메뉴 건너뛰기




Volumn 106, Issue 49, 2009, Pages 20764-20769

Identification of a single peridinin sensing Chl-a excitation in reconstituted PCP by crystallography and spectroscopy

Author keywords

Light harvesting; Peridinin; Protein crystallography; Refolding; Transient absorption spectroscopy

Indexed keywords

MUTANT PROTEIN;

EID: 73949151567     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0908938106     Document Type: Article
Times cited : (69)

References (45)
  • 1
    • 0004133553 scopus 로고    scopus 로고
    • Frank HA, Young AJ, Britton G, Cogdell RJ eds, Kluwer Academic Publishers, Dordrecht
    • Frank HA, Young AJ, Britton G, Cogdell RJ eds. (1999) The Photochemistry of Carotenoids. (Kluwer Academic Publishers, Dordrecht).
    • (1999) The Photochemistry of Carotenoids
  • 2
    • 73949138571 scopus 로고    scopus 로고
    • Green BR, Parson WW eds. (2003) Advances in Photosynthesis and Respiration 13: Light Harvesting Antennas. (Kluwer academic publishers, Dordrecht). 1st Ed.
    • Green BR, Parson WW eds. (2003) Advances in Photosynthesis and Respiration Vol. 13: Light Harvesting Antennas. (Kluwer academic publishers, Dordrecht). 1st Ed.
  • 3
    • 33845698300 scopus 로고    scopus 로고
    • The architecture and function of the light-harvesting apparatus of purple bacteria: From single molecules to in vivo membranes
    • Cogdell RJ, Gall A, Köhler J (2006) The architecture and function of the light-harvesting apparatus of purple bacteria: From single molecules to in vivo membranes. Q Rev Biophys 39:227-324.
    • (2006) Q Rev Biophys , vol.39 , pp. 227-324
    • Cogdell, R.J.1    Gall, A.2    Köhler, J.3
  • 4
    • 11744291937 scopus 로고    scopus 로고
    • Mechanism of energy transfer from carotenoids to bacteriochlorophyll: Light-harvesting by carotenoids having different extents of π-electron conjugation incorporated into the B850 antenna complex from the carotenoidless bacterium rhodobacter sphaeroides R-26.1
    • Desamero RZB, et al. (1998) Mechanism of energy transfer from carotenoids to bacteriochlorophyll: Light-harvesting by carotenoids having different extents of π-electron conjugation incorporated into the B850 antenna complex from the carotenoidless bacterium rhodobacter sphaeroides R-26.1. J Phys Chem B 102:8151-8162.
    • (1998) J Phys Chem B , vol.102 , pp. 8151-8162
    • Desamero, R.Z.B.1
  • 5
    • 0026514581 scopus 로고
    • Pigment-binding properties of mutant light-harvesting chlorophyll-a/b-binding protein
    • Paulsen H, Hobe S (1992) Pigment-binding properties of mutant light-harvesting chlorophyll-a/b-binding protein. Eur J Biochem 205:71-76.
    • (1992) Eur J Biochem , vol.205 , pp. 71-76
    • Paulsen, H.1    Hobe, S.2
  • 6
    • 0029637583 scopus 로고
    • Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria
    • McDermott G, et al. (1995) Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria. Nature 374:517-521.
    • (1995) Nature , vol.374 , pp. 517-521
    • McDermott, G.1
  • 7
    • 0037424652 scopus 로고    scopus 로고
    • The structure and thermal motion of the B800-850 LH2 complex from Rps.acidophila at 2.0A resolution and 100K: New structural features and functionally relevant motions
    • Papiz MZ, Prince SM, Howard T, Cogdell RJ, Isaacs NW (2003) The structure and thermal motion of the B800-850 LH2 complex from Rps.acidophila at 2.0A resolution and 100K: New structural features and functionally relevant motions. J Mol Biol 326:1523-1538.
    • (2003) J Mol Biol , vol.326 , pp. 1523-1538
    • Papiz, M.Z.1    Prince, S.M.2    Howard, T.3    Cogdell, R.J.4    Isaacs, N.W.5
  • 8
    • 0030585121 scopus 로고    scopus 로고
    • The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum
    • Koepke J, Hu X, Muenke C, Schulten K, Michel H (1996) The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum. Structure 4:581-597.
    • (1996) Structure , vol.4 , pp. 581-597
    • Koepke, J.1    Hu, X.2    Muenke, C.3    Schulten, K.4    Michel, H.5
  • 9
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach major light-harvesting complex at 2.72 A resolution
    • Liu Z, et al. (2004) Crystal structure of spinach major light-harvesting complex at 2.72 A resolution. Nature 428:287-292.
