메뉴 건너뛰기




Volumn 48, Issue 21, 2009, Pages 4466-4475

X-ray structure of the high-salt form of the peridinin-chlorophyll α-protein from the dinoflagellate Amphidinium carterae: Modulation of the spectral properties of pigments by the protein environment

Author keywords

[No Author keywords available]

Indexed keywords

BLUE-SHIFTED; CHLOROPHYLL A; DIFFERENT STRUCTURE; ELECTROSTATIC EFFECT; GEOMETRY DISTORTION; IDEAL MODEL; LIGHT-HARVESTING COMPLEX; LIPID MOLECULES; MACROCYCLE; PERIDININ; PIGMENT COMPOSITION; PROTEIN INTERACTION; SEQUENCE VARIATIONS; SMALL VARIATIONS; SPECTRAL PROPERTIES; STRUCTURAL COMPARISON; STRUCTURAL SIMILARITY; TUNING MECHANISM; X-RAY STRUCTURE;

EID: 66349088474     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802320q     Document Type: Article
Times cited : (31)

References (65)
  • 1
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine, A. A., Richelle, J., and Wodak, S. J. (1999) SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr. D55, 191-205. (Pubitemid 29053816)
    • (1999) Acta Crystallographica Section D: Biological Crystallography , vol.55 , Issue.1 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 2
    • 84862812686 scopus 로고    scopus 로고
    • Antenna complexes and energy transfer processes
    • Blankenship, R. E., Ed. 2nd ed., Blackwell Science, Oxford, U.K.
    • Blankenship, R. E. (2002) Antenna complexes and energy transfer processes. In Molecular mechanisms of photosynthesis (Blankenship, R. E., Ed.) 2nd ed., pp 61-94. Blackwell Science, Oxford, U.K.
    • (2002) Molecular Mechanisms of Photosynthesis , pp. 61-94
    • Blankenship, R.E.1
  • 3
    • 17844409505 scopus 로고    scopus 로고
    • Light-harvesting systems in chlorophyll c-containing algae
    • Green, B. R., and Parson, W. W., Eds. 1st ed., Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Macpherson, A. N., and Hiller, R. G. (2003) Light-harvesting systems in chlorophyll c-containing algae. In Advances in photosynthesis and respiration. Volume 13: Light harvesting antennas (Green, B. R., and Parson, W. W., Eds.) 1st ed., pp 323-352, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (2003) Advances in Photosynthesis and Respiration. Volume 13: Light Harvesting Antennas , pp. 323-352
    • Macpherson, A.N.1    Hiller, R.G.2
  • 4
    • 17844371876 scopus 로고    scopus 로고
    • Antenna systems and energy transfer in cyanophyta and rhodophyta
    • Green, B. R., and Parson, W. W., Eds. 1st ed., Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Mimuro, M., and Kikuchi, H. (2003) Antenna systems and energy transfer in cyanophyta and rhodophyta. In Advances in photosynthesis and respiration. Volume 13: Light harvesting antennas (Green, B. R., and Parson, W. W., Eds.) 1st ed., pp 282-306, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (2003) Advances in Photosynthesis and Respiration. Volume 13: Light Harvesting Antennas , pp. 282-306
    • Mimuro, M.1    Kikuchi, H.2
  • 5
    • 2342539764 scopus 로고    scopus 로고
    • Ultrafast dynamics of carotenoid excited states: From solution to natural and artificial systems
    • Polívka, T., and Sundström, V. (2004) Ultrafast dynamics of carotenoid excited states: From solution to natural and artificial systems. Chem. Rev. 104, 2021-2071.
    • (2004) Chem. Rev. , vol.104 , pp. 2021-2071
    • Polívka, T.1    Sundström, V.2
  • 6
    • 0000402734 scopus 로고    scopus 로고
    • The Electronic States of Carotenoids
    • Frank, H. A., Young, A. J., Britton, G., and Cogdell, R. J., Eds. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Christensen, R. L. (1999) The Electronic States of Carotenoids. In The Photochemistry of Carotenoids (Frank, H. A., Young, A. J., Britton, G., and Cogdell, R. J., Eds.) pp 137-157, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1999) The Photochemistry of Carotenoids , pp. 137-157
    • Christensen, R.L.1
  • 7
    • 33846885226 scopus 로고    scopus 로고
    • Spectroscopy of the peridinin-chlorophyll-a protein: Insight into light-harvesting strategy of marine algae
    • Polívka, T., Hiller, R. G., and Frank, H. A. (2007) Spectroscopy of the peridinin-chlorophyll-a protein: Insight into light-harvesting strategy of marine algae. Arch. Biochem. Biophys. 458, 111-120.
