, B.1    Volke, D.2    Szabo, M.3    Hoffmann, R.4    Garab, G.5    Wilhelm, C.6    Goss, R.7
  • 41
    • 34247576821 scopus 로고    scopus 로고
    • The structure of a plant photosystem I supercomplex at 3.4 Å resolution
    • Amunts A., Drory O., and Nelson N. The structure of a plant photosystem I supercomplex at 3.4 Å resolution. Nature 447 (2007) 58-63
    • (2007) Nature , vol.447 , pp. 58-63
    • Amunts, A.1    Drory, O.2    Nelson, N.3
  • 42
    • 36549005048 scopus 로고    scopus 로고
    • The monomeric photosystem I-complex of the diatom Phaeodactylum tricornutum binds specific fucoxanthin chlorophyll proteins (FCPs) as light-harvesting complexes
    • Veith T., and Büchel C. The monomeric photosystem I-complex of the diatom Phaeodactylum tricornutum binds specific fucoxanthin chlorophyll proteins (FCPs) as light-harvesting complexes. Biochim. Biophys. Acta 1767 (2007) 1428-1435
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1428-1435
    • Veith, T.1    Büchel, C.2
  • 43
    • 0242675940 scopus 로고    scopus 로고
    • Fucoxanthin-chlorophyll proteins in diatoms: 18 and 19 kDa subunits assemble into different oligomeric states
    • Büchel C. Fucoxanthin-chlorophyll proteins in diatoms: 18 and 19 kDa subunits assemble into different oligomeric states. Biochemistry 42 (2003) 13027-13034
    • (2003) Biochemistry , vol.42 , pp. 13027-13034
    • Büchel, C.1
  • 44
    • 84985475670 scopus 로고
    • Energy transfer in a light-harvesting carotenoid-chlorophyll c-chlorophyll a-protein of Phaeodactylum tricornutum
    • Gugliemelli L.A., Dutton H.J., Jursinic P.A., and Siegelman H.W. Energy transfer in a light-harvesting carotenoid-chlorophyll c-chlorophyll a-protein of Phaeodactylum tricornutum. Photochem. Photobiol. 33 (1981) 903-907
    • (1981) Photochem. Photobiol. , vol.33 , pp. 903-907
    • Gugliemelli, L.A.1    Dutton, H.J.2    Jursinic, P.A.3    Siegelman, H.W.4
  • 45
  • 47
    • 33751082107 scopus 로고    scopus 로고
    • Subunit composition and pigmentation of fucoxanthin-chlorophyll proteins in diatoms: evidence for a subunit involved in diadinoxanthin and diatoxanthin binding
    • Beer A., Gundermann K., Beckmann J., and Büchel C. Subunit composition and pigmentation of fucoxanthin-chlorophyll proteins in diatoms: evidence for a subunit involved in diadinoxanthin and diatoxanthin binding. Biochemistry 45 (2006) 13046-13053
    • (2006) Biochemistry , vol.45 , pp. 13046-13053
    • Beer, A.1    Gundermann, K.2    Beckmann, J.3    Büchel, C.4
  • 48
    • 25444472561 scopus 로고    scopus 로고
    • Spectroscopic characterization of the excitation energy transfer in the fucoxanthin-chlorophyll protein of diatoms
    • Papagiannakis E., van Stokkum I.H.M., Fey H., Büchel C., and van Grondelle R. Spectroscopic characterization of the excitation energy transfer in the fucoxanthin-chlorophyll protein of diatoms. Photosynth. Res. 86 (2005) 241-250
    • (2005) Photosynth. Res. , vol.86 , pp. 241-250
    • Papagiannakis, E.1    van Stokkum, I.H.M.2    Fey, H.3    Büchel, C.4    van Grondelle, R.5
  • 49
    • 0033729597 scopus 로고    scopus 로고
    • Selective extraction of antenna chlorophylls, carotenoids and quinones from photosystem I reaction center
    • Ikegami I., Itoh S., and Iwaki M. Selective extraction of antenna chlorophylls, carotenoids and quinones from photosystem I reaction center. Plant Cell Physiol. 41 (2000) 1085-1095
    • (2000) Plant Cell Physiol. , vol.41 , pp. 1085-1095
    • Ikegami, I.1    Itoh, S.2    Iwaki, M.3
  • 50
    • 0003003729 scopus 로고
