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Volumn 1787, Issue 12, 2009, Pages 1499-1504

Filling the "green gap" of the major light-harvesting chlorophyll a/b complex by covalent attachment of Rhodamine Red

Author keywords

FRET (F rster resonance energy transfer); LHCII; Maleimide dye; Photosynthesis; Site specific labeling; Solar spectrum

Indexed keywords

APOPROTEIN; CHLOROPHYLL A; CHLOROPHYLL B; CYSTEINE; DYE; PIGMENT; RHODAMINE RED; UNCLASSIFIED DRUG;

EID: 69249205578     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2009.07.003     Document Type: Article
Times cited : (38)

References (45)
  • 1
    • 33645782025 scopus 로고    scopus 로고
    • Approaches for biological and biomimetic energy conversion
    • LaVan D.A., and Cha J.N. Approaches for biological and biomimetic energy conversion. Proc. Nat. Acad. Sci. U.S.A. 103 (2006) 5251-5255
    • (2006) Proc. Nat. Acad. Sci. U.S.A. , vol.103 , pp. 5251-5255
    • LaVan, D.A.1    Cha, J.N.2
  • 2
    • 0000484406 scopus 로고
    • Bioelectronics and biometallocatalysis for production of fuels and chemicals by photosynthetic water splitting
    • Lee J., and Greenbaum E. Bioelectronics and biometallocatalysis for production of fuels and chemicals by photosynthetic water splitting. Appl. Biochem. Biotechnol. 51-2 (1995) 295-305
    • (1995) Appl. Biochem. Biotechnol. , vol.51-2 , pp. 295-305
    • Lee, J.1    Greenbaum, E.2
  • 6
    • 42149143542 scopus 로고    scopus 로고
    • Overcoming kinetic limitations of electron injection in the dye solar cell via coadsorption and FRET
    • Siegers C., Würfel U., Zistler M., Gores H., Hohl-Ebinger J., Hinsch A., and Haag R. Overcoming kinetic limitations of electron injection in the dye solar cell via coadsorption and FRET. Chem. Phys. Chem. 9 (2008) 793-798
    • (2008) Chem. Phys. Chem. , vol.9 , pp. 793-798
    • Siegers, C.1    Würfel, U.2    Zistler, M.3    Gores, H.4    Hohl-Ebinger, J.5    Hinsch, A.6    Haag, R.7
  • 7
    • 24344466865 scopus 로고    scopus 로고
    • Tailoring porphyrins and chlorins for self-assembly in biomimetic artificial antenna systems
    • Balaban T.S. Tailoring porphyrins and chlorins for self-assembly in biomimetic artificial antenna systems. Acc. Chem. Res. 38 (2008) 612-623
    • (2008) Acc. Chem. Res. , vol.38 , pp. 612-623
    • Balaban, T.S.1
  • 10
    • 0037119724 scopus 로고    scopus 로고
    • Biomimetic model of a plant photosystem consisting of a recombinant light-harvesting complex and a terrylene dye
    • Wolf-Klein H., Kohl C., Müllen K., and Paulsen H. Biomimetic model of a plant photosystem consisting of a recombinant light-harvesting complex and a terrylene dye. Angew. Chem. Int. Ed. 41 (2002) 3380-3382
    • (2002) Angew. Chem. Int. Ed. , vol.41 , pp. 3380-3382
    • Wolf-Klein, H.1    Kohl, C.2    Müllen, K.3    Paulsen, H.4
  • 11
    • 51449119719 scopus 로고    scopus 로고
    • Immobilization of light-harvesting chlorophyll a/b complex (LHCIIb) studied by surface plasmon field-enhanced fluorescence spectroscopy
    • Liu J., Lauterbach R., Paulsen H., and Knoll W. Immobilization of light-harvesting chlorophyll a/b complex (LHCIIb) studied by surface plasmon field-enhanced fluorescence spectroscopy. Langmuir 24 (2008) 9661-9667
    • (2008) Langmuir , vol.24 , pp. 9661-9667
    • Liu, J.1    Lauterbach, R.2    Paulsen, H.3    Knoll, W.4
  • 12
    • 16344363252 scopus 로고    scopus 로고
    • Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 Å resolution
    • Standfuss R., van Scheltinga A.C.T., Lamborghini M., and Kühlbrandt W. 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, R.1    van Scheltinga, A.C.T.2    Lamborghini, M.3    Kühlbrandt, W.4