    • (2007) Arch. Biochem. Biophys. , vol.458 , pp. 111-120
    • Polívka, T.1    Hiller, R.G.2    Frank, H.A.3
  • 8
    • 0001412677 scopus 로고    scopus 로고
    • Excited State Properties of Peridinin: Observation of a Solvent Dependence of the Lowest Excited Singlet State Lifetime and Spectral Behavior Unique among Carotenoids
    • Bautista, J. A., Connors, R. E., Raju, B. B., Hiller, R. G., Sharples, F. P., Gosztola, D., Wasielewski, M. R., and Frank, H. A. (1999) Excited State Properties of Peridinin: Observation of a Solvent Dependence of the Lowest Excited Singlet State Lifetime and Spectral Behavior Unique among Carotenoids. J. Phys. Chem. B 103, 8751-8758.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 8751-8758
    • Bautista, J.A.1    Connors, R.E.2    Raju, B.B.3    Hiller, R.G.4    Sharples, F.P.5    Gosztola, D.6    Wasielewski, M.R.7    Frank, H.A.8
  • 9
    • 0000051201 scopus 로고    scopus 로고
    • Effect of the Solvent Environment on the Spectroscopic Properties and Dynamics of the Lowest Excited States of Carotenoids
    • Frank, H. A., Bautista, J. A., Josue, J., Pendon, Z., Hiller, R. G., Sharples, F. P., Gosztola, D., and Wasielewski, M. R. (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    Bautista, J.A.2    Josue, J.3    Pendon, Z.4    Hiller, R.G.5    Sharples, F.P.6    Gosztola, D.7    Wasielewski, M.R.8
  • 10
    • 0035892221 scopus 로고    scopus 로고
    • Spectroscopic and Dynamic Properties of the Peridinin Lowest Singlet Excited States
    • Zigmantas, D., Polivka, T., Hiller, R. G., Yartsev, A., and Sundstrom, V. (2001) Spectroscopic and Dynamic Properties of the Peridinin Lowest Singlet Excited States. J. Phys. Chem. A 105, 10296-10306.
    • (2001) J. Phys. Chem. A , vol.105 , pp. 10296-10306
    • Zigmantas, D.1    Polivka, T.2    Hiller, R.G.3    Yartsev, A.4    Sundstrom, V.5
  • 12
    • 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, R. G., Sundstrom, V., and 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. U.S.A. 99, 16760-16765.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16760-16765
    • Zigmantas, D.1    Hiller, R.G.2    Sundstrom, V.3    Polivka, T.4
  • 13
    • 0030055628 scopus 로고    scopus 로고
    • Structural basis of light harvesting by carotenoids: Peridinin- Chlorophyll-protein from Amphidinium carterae
    • Hofmann, E., Wrench, P. M., Sharples, F. P., Hiller, R. G., Welte, W., and Diederichs, K. (1996) Structural basis of light harvesting by carotenoids: Peridinin-chlorophyll-protein from Amphidinium carterae. Science 272, 1788-1791. (Pubitemid 26256398)
    • (1996) Science , vol.272 , Issue.5269 , pp. 1788-1791
    • Hofmann, E.1    Wrench, P.M.2    Sharples, F.P.3    Hiller, R.G.4    Welte, W.5    Diederichs, K.6
  • 14
    • 0034790212 scopus 로고    scopus 로고
    • The 15-kDa forms of the apo-peridinin-chlorophyll a protein (PCP) in dinoflagellates show high identity with the apo-32 kDa PCP forms, and have similar N-terminal leaders and gene arrangements
    • Hiller, R. G., Crossley, L. G., Wrench, P. M., Santucci, N., and Hofmann, E. (2001) The 15-kDa forms of the apo-peridinin-chlorophyll a protein (PCP) in dinoflagellates show high identity with the apo-32 kDa PCP forms, and have similar N-terminal leaders and gene arrangements. Mol. Genet. Genomics 266, 254-259.