    • (2004) Nature , vol.428 , pp. 287-292
    • Liu, Z.1
  • 10
    • 16344363252 scopus 로고    scopus 로고
    • Mechanisms of photoprotection and nonphotochemical quenching in pea lightharvesting complex at 2.5 A resolution
    • Standfuss J, Terwisscha van Scheltinga AC, Lamborghini M, Kühlbrandt W (2005) Mechanisms of photoprotection and nonphotochemical quenching in pea lightharvesting complex at 2.5 A resolution. EMBO J 24:919-928.
    • (2005) EMBO J , vol.24 , pp. 919-928
    • Standfuss, J.1    Terwisscha van Scheltinga, A.C.2    Lamborghini, M.3    Kühlbrandt, W.4
  • 11
    • 0028049588 scopus 로고
    • Trimerization and crystallization of reconstituted light-harvesting chlorophyll a/b complex
    • Hobe S, Prytulla S, Kühlbrandt W, Paulsen H (1994) Trimerization and crystallization of reconstituted light-harvesting chlorophyll a/b complex. EMBO J 13:3423-3429.
    • (1994) EMBO J , vol.13 , pp. 3423-3429
    • Hobe, S.1    Prytulla, S.2    Kühlbrandt, W.3    Paulsen, H.4
  • 12
    • 0030055628 scopus 로고    scopus 로고
    • Structural basis of light harvesting by carotenoids: Peridininchlorophyll-protein from Amphidinium carterae
    • Hofmann E, et al. (1996) Structural basis of light harvesting by carotenoids: Peridininchlorophyll-protein from Amphidinium carterae. Science 272:1788-1791.
    • (1996) Science , vol.272 , pp. 1788-1791
    • Hofmann, E.1
  • 13
    • 0000051201 scopus 로고    scopus 로고
    • Effect of the solvent environment on the spectroscopic properties and dynamics of the lowest excited states of carotenoids
    • Frank HA, et al. (2000) Effect of the solvent environment on the spectroscopic properties and dynamics of the lowest excited states of carotenoids. J Phys Chem B 104:4569-4577.
    • (2000) J Phys Chem B , vol.104 , pp. 4569-4577
    • Frank, H.A.1
  • 14
    • 0001001551 scopus 로고    scopus 로고
    • Singlet and triplet energy transfer in the peridinin-chlorophyll a-protein from Amphidinium carterae
    • Bautista JA, et al. (1999) Singlet and triplet energy transfer in the peridinin-chlorophyll a-protein from Amphidinium carterae. J Phys Chem A 103:2267-2273.
    • (1999) J Phys Chem A , vol.103 , pp. 2267-2273
    • Bautista, J.A.1
  • 15
    • 0037168673 scopus 로고    scopus 로고
    • Carotenoid to chlorophyll energy transfer in the peridinin-chlorophyll-a-protein complex involves an intramolecular charge transfer state
    • Zigmantas D, Hiller RG, Sundstrom V, Polivka T (2002) Carotenoid to chlorophyll energy transfer in the peridinin-chlorophyll-a-protein complex involves an intramolecular charge transfer state. Proc Natl Acad Sci USA 99:16760-16765.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16760-16765
    • Zigmantas, D.1    Hiller, R.G.2    Sundstrom, V.3    Polivka, T.4
  • 16
    • 0035006465 scopus 로고    scopus 로고
    • Energy transfer in the peridinin chlorophyll-a protein of Amphidinium carterae studied by polarized transient absorption and target analysis
    • Krueger BP, et al. (2001) Energy transfer in the peridinin chlorophyll-a protein of Amphidinium carterae studied by polarized transient absorption and target analysis. Biophys J 80:2843-2855.
    • (2001) Biophys J , vol.80 , pp. 2843-2855
    • Krueger, B.P.1
  • 17
    • 3042737690 scopus 로고    scopus 로고
    • Effect of a conjugated carbonyl group on the photophysical properties of carotenoids
    • Zigmantas D, et al. (2004) Effect of a conjugated carbonyl group on the photophysical properties of carotenoids. Phys Chem Chem Phys 6:3009-3016.
    • (2004) Phys Chem Chem Phys , vol.6 , pp. 3009-3016
    • Zigmantas, D.1
  • 18
    • 0034595303 scopus 로고    scopus 로고
    • Peridinin chlorophyll a protein: Relating structure and steady-state spectroscopy
    • Kleima FJ, et al. (2000) Peridinin chlorophyll a protein: Relating structure and steady-state spectroscopy. Biochemistry 39:5184-5195.
    • (2000) Biochemistry , vol.39 , pp. 5184-5195
    • Kleima, F.J.1
  • 19
    • 0001114094 scopus 로고    scopus 로고
    • Structure-based calculations of the optical spectra of the light-harvesting peridinin-chlorophyll-protein complexes from Amphidinium carterae and Heterocapsa pygmaea