  • 13
    • 0000692897 scopus 로고
    • Concentration quenching in chlorophyll
    • Beddard G.S., and Porter G. Concentration quenching in chlorophyll. Nature 260 (1976) 366-376
    • (1976) Nature , vol.260 , pp. 366-376
    • Beddard, G.S.1    Porter, G.2
  • 14
    • 0141642102 scopus 로고    scopus 로고
    • Characterization of Chlorobium tepidum chlorosomes: a calculation of bacteriochlorophyll c per chlorosome and oligomer modeling
    • Montano G.A., Bowen B.P., LaBelle J.T., Woodbury N.W., Pizziconi V.B., and Blankenship R.E. Characterization of Chlorobium tepidum chlorosomes: a calculation of bacteriochlorophyll c per chlorosome and oligomer modeling. Biophys. J. 85 (2003) 2560-2565
    • (2003) Biophys. J. , vol.85 , pp. 2560-2565
    • Montano, G.A.1    Bowen, B.P.2    LaBelle, J.T.3    Woodbury, N.W.4    Pizziconi, V.B.5    Blankenship, R.E.6
  • 15
    • 0028972073 scopus 로고
    • CP-MAS C-13-NMR dipolar correlation spectroscopy of C-13-enriched chlorosomes and isolated bacteriochlorophyll c aggregates of Chlorobium tepidum: the self-organization of pigments is the main structural feature of chlorosomes
    • Balaban T., Holzwarth A., Schaffner K., Boender G., and Degroot H. CP-MAS C-13-NMR dipolar correlation spectroscopy of C-13-enriched chlorosomes and isolated bacteriochlorophyll c aggregates of Chlorobium tepidum: the self-organization of pigments is the main structural feature of chlorosomes. Biochemistry 34 (1995) 15259-15266
    • (1995) Biochemistry , vol.34 , pp. 15259-15266
    • Balaban, T.1    Holzwarth, A.2    Schaffner, K.3    Boender, G.4    Degroot, H.5
  • 16
    • 0000717687 scopus 로고    scopus 로고
    • Insertion of light-harvesting chlorophyll a/b protein into the thylakoid - topographical studies
    • Kosemund K., Geiger I., and Paulsen H. Insertion of light-harvesting chlorophyll a/b protein into the thylakoid - topographical studies. Eur. J. Biochem. 267 (2000) 1138-1145
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1138-1145
    • Kosemund, K.1    Geiger, I.2    Paulsen, H.3
  • 18
    • 59649083740 scopus 로고    scopus 로고
    • Crystal structure of plant light-harvesting complex shows the active, energy-transmitting state
    • Barros T., Royant A., Standfuss J., Dreuw A., and Kühlbrandt W. Crystal structure of plant light-harvesting complex shows the active, energy-transmitting state. EMBO J. 28 (2008) 298-306
    • (2008) EMBO J. , vol.28 , pp. 298-306
    • Barros, T.1    Royant, A.2    Standfuss, J.3    Dreuw, A.4    Kühlbrandt, W.5
  • 19
    • 69249214371 scopus 로고
    • Rhodamine lipid derivatives increase the light-harvesting ability of isolated chloroplasts
    • Razinkov V., Sorokin E., Bobylev G., and Molotkovsky J. Rhodamine lipid derivatives increase the light-harvesting ability of isolated chloroplasts. Biol. Membrany 11 (1994) 660-663
    • (1994) Biol. Membrany , vol.11 , pp. 660-663
    • Razinkov, V.1    Sorokin, E.2    Bobylev, G.3    Molotkovsky, J.4
  • 20
    • 33646720105 scopus 로고    scopus 로고
    • Efficient energy transfer from peripheral chromophores to the self-assembled zinc chlorin rod antenna: a bioinspired light-harvesting system to bridge the "green gap"
    • Röger C., Müller M.G., Lysetska M., Holzwarth A.R., and Würthner F. Efficient energy transfer from peripheral chromophores to the self-assembled zinc chlorin rod antenna: a bioinspired light-harvesting system to bridge the "green gap". J. Am. Chem. Soc. 128 (2006) 6542-6543
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 6542-6543
    • Röger, C.1    Müller, M.G.2    Lysetska, M.3    Holzwarth, A.R.4    Würthner, F.5
  • 21
    • 0001682178 scopus 로고