    • (2001) Mol. Genet. Genomics , vol.266 , pp. 254-259
    • Hiller, R.G.1    Crossley, L.G.2    Wrench, P.M.3    Santucci, N.4    Hofmann, E.5
  • 15
    • 0036186407 scopus 로고    scopus 로고
    • Characterization of a short form Peridinin-chlorophyll-protein (PCP) cDNA and protein from the symbiotic dinoflagellate Symbiodinium muscatinei (Dinophyceae) from the sea anemone Anthopleura elegantissima (Cnidaria)
    • DOI 10.1046/j.1529-8817.2002.01132.x
    • Weis, V., Verde, E., and Reynolds, W. (2002) Characterization of a short form Peridinin-Chlorophyll a-Protein (PCP) from the symbiotic dinoflagellate Symbodinium muscatinei (Dinophycae) from the sea anemone Anthopleura elegantissima (Cnidaria). J. Phycol. 38, 157-163. (Pubitemid 34196838)
    • (2002) Journal of Phycology , vol.38 , Issue.1 , pp. 157-163
    • Weis, V.M.1    Alan Verde, E.2    Reynolds, W.S.3
  • 16
    • 0000717368 scopus 로고
    • Purification and characterization of peridinin-chlorophyll a-proteins from the marine dinoflagellates Glenodinium sp. and Gonyaulax polyedra
    • Prézelin, B. B., and Haxo, F. T. (1976) Purification and characterization of peridinin-chlorophyll a-proteins from the marine dinoflagellates Glenodinium sp. and Gonyaulax polyedra. Planta 128 133-141.
    • (1976) Planta , vol.128 , pp. 133-141
    • Prézelin, B.B.1    Haxo, F.T.2
  • 17
    • 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., and Hiller, R. G. (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
  • 18
    • 0033799023 scopus 로고    scopus 로고
    • Excitation transfer in the peridinin-chlorophyll-protein of Amphidinium carterae
    • Damjanović, A., Ritz, T., and Schulten, K. (2000) Excitation transfer in the peridinin-chlorophyll-protein of Amphidinium carterae. Biophys. J. 79, 1695-1705.
    • (2000) Biophys. J. , vol.79 , pp. 1695-1705
    • Damjanović, A.1    Ritz, T.2    Schulten, K.3
  • 20
    • 1042299984 scopus 로고    scopus 로고
    • Spectroscopic Properties of the Main-Form and High-Salt Peridinin-Chlorophyll a Proteins from Amphidinium carterae
    • DOI 10.1021/bi0357964
    • Ilagan, R. P., Shima, S., Melkozernov, A., Lin, S., Blankenship, R. E., Sharples, F. P., Hiller, R. G., Birge, R. R., and Frank, H. A. (2004) Spectroscopic properties of the main-form and high-salt peridinin-chlorophyll a proteins from Amphidinium carterae. Biochemistry 43, 1478-1487. (Pubitemid 38200553)
    • (2004) Biochemistry , vol.43 , Issue.6 , pp. 1478-1487
    • Ilagan, R.P.1    Shima, S.2    Melkozernov, A.3    Lin, S.4    Blankenship, R.E.5    Sharples, F.P.6    Hiller, R.G.7    Birge, R.R.8    Frank, H.A.9
  • 21
    • 25444446803 scopus 로고    scopus 로고
    • Tuning energy transfer in the peridinin-chlorophyll complex by reconstitution with different chlorophylls
    • Polívka, T., Pascher, T., Sundström, V., and Hiller, R. G. (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
  • 22
    • 43149098310 scopus 로고    scopus 로고
    • Energy transfer in the peridinin-chlorophyll protein complex reconstituted with mixed chlorophyll sites
    • Polívka, T., Pascher, T., and Hiller, R. G. (2008) Energy transfer in the peridinin-chlorophyll protein complex reconstituted with mixed chlorophyll sites. Biophys. J. 94, 3198-3207.