    • Carbonera D, Giacometti G, Segre U, Hofmann E, Hiller RG (1999) Structure-based calculations of the optical spectra of the light-harvesting peridinin-chlorophyll-protein complexes from Amphidinium carterae and Heterocapsa pygmaea. J Phys Chem B 103:6349-6356.
    • (1999) J Phys Chem B , vol.103 , pp. 6349-6356
    • Carbonera, D.1    Giacometti, G.2    Segre, U.3    Hofmann, E.4    Hiller, R.G.5
  • 20
    • 1042299984 scopus 로고    scopus 로고
    • Spectroscopic properties of the main-form and high-salt peridinin-chlorophyll a proteins from Amphidinium carterae
    • Ilagan RP, et al. (2004) Spectroscopic properties of the main-form and high-salt peridinin-chlorophyll a proteins from Amphidinium carterae. Biochemistry 43:1478-1487.
    • (2004) Biochemistry , vol.43 , pp. 1478-1487
    • Ilagan, R.P.1
  • 21
    • 0033799023 scopus 로고    scopus 로고
    • Excitation transfer in the peridinin-chlorophyllprotein of Amphidinium carterae
    • SchultenK
    • Damjanović A, Ritz T, SchultenK(2000) Excitation transfer in the peridinin-chlorophyllprotein of Amphidinium carterae. Biophys J 79:1695-1705.
    • (2000) Biophys J , vol.79 , pp. 1695-1705
    • Damjanović, A.1    Ritz, T.2
  • 22
    • 66349088474 scopus 로고    scopus 로고
    • X-ray structure of the high-salt form of the peridinin-chlorophyll a-protein from the dinoflagellate Amphidinium carterae: Modulation of the spectral properties of pigments by the protein environment
    • Schulte T, Sharples FP, Hiller RG, Hofmann E (2009) X-ray structure of the high-salt form of the peridinin-chlorophyll a-protein from the dinoflagellate Amphidinium carterae: Modulation of the spectral properties of pigments by the protein environment. Biochemistry 48:4466-4475.
    • (2009) Biochemistry , vol.48 , pp. 4466-4475
    • Schulte, T.1    Sharples, F.P.2    Hiller, R.G.3    Hofmann, E.4
  • 23
    • 33751568892 scopus 로고    scopus 로고
    • Femtosecond time-resolved absorption spectroscopy of mainform and high-salt peridinin-chlorophyll a-proteins at low temperatures
    • Ilagan RP, et al. (2006) Femtosecond time-resolved absorption spectroscopy of mainform and high-salt peridinin-chlorophyll a-proteins at low temperatures. Biochemistry 45:14052-14063.
    • (2006) Biochemistry , vol.45 , pp. 14052-14063
    • Ilagan, R.P.1
  • 24
    • 25444446803 scopus 로고    scopus 로고
    • Tuning energy transfer in the peridinin-chlorophyll complex by reconstitution with different chlorophylls
    • Polívka T, Pascher T, Sundström V, Hiller RG (2005) Tuning energy transfer in the peridinin-chlorophyll complex by reconstitution with different chlorophylls. Photosynth Res 86:217-227.
    • (2005) Photosynth Res , vol.86 , pp. 217-227
    • Polívka, T.1    Pascher, T.2    Sundström, V.3    Hiller, R.G.4
  • 25
    • 59649114302 scopus 로고    scopus 로고
    • Inter-pigment interactions in the peridinin chlorophyll protein studied by global and target analysis of time resolved absorption spectra
    • Stokkum IHV, et al. (2009) Inter-pigment interactions in the peridinin chlorophyll protein studied by global and target analysis of time resolved absorption spectra. Chem Phys 357:70-78.
    • (2009) Chem Phys , vol.357 , pp. 70-78
    • Stokkum, I.H.V.1
  • 26
    • 34548749295 scopus 로고    scopus 로고
    • Triplet state dynamics in peridinin-chlorophyll-a-protein: A new pathway of photoprotection in LHCs?
    • Alexandre MTA, et al. (2007) Triplet state dynamics in peridinin-chlorophyll-a-protein: A new pathway of photoprotection in LHCs? Biophys J 93:2118-2128.
    • (2007) Biophys J , vol.93 , pp. 2118-2128
    • Alexandre, M.T.A.1
  • 27
    • 38549111025 scopus 로고    scopus 로고
    • Identification by time-resolved EPR of the peridinins directly involved in chlorophyll triplet quenching in the peridinin-chlorophyll a-protein from Amphidinium carterae
    • Di Valentin M, Ceola S, Salvadori E, Agostini G, Carbonera D (2008) Identification by time-resolved EPR of the peridinins directly involved in chlorophyll triplet quenching in the peridinin-chlorophyll a-protein from Amphidinium carterae. Biochim Biophys Acta 1777:186-195.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 186-195
    • Di Valentin, M.1    Ceola, S.2    Salvadori, E.3    Agostini, G.4    Carbonera, D.5
  • 28
    • 37849032090 scopus 로고    scopus 로고