    • Electron transfer in spinach photosystem I reaction center containing benzo-, naphtho- and anthraquinones in place of phylloquinone
    • Iwaki M., and Itoh S. Electron transfer in spinach photosystem I reaction center containing benzo-, naphtho- and anthraquinones in place of phylloquinone. FEBS Lett. 256 (1989) 11-16
    • (1989) FEBS Lett. , vol.256 , pp. 11-16
    • Iwaki, M.1    Itoh, S.2
  • 51
    • 0035955726 scopus 로고    scopus 로고
    • Recruitment of a foreign quinone into the A1 site of photosystem I. In vivo replacement of plastoquinone-9 by media-supplemented naphthoquinones in phylloquinone biosynthetic pathway mutants of Synechocystis sp. PCC 6803
    • Johnson T.W., Zybailov B., Jones A.D., Bittl R., Zech S., Stehlik D., Golbeck J.H., and Chitnis P.R. Recruitment of a foreign quinone into the A1 site of photosystem I. In vivo replacement of plastoquinone-9 by media-supplemented naphthoquinones in phylloquinone biosynthetic pathway mutants of Synechocystis sp. PCC 6803. J. Biol. Chem. 276 (2001) 39512-39521
    • (2001) J. Biol. Chem. , vol.276 , pp. 39512-39521
    • Johnson, T.W.1    Zybailov, B.2    Jones, A.D.3    Bittl, R.4    Zech, S.5    Stehlik, D.6    Golbeck, J.H.7    Chitnis, P.R.8
  • 52
    • 21244467212 scopus 로고    scopus 로고
    • The secondary electron acceptor of photosystem I in Gloeobacter violaceus PCC 7421 is menaquinone-4 that is synthesized by a unique but unknown pathway
    • Mimuro M., Tsuchiya T., Inoue H., Sakuragi Y., Itoh Y., Gotoh T., Miyashita H., Bryant D.A., and Kobayashi M. The secondary electron acceptor of photosystem I in Gloeobacter violaceus PCC 7421 is menaquinone-4 that is synthesized by a unique but unknown pathway. FEBS Lett. 579 (2005) 3493-3496
    • (2005) FEBS Lett. , vol.579 , pp. 3493-3496
    • Mimuro, M.1    Tsuchiya, T.2    Inoue, H.3    Sakuragi, Y.4    Itoh, Y.5    Gotoh, T.6    Miyashita, H.7    Bryant, D.A.8    Kobayashi, M.9
  • 53
    • 0042816294 scopus 로고    scopus 로고
    • Reversed-phase HPLC determination of chlorophyll a' and naphthoquinones in photosystem I of red algae: existence of two menaquinone-4 molecules in photosystem I of Cyanidium caldarium
    • Yoshida E., Nakamura A., and Watanabe T. Reversed-phase HPLC determination of chlorophyll a' and naphthoquinones in photosystem I of red algae: existence of two menaquinone-4 molecules in photosystem I of Cyanidium caldarium. Anal. Sci. 19 (2003) 1001-1005
    • (2003) Anal. Sci. , vol.19 , pp. 1001-1005
    • Yoshida, E.1    Nakamura, A.2    Watanabe, T.3
  • 54
    • 0037614846 scopus 로고    scopus 로고
    • Enrichment of the light-harvesting complex in diadinoxanthin and implications for the nonphotochemical fluorescence quenching in diatoms
    • Lavaud J., Rousseau B., and Etienne A.L. Enrichment of the light-harvesting complex in diadinoxanthin and implications for the nonphotochemical fluorescence quenching in diatoms. Biochemistry 42 (2003) 5802-5808
    • (2003) Biochemistry , vol.42 , pp. 5802-5808
    • Lavaud, J.1    Rousseau, B.2    Etienne, A.L.3
  • 55
    • 0001427672 scopus 로고
    • Light-harvesting function in the diatom Phaeodactylum tricornutum: I. Isolation and characterization of pigment-protein complexes
    • Owens T.G., and Wold E.R. Light-harvesting function in the diatom Phaeodactylum tricornutum: I. Isolation and characterization of pigment-protein complexes. Plant Physiol. 80 (1986) 732-738
    • (1986) Plant Physiol. , vol.80 , pp. 732-738
    • Owens, T.G.1    Wold, E.R.2
  • 56
    • 40949162550 scopus 로고