    • (2008) Biophys. J. , vol.94 , pp. 3198-3207
    • Polívka, T.1    Pascher, T.2    Hiller, R.G.3
  • 23
    • 36049052096 scopus 로고    scopus 로고
    • Energy transfer in reconstituted peridinin-chlorophyll-protein complexes: Ensemble and single-molecule spectroscopy studies
    • DOI 10.1529/biophysj.107.112094
    • Mackowski, S., Wörmke, S., Brotosudarmo, T. H. P., Jung, C., Hiller, R. G., Scheer, H., and Bräuchle, C. (2007) Energy transfer in reconstituted peridinin-chlorophyll-protein complexes: Ensemble and single-molecule spectroscopy studies. Biophys. J. 93, 3249-3258. (Pubitemid 350097115)
    • (2007) Biophysical Journal , vol.93 , Issue.9 , pp. 3249-3258
    • Mackowski, S.1    Wormke, S.2    Brotosudarmo, T.H.P.3    Jung, C.4    Hiller, R.G.5    Scheer, H.6    Brauchle, C.7
  • 25
    • 3442885385 scopus 로고    scopus 로고
    • Transient Absorption Study of Peridinin and Peridinin-Chlorophyll a-Protein after Two-Photon Excitation
    • Linden, P. A., Zimmermann, J., Brixner, T., Holt, N. E., Vaswani, H. M., Hiller, R. G., and Fleming, G. R. (2004) Transient Absorption Study of Peridinin and Peridinin-Chlorophyll a-Protein after Two-Photon Excitation. J. Phys. Chem. B 108, 10340-10345.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 10340-10345
    • Linden, P.A.1    Zimmermann, J.2    Brixner, T.3    Holt, N.E.4    Vaswani, H.M.5    Hiller, R.G.6    Fleming, G.R.7
  • 26
    • 0030595236 scopus 로고    scopus 로고
    • Excitation energy transfer in carotenoid-chlorophyll protein complexes probed by femtosecond fluorescence decays
    • Akimoto, S., Takaichi, S., Ogata, T., Nishimura, Y., Yamazaki, I., and Mimuro, M. (1996) Excitation energy transfer in carotenoid-chlorophyll protein complexes probed by femtosecond fluorescence decays. Chem. Phys. Lett. 260, 147-152.
    • (1996) Chem. Phys. Lett. , vol.260 , pp. 147-152
    • Akimoto, S.1    Takaichi, S.2    Ogata, T.3    Nishimura, Y.4    Yamazaki, I.5    Mimuro, M.6
  • 27
    • 0001001551 scopus 로고    scopus 로고
    • Singlet and Triplet Energy Transfer in the Peridinin-Chlorophyll a-Protein from Amphidinium carterae
    • Bautista, J. A., Hiller, R. G., Sharples, F. P., Gosztola, D., Wasielewski, M., and Frank, H. A. (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    Hiller, R.G.2    Sharples, F.P.3    Gosztola, D.4    Wasielewski, M.5    Frank, H.A.6
  • 28
    • 84961979081 scopus 로고    scopus 로고
    • Two-Photon and Fluorescence Spectroscopy and the Effect of Environment on the Photochemical Properties of Peridinin in Solution and in the Peridinin-Chlorophyll-Protein from Amphidinium carterae
    • Shima, S., Ilagan, R. P., Gillespie, N., Sommer, B. J., Hiller, R. G., Sharples, F. P., Frank, H. A., and Birge, R. R. (2003) Two-Photon and Fluorescence Spectroscopy and the Effect of Environment on the Photochemical Properties of Peridinin in Solution and in the Peridinin-Chlorophyll-Protein from Amphidinium carterae. J. Phys. Chem. A 107, 8052-8066.
    • (2003) J. Phys. Chem. A , vol.107 , pp. 8052-8066
    • Shima, S.1    Ilagan, R.P.2    Gillespie, N.3    Sommer, B.J.4    Hiller, R.G.5    Sharples, F.P.6    Frank, H.A.7    Birge, R.R.8
  • 29
    • 0030581507 scopus 로고    scopus 로고
    • Two distinct forms of the peridinin-chlorophyll a-protein from Amphidinium carterae
    • Sharples, F. P., Wrench, P. M., Ou, K., and Hiller, R. G. (1996) Two distinct forms of the peridinin-chlorophyll a-protein from Amphidinium carterae. Biochim. Biophys. Acta 1276, 117-123.