    • Spin-density distribution of the carotenoid triplet state in the peridinin-chlorophyll-protein antenna. A Q-band pulse electron-nuclear double resonance and density functional theory study
    • Niklas J, et al. (2007) Spin-density distribution of the carotenoid triplet state in the peridinin-chlorophyll-protein antenna. A Q-band pulse electron-nuclear double resonance and density functional theory study. J Am Chem Soc 129:15442-15443.
    • (2007) J Am Chem Soc , vol.129 , pp. 15442-15443
    • Niklas, J.1
  • 29
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60:2256-2268.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 31
    • 33846284164 scopus 로고    scopus 로고
    • Optical spectroscopic studies of light-harvesting by pigment-reconstituted peridinin-chlorophyll-proteins at cryogenic temperatures
    • Ilagan RP, et al. (2006) Optical spectroscopic studies of light-harvesting by pigment-reconstituted peridinin-chlorophyll-proteins at cryogenic temperatures. Photosynth Res 90:5-15.
    • (2006) Photosynth Res , vol.90 , pp. 5-15
    • Ilagan, R.P.1
  • 32
    • 3442883070 scopus 로고    scopus 로고
    • Ultrafast carotenoid band shifts: Experiment and theory
    • Herek JL et al. (2004) Ultrafast carotenoid band shifts: Experiment and theory. J Phys Chem B 108:10398-10403.
    • (2004) J Phys Chem B , vol.108 , pp. 10398-10403
    • Herek, J.L.1
  • 33
    • 0042558799 scopus 로고    scopus 로고
    • Selective interaction between xanthophylls and chlorophylls in LHCII probed by femtosecond transient absorption spectroscopy
    • Gradinaru CC, van Grondelle R, van Amerongen H (2003) Selective interaction between xanthophylls and chlorophylls in LHCII probed by femtosecond transient absorption spectroscopy. J Phys Chem B 107:3938-3943.
    • (2003) J Phys Chem B , vol.107 , pp. 3938-3943
    • Gradinaru, C.C.1    van Grondelle, R.2    van Amerongen, H.3
  • 34
    • 0001269334 scopus 로고
    • ed Lim EC Academic, New York, p
    • Liptay W (1974) in Excited States., ed Lim EC (Academic, New York), p 129.
    • (1974) Excited States , pp. 129
    • Liptay, W.1
  • 36
    • 0033621630 scopus 로고    scopus 로고
    • Förster excitation energy transfer in peridinin-chlorophyll-a-protein
    • Kleima FJ, et al. (2000) Förster excitation energy transfer in peridinin-chlorophyll-a-protein. Biophys J 78:344-353.
    • (2000) Biophys J , vol.78 , pp. 344-353
    • Kleima, F.J.1
  • 37
    • 0004178331 scopus 로고
    • eds Isler O, Gutman H, Solms U Birkhauser Verlag, Basel
    • Krinsky N (1971) Carotenoids. eds Isler O, Gutman H, Solms U (Birkhauser Verlag, Basel).
    • (1971) Carotenoids
    • Krinsky, N.1
  • 38
    • 25444500136 scopus 로고    scopus 로고
    • Reconstitution of the peridinin-chlorophyll a protein (PCP): Evidence for functional flexibility in chlorophyll binding
    • Miller DJ, et al. (2005) Reconstitution of the peridinin-chlorophyll a protein (PCP): Evidence for functional flexibility in chlorophyll binding. Photosynth Res 86:229-240.
    • (2005) Photosynth Res , vol.86 , pp. 229-240
    • Miller, D.J.1
  • 39
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr 26:795-800.
    • (1993) J Appl Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 40
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy AJ (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr D Biol Crystallogr 63:32-41.
    • (2007) Acta Crystallogr D Biol Crystallogr , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 41
    • 0028103275 scopus 로고    scopus 로고
    • The CCP4 suite: Programs for protein crystallography (1994) Acta Crystallogr D Biol Crystallogr 50:760-763.
    • The CCP4 suite: Programs for protein crystallography (1994) Acta Crystallogr D Biol Crystallogr 50:760-763.
  • 42
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger AT, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 54:905-921.
    • (1998) Acta Crystallogr D Biol Crystallogr , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 44
  • 45
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin A, Teplyakov A (1997) MOLREP: An automated program for molecular replacement. J Appl Crystallogr 30:1022-1025.
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.