    • Structure and expression of a pea nuclear gene encoding a light-harvesting chlorophyll a/b-binding polypeptide
    • Cashmore A.R. Structure and expression of a pea nuclear gene encoding a light-harvesting chlorophyll a/b-binding polypeptide. Proc. Natl. Acad. Sci. U.S.A. 81 (1984) 2960-2964
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 2960-2964
    • Cashmore, A.R.1
  • 22
    • 21444441143 scopus 로고    scopus 로고
    • Localization of the N-terminal domain in light-harvesting chlorophyll a/b protein (LHCIIb) by electron paramagnetic resonance (EPR) measurements
    • Jeschke G., Bender A., Schweikardt T., Panek G., Decker H., and Paulsen H. Localization of the N-terminal domain in light-harvesting chlorophyll a/b protein (LHCIIb) by electron paramagnetic resonance (EPR) measurements. J. Biol. Chem. 280 (2005) 18623-18630
    • (2005) J. Biol. Chem. , vol.280 , pp. 18623-18630
    • Jeschke, G.1    Bender, A.2    Schweikardt, T.3    Panek, G.4    Decker, H.5    Paulsen, H.6
  • 23
    • 0001456147 scopus 로고
    • Reconstitution of pigment-containing complexes from light-harvesting chlorophyll a/b-binding protein overexpressed in E. coli
    • Paulsen H., Rümler U., and Rüdiger W. Reconstitution of pigment-containing complexes from light-harvesting chlorophyll a/b-binding protein overexpressed in E. coli. Planta 181 (1990) 204-211
    • (1990) Planta , vol.181 , pp. 204-211
    • Paulsen, H.1    Rümler, U.2    Rüdiger, W.3
  • 24
    • 0030000359 scopus 로고    scopus 로고
    • Assembly of light-harvesting chlorophyll a/b complex in vitro. Time-resolved fluorescence measurements
    • Booth P., and Paulsen H. Assembly of light-harvesting chlorophyll a/b complex in vitro. Time-resolved fluorescence measurements. Biochemistry 35 (1996) 5103-5108
    • (1996) Biochemistry , vol.35 , pp. 5103-5108
    • Booth, P.1    Paulsen, H.2
  • 25
    • 0027301940 scopus 로고
    • Pigments induce folding of light-harvesting chlorophyll a/b-binding protein
    • Paulsen H., Finkenzeller B., and Kühlein N. Pigments induce folding of light-harvesting chlorophyll a/b-binding protein. Eur. J. Biochem. 215 (1993) 809-816
    • (1993) Eur. J. Biochem. , vol.215 , pp. 809-816
    • Paulsen, H.1    Finkenzeller, B.2    Kühlein, N.3
  • 26
    • 0037461321 scopus 로고    scopus 로고
    • The light-harvesting chlorophyll a/b complex can be reconstituted in vitro from its completely unfolded apoprotein
    • Yang C., Horn R., and Paulsen H. The light-harvesting chlorophyll a/b complex can be reconstituted in vitro from its completely unfolded apoprotein. Biochemistry 42 (2003) 4527-4533
    • (2003) Biochemistry , vol.42 , pp. 4527-4533
    • Yang, C.1    Horn, R.2    Paulsen, H.3
  • 27
    • 0028049588 scopus 로고
    • Trimerization and crystallization of reconstituted light-harvesting chlorophyll a/b complex
    • Hobe S., Prytulla S., Kühlbrandt W., and Paulsen H. Trimerization and crystallization of reconstituted light-harvesting chlorophyll a/b complex. EMBO J. 13 (1994) 3423-3429
    • (1994) EMBO J. , vol.13 , pp. 3423-3429
    • Hobe, S.1    Prytulla, S.2    Kühlbrandt, W.3    Paulsen, H.4
  • 28
    • 0001473449 scopus 로고
    • Determination of the aggregate size in detergent solution of the light-harvesting chlorophyll a/b-protein complex from chloroplast membranes
    • Butler P.J.G., and Kühlbrandt W. Determination of the aggregate size in detergent solution of the light-harvesting chlorophyll a/b-protein complex from chloroplast membranes. Proc. Natl. Acad. Sci. U.S.A. 85 (1988) 3797-3801
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 3797-3801
    • Butler, P.J.G.1    Kühlbrandt, W.2