    • (1996) Biochim. Biophys. Acta , vol.1276 , pp. 117-123
    • Sharples, F.P.1    Wrench, P.M.2    Ou, K.3    Hiller, R.G.4
  • 30
    • 33751568892 scopus 로고    scopus 로고
    • Femtosecond time-resolved absorption spectroscopy of main-form and high-salt peridinin-chlorophyll a-proteins at low temperatures
    • DOI 10.1021/bi061217u
    • Ilagan, R. P., Koscielecki, J. F., Hiller, R. G., Sharples, F. P., Gibson, G. N., Birge, R. R., and Frank, H. A. (2006) Femtosecond time-resolved absorption spectroscopy of main-form and high-salt peridinin-chlorophyll a-proteins at low temperatures. Biochemistry 45, 14052-14063. (Pubitemid 44846194)
    • (2006) Biochemistry , vol.45 , Issue.47 , pp. 14052-14063
    • Ilagan, R.P.1    Koscielecki, J.F.2    Hiller, R.G.3    Sharples, F.P.4    Gibson, G.N.5    Birge, R.R.6    Frank, H.A.7
  • 31
    • 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
  • 32
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An Automated Program for Molecular Replacement
    • Vagin, A., and 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
  • 33
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • DOI 10.1107/S0907444994003112
    • Collaborative Computational Project No.4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D50, 760-763. (Pubitemid 2143461)
    • (1994) Acta Crystallographica Section D: Biological Crystallography , vol.50 , Issue.5 , pp. 760-763
  • 38
    • 0030845843 scopus 로고    scopus 로고
    • Model building and refinement practice
    • DOI 10.1016/S0076-6879(97)77013-7
    • Kleywegt, G. J., and Jones, T. A. (1997) Model building and refinement practice. Methods Enzymol. 277, 208-230. (Pubitemid 27390923)
    • (1997) Methods in Enzymology , vol.277 , pp. 208-230
    • Kleywegt, G.J.1    Jones, T.A.2
  • 39
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • 29
    • Vriend, G. (1990) WHAT IF: A molecular modeling and drug design program. J. Mol. Graphics 8, 52-56, 29.
    • (1990) J. Mol. Graphics , vol.8 , pp. 52-56
    • Vriend, G.1
  • 41
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • DOI 10.1107/S0907444904026460
    • Krissinel, E., and Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D60, 2256-2268. (Pubitemid 41742778)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.12 I , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 42
    • 52949120294 scopus 로고    scopus 로고
    • Spectroscopic properties of the peridinins involved in chlorophyll triplet quenching in high-salt peridinin-chlorophyll a-protein from Amphidinium carterae as revealed by optically detected magnetic resonance, pulse EPR and pulse ENDOR spectroscopies
    • Di Valentin, M., Ceola, S., Salvadori, E., Agostini, G., Giacometti, G. M., and Carbonera, D. (2008) Spectroscopic properties of the peridinins involved in chlorophyll triplet quenching in high-salt peridinin-chlorophyll a-protein from Amphidinium carterae as revealed by optically detected magnetic resonance, pulse EPR and pulse ENDOR spectroscopies. Biochim. Biophys. Acta 1777, 1355-1363.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1355-1363
    • Di Valentin, M.1    Ceola, S.2    Salvadori, E.3    Agostini, G.4    Giacometti, G.M.5    Carbonera, D.6
  • 45
    • 84981779372 scopus 로고
    • Zwischenmolekulare Energiewanderung und Fluoreszenz
    • Förster, T. (1948) Zwischenmolekulare Energiewanderung und Fluoreszenz. Ann. Phys. 437, 55-75.
    • (1948) Ann. Phys. , vol.437 , pp. 55-75
    • Förster, T.1
  • 46
    • 33845907977 scopus 로고    scopus 로고
    • Protein-bound chromophores astaxanthin and phytochromobilin: Excited state quantum chemical studies
    • Durbeej, B., and Eriksson, L. A. (2006) Protein-bound chromophores astaxanthin and phytochromobilin: Excited state quantum chemical studies. Phys. Chem. Chem. Phys. 8, 4053-4071.
    • (2006) Phys. Chem. Chem. Phys. , vol.8 , pp. 4053-4071
    • Durbeej, B.1    Eriksson, L.A.2
  • 47
    • 33645466086 scopus 로고    scopus 로고
    • Quantum chemical simulation of excited states of chlorophylls, bacteriochlorophylls and their complexes
    • Linnanto, J., and Korppi-Tommola, J. (2006) Quantum chemical simulation of excited states of chlorophylls, bacteriochlorophylls and their complexes. Phys. Chem. Chem. Phys. 8, 663-687.