    • Femtosecond dynamics of carotenoid to chlorophyll energy transfer in thylakoid membrane preparations from Phaeodactylum tricornutum and Nannochloropsis sp
    • Baltscheffsky M. (Ed), Kluwer Academic Publishers, Dordrecht
    • Trautman J.K., Shreve A.P., Owens T.G., and Albrecht A.C. Femtosecond dynamics of carotenoid to chlorophyll energy transfer in thylakoid membrane preparations from Phaeodactylum tricornutum and Nannochloropsis sp. In: Baltscheffsky M. (Ed). Recent Progress of Photosynthesis Research vol. II (1990), Kluwer Academic Publishers, Dordrecht 289-292
    • (1990) Recent Progress of Photosynthesis Research , vol.II , pp. 289-292
    • Trautman, J.K.1    Shreve, A.P.2    Owens, T.G.3    Albrecht, A.C.4
  • 58
    • 0001439685 scopus 로고
    • Studies of excitation energy transfer within the green alga Chlamydomonas reinhardtii and its mutants at 77 K
    • Lin S., and Knox R.S. Studies of excitation energy transfer within the green alga Chlamydomonas reinhardtii and its mutants at 77 K. Photosynth. Res. 27 (1991) 157-168
    • (1991) Photosynth. Res. , vol.27 , pp. 157-168
    • Lin, S.1    Knox, R.S.2
  • 60
    • 0035983330 scopus 로고    scopus 로고
    • Unique fluorescence properties of a cyanobacterium Gloeobacter violaceus PCC 7421: reasons for absence of the long-wavelength PSI Chl a fluorescence at - 196 °C
    • Mimuro M., Ookubo T., Takahashi D., Sakawa T., Akimoto S., Yamazaki I., and Miyashita H. Unique fluorescence properties of a cyanobacterium Gloeobacter violaceus PCC 7421: reasons for absence of the long-wavelength PSI Chl a fluorescence at - 196 °C. Plant Cell Physiol. 43 (2002) 587-594
    • (2002) Plant Cell Physiol. , vol.43 , pp. 587-594
    • Mimuro, M.1    Ookubo, T.2    Takahashi, D.3    Sakawa, T.4    Akimoto, S.5    Yamazaki, I.6    Miyashita, H.7
  • 61
    • 40949094151 scopus 로고
    • Chlorophyll fluorescence transients as indications of changes in the redox state of plastoquinone in intact Bryopsis corticulans
    • Satoh K., and Fork D.C. Chlorophyll fluorescence transients as indications of changes in the redox state of plastoquinone in intact Bryopsis corticulans. Plant Sci. Lett. 29 (1983) 133-144
    • (1983) Plant Sci. Lett. , vol.29 , pp. 133-144
    • Satoh, K.1    Fork, D.C.2
  • 62
    • 2342552611 scopus 로고
    • Fluorescence of chlorophyll in brown algae and diatoms
    • Sugahara K., Murata N., and Takamiya A. Fluorescence of chlorophyll in brown algae and diatoms. Plant Cell Physiol. 12 (1971) 377-385
    • (1971) Plant Cell Physiol. , vol.12 , pp. 377-385
    • Sugahara, K.1    Murata, N.2    Takamiya, A.3
  • 63
    • 0028843428 scopus 로고
    • Gloeobacter violaceus - investigation of an unusual photosynthetic apparatus. Absence of the long wavelength emission of photosystem I in 77 K fluorescence spectra
    • Koenig F., and Schmidt M. Gloeobacter violaceus - investigation of an unusual photosynthetic apparatus. Absence of the long wavelength emission of photosystem I in 77 K fluorescence spectra. Physiol. Plant. 94 (1995) 621-628
    • (1995) Physiol. Plant. , vol.94 , pp. 621-628
    • Koenig, F.1    Schmidt, M.2
  • 64
    • 3042595709 scopus 로고    scopus 로고
    • De-epoxidation of violaxanthin in light-harvesting complex I proteins
    • Wehner A., Storf S., Jahns P., and Schmid V.H. De-epoxidation of violaxanthin in light-harvesting complex I proteins. J. Biol. Chem. 279 (2004) 26823-26829
    • (2004) J. Biol. Chem. , vol.279 , pp. 26823-26829
    • Wehner, A.1    Storf, S.2    Jahns, P.3    Schmid, V.H.4


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