  • 29
    • 0029067862 scopus 로고
    • One-step extraction and concentration of pigments and acyl lipids by sec-butanol from in vitro and in vivo samples
    • Martinson T., and Plumley F. One-step extraction and concentration of pigments and acyl lipids by sec-butanol from in vitro and in vivo samples. Anal. Biochem. 228 (1995) 123-130
    • (1995) Anal. Biochem. , vol.228 , pp. 123-130
    • Martinson, T.1    Plumley, F.2
  • 31
    • 33947094704 scopus 로고
    • Absolute quantum yield determination by thermal blooming - fluorescein
    • Brannon J.H., and Magde D. Absolute quantum yield determination by thermal blooming - fluorescein. J. Biol. Chem. 82 (1978) 705-709
    • (1978) J. Biol. Chem. , vol.82 , pp. 705-709
    • Brannon, J.H.1    Magde, D.2
  • 33
    • 84989723688 scopus 로고
    • Förster transfer calculations based on crystal structure data from Agmenellum quadruplicatum C-phycocyanin
    • Sauer K., Scheer H., and Sauer P. Förster transfer calculations based on crystal structure data from Agmenellum quadruplicatum C-phycocyanin. Photochem. Photobiol. 46 (1987) 427-440
    • (1987) Photochem. Photobiol. , vol.46 , pp. 427-440
    • Sauer, K.1    Scheer, H.2    Sauer, P.3
  • 34
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb Viewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M. SWISS-MODEL and the Swiss-Pdb Viewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.2
  • 35
    • 59649124429 scopus 로고    scopus 로고
    • Ultrafast resonance energy transfer from a site-specifically attached fluorescent chromophore reveals the folding of the N-terminal domain of CP29
    • van Oort B., Murali S., Wientjes E., Koehorst R.B., Spruijt R.B., van Hoek A., Croce R., and van Amerongen H. Ultrafast resonance energy transfer from a site-specifically attached fluorescent chromophore reveals the folding of the N-terminal domain of CP29. Chem. Phys. 357 (2009) 113-119
    • (2009) Chem. Phys. , vol.357 , pp. 113-119
    • van Oort, B.1    Murali, S.2    Wientjes, E.3    Koehorst, R.B.4    Spruijt, R.B.5    van Hoek, A.6    Croce, R.7    van Amerongen, H.8
  • 36
    • 34247472611 scopus 로고    scopus 로고
    • Understanding the changes in the circular dichroism of light harvesting complex II upon varying its pigment composition and organization
    • Georgakopoulou S., van der Zwan G., Bassi R., van Grondelle R., van Amerongen H., and Croce R. Understanding the changes in the circular dichroism of light harvesting complex II upon varying its pigment composition and organization. Biochemistry 46 (2007) 4745-4754
    • (2007) Biochemistry , vol.46 , pp. 4745-4754
    • Georgakopoulou, S.1    van der Zwan, G.2    Bassi, R.3    van Grondelle, R.4    van Amerongen, H.5    Croce, R.6
  • 37
    • 0001305233 scopus 로고    scopus 로고
    • Carotenoid binding sites in LHCIIb - relative affinities towards major xanthophylls of higher plants
    • Hobe S., Niemeier H., Bender A., and Paulsen H. Carotenoid binding sites in LHCIIb - relative affinities towards major xanthophylls of higher plants. Eur. J. Biochem. 267 (2000) 616-624
    • (2000) Eur. J. Biochem. , vol.267 , pp. 616-624
    • Hobe, S.1    Niemeier, H.2    Bender, A.3    Paulsen, H.4
  • 38
    • 4344625034 scopus 로고    scopus 로고
    • The three isoforms of the light-harvesting complex II - spectroscopic features, trimer formation, and functional roles
    • Standfuss J., and Kühlbrandt W. The three isoforms of the light-harvesting complex II - spectroscopic features, trimer formation, and functional roles. J. Biol. Chem. 279 (2004) 36884-36891
    • (2004) J. Biol. Chem. , vol.279 , pp. 36884-36891
    • Standfuss, J.1    Kühlbrandt, W.2