    • (2006) Phys. Chem. Chem. Phys. , vol.8 , pp. 663-687
    • Linnanto, J.1    Korppi-Tommola, J.2
  • 48
  • 49
    • 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, R. J., Gall, A., and 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
  • 50
    • 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., and 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
  • 51
    • 40049088169 scopus 로고    scopus 로고
    • Pulse ENDOR and density functional theory on the peridinin triplet state involved in the photo-protective mechanism in the peridinin-chlorophyll a-protein from Amphidinium carterae
    • Di Valentin, M., Ceola, S., Agostini, G., Giacometti, G. M., Angerhofer, A., Crescenzi, O., Barone, V., and Carbonera, D. (2008) Pulse ENDOR and density functional theory on the peridinin triplet state involved in the photo-protective mechanism in the peridinin-chlorophyll a-protein from Amphidinium carterae. Biochim. Biophys. Acta 1777, 295-307.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 295-307
    • Di Valentin, M.1    Ceola, S.2    Agostini, G.3    Giacometti, G.M.4    Angerhofer, A.5    Crescenzi, O.6    Barone, V.7    Carbonera, D.8
  • 54
    • 34548786207 scopus 로고    scopus 로고
    • y electronic energy in chlorophyll-protein complexes and generates spectral forms
    • DOI 10.1529/biophysj.107.104554
    • Zucchelli, G., Brogioli, D., Casazza, A. P., Garlaschi, F. M., and Jennings, R. C. (2007) Chlorophyll ring deformation modulates Qy electronic energy in chlorophyll-protein complexes and generates spectral forms. Biophys. J. 93, 2240-2254. (Pubitemid 47437607)
    • (2007) Biophysical Journal , vol.93 , Issue.6 , pp. 2240-2254
    • Zucchelli, G.1    Brogioli, D.2    Casazza, A.P.3    Garlaschi, F.M.4    Jennings, R.C.5
  • 56
    • 31144435722 scopus 로고    scopus 로고
    • Use of ultrafast dispersed pump-dump-probe and pump-repump-probe spectroscopies to explore the light-induced dynamics of peridinin in solution
    • Papagiannakis, E., Vengris, M., Larsen, D. S., van Stokkum, I. H. M., Hiller, R. G., and van Grondelle, R. (2006) Use of ultrafast dispersed pump-dump-probe and pump-repump-probe spectroscopies to explore the light-induced dynamics of peridinin in solution. J. Phys. Chem. B 110, 512-521.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 512-521
    • Papagiannakis, E.1    Vengris, M.2    Larsen, D.S.3    Van Stokkum, I.H.M.4    Hiller, R.G.5    Van Grondelle, R.6
  • 58
    • 33847142225 scopus 로고    scopus 로고
    • CAVER: A new tool to explore routes from protein clefts, pockets and cavities
    • DOI 10.1186/1471-2105-7-316
    • Petrek, M., Otyepka, M., Banás, P., Kosinová, P., Koca, J., and Damborský, J. (2006) CAVER: A new tool to explore routes from protein clefts, pockets and cavities. BMC Bioinf. 7, 316. (Pubitemid 46277092)
    • (2006) BMC Bioinformatics , vol.7 , pp. 316
    • Petrek, M.1    Otyepka, M.2    Banas, P.3    Kosinova, P.4    Koca, J.5    Damborsky, J.6
  • 59
    • 25444500136 scopus 로고    scopus 로고
    • Reconstitution of the peridinin-chlorophyll a protein (PCP): Evidence for functional flexibility in chlorophyll binding
    • Miller, D. J., Catmull, J., Puskeiler, R., Tweedale, H., Sharples, F. P., and Hiller, R. G. (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    Catmull, J.2    Puskeiler, R.3    Tweedale, H.4    Sharples, F.P.5    Hiller, R.G.6
  • 60
    • 0038171507 scopus 로고    scopus 로고
    • Dynamics of Excited States of the Carotenoid Peridinin in Polar Solvents: Dependence on Excitation Wavelength, Viscosity, and Temperature
    • Zigmantas, D., Hiller, R. G., Yartsev, A., Sundstrom, V., and Polivka, T. (2003) Dynamics of Excited States of the Carotenoid Peridinin in Polar Solvents: Dependence on Excitation Wavelength, Viscosity, and Temperature. J. Phys. Chem. B 107, 5339-5348.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 5339-5348
    • Zigmantas, D.1    Hiller, R.G.2    Yartsev, A.3    Sundstrom, V.4    Polivka, T.5
  • 63
    • 0030970581 scopus 로고    scopus 로고
    • Resonance raman examination of the wavelength regulation mechanism in human visual pigments
    • DOI 10.1021/bi970322o
    • Kochendoerfer, G. G., Wang, Z., Oprian, D. D., and Mathies, R. A. (1997) Resonance Raman examination of the wavelength regulation mechanism in human visual pigments. Biochemistry 36 6577-6587. (Pubitemid 27242315)
    • (1997) Biochemistry , vol.36 , Issue.22 , pp. 6577-6587
    • Kochendoerfer, G.G.1    Wang, Z.2    Oprian, D.D.3    Mathies, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.