  • 39
    • 33751541727 scopus 로고    scopus 로고
    • Thermal stability of trimeric light-harvesting chlorophyll a/b complex (LHCIIb) in liposomes of thylakoid lipids
    • Yang C.H., Boggasch S., Haase W., and Paulsen H. Thermal stability of trimeric light-harvesting chlorophyll a/b complex (LHCIIb) in liposomes of thylakoid lipids. Biochim. Biophys. Acta 1757 (2006) 1642-1648
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1642-1648
    • Yang, C.H.1    Boggasch, S.2    Haase, W.3    Paulsen, H.4
  • 40
    • 15244360930 scopus 로고    scopus 로고
    • Fluorescence energy transfer methods in bioanalysis
    • Miller J.N. Fluorescence energy transfer methods in bioanalysis. Analyst 130 (2005) 265-270
    • (2005) Analyst , vol.130 , pp. 265-270
    • Miller, J.N.1
  • 41
    • 33748755459 scopus 로고    scopus 로고
    • Assembly of the major light-harvesting chlorophyll-a/b complex - thermodynamics and kinetics of neoxanthin binding
    • Hobe S., Trostmann I., Raunser S., and Paulsen H. Assembly of the major light-harvesting chlorophyll-a/b complex - thermodynamics and kinetics of neoxanthin binding. J. Biol. Chem. 281 (2006) 25156-25166
    • (2006) J. Biol. Chem. , vol.281 , pp. 25156-25166
    • Hobe, S.1    Trostmann, I.2    Raunser, S.3    Paulsen, H.4
  • 42
    • 38049101008 scopus 로고    scopus 로고
    • Structural and functional analysis of the antiparallel strands in the lumenal loop of the major light-harvesting chlorophyll a/b complex of photosystem II (LHCIIb) by site-directed mutagenesis
    • Liu C., Zhang Y., Cao D., He Y., Kuang T., and Yang C. Structural and functional analysis of the antiparallel strands in the lumenal loop of the major light-harvesting chlorophyll a/b complex of photosystem II (LHCIIb) by site-directed mutagenesis. J. Biol. Chem. 283 (2008) 487-495
    • (2008) J. Biol. Chem. , vol.283 , pp. 487-495
    • Liu, C.1    Zhang, Y.2    Cao, D.3    He, Y.4    Kuang, T.5    Yang, C.6
  • 43
    • 0033569933 scopus 로고    scopus 로고
    • Carotenoid-binding sites of the major light-harvesting complex II of higher plants
    • Croce R., Weiss S., and Bassi R. Carotenoid-binding sites of the major light-harvesting complex II of higher plants. J. Biol. Chem. 274 (1999) 29613-29623
    • (1999) J. Biol. Chem. , vol.274 , pp. 29613-29623
    • Croce, R.1    Weiss, S.2    Bassi, R.3
  • 44
    • 54849433772 scopus 로고    scopus 로고
    • The negatively charged amino acids in the lumenal loop influence the pigment binding and conformation of the major light-harvesting chlorophyll a/b complex of photosystem II
    • Yang C., Lambrev P., Chen Z., Javorfi T., Kiss A.Z., Paulsen H., and Garab G. The negatively charged amino acids in the lumenal loop influence the pigment binding and conformation of the major light-harvesting chlorophyll a/b complex of photosystem II. Biochim. Biophys. Acta 1777 (2008) 1463-1470
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1463-1470
    • Yang, C.1    Lambrev, P.2    Chen, Z.3    Javorfi, T.4    Kiss, A.Z.5    Paulsen, H.6    Garab, G.7
  • 45
    • 0029852006 scopus 로고    scopus 로고
    • The C-terminal domain of light-harvesting chlorophyll-a/b-binding protein is involved in the stabilisation of trimeric light-harvesting complex
    • Kuttkat A., Hartmann A., Hobe S., and Paulsen H. The C-terminal domain of light-harvesting chlorophyll-a/b-binding protein is involved in the stabilisation of trimeric light-harvesting complex. Eur. J. Biochem. 242 (1996) 288-292
    • (1996) Eur. J. Biochem. , vol.242 , pp. 288-292
    • Kuttkat, A.1    Hartmann, A.2    Hobe, S.3    Paulsen, H.4


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