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Volumn 15, Issue 4, 2014, Pages 332-350

The unique photophysical properties of the Peridinin-Chlorophyll-a-Protein

Author keywords

Carotenoids; Light harvesting; Peridinin; Peridinin chlorophyll protein; Photoprotection

Indexed keywords

CAROTENOID; NANOMATERIAL; PERIDININ CHLOROPHYLL A PROTEIN; PLANT MEDICINAL PRODUCT; UNCLASSIFIED DRUG; PERIDININ CHLOROPHYLL-A PROTEIN, DINOPHYCEAE; PROTOZOAL PROTEIN;

EID: 84901979721     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/1389203715666140327111139     Document Type: Article
Times cited : (38)

References (148)
  • 1
    • 78149406115 scopus 로고    scopus 로고
    • Structure and function of native and refolded peridinin-chlorophyll-proteins from dinoflagellates
    • Schulte, T.; Johanning, S.; Hofmann, E. Structure and function of native and refolded peridinin-chlorophyll-proteins from dinoflagellates. Eur. J. Cell Biol., 2010, 89, 990-997.
    • (2010) Eur. J. Cell Biol , vol.89 , pp. 990-997
    • Schulte, T.1    Johanning, S.2    Hofmann, E.3
  • 2
    • 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.; Frank, H.A. Spectroscopy of the peridinin- chlorophyll-a protein: insight into light-harvesting strategy of marine algae. Arch. Biochem. Biophys., 2007, 458, 111-120.
    • (2007) Arch. Biochem. Biophys , vol.458 , pp. 111-120
    • Polívka, T.1    Hiller, R.G.2    Frank, H.A.3
  • 3
    • 0017107168 scopus 로고
    • Molecular topology of photosynthetic light-harvesting pigment complex, peridininchlorophyll- a-protein, from marine dinoflagellates
    • Song, P-S.; Koka, P.; Prezelin, B.B.; Haxo, F.T. Molecular topology of photosynthetic light-harvesting pigment complex, peridininchlorophyll- a-protein, from marine dinoflagellates, Biochemistry, 1976, 15, 4422-4427.
    • (1976) Biochemistry , vol.15 , pp. 4422-4427
    • Song, P.-S.1    Koka, P.2    Prezelin, B.B.3    Haxo, F.T.4
  • 4
    • 0017697816 scopus 로고
    • The chromophore topography and binding environment of peridinin-chlorophyll-a-protein complexes from marine dinoflagellate algae
    • Koka, P.; Song, P.-S. The chromophore topography and binding environment of peridinin-chlorophyll-a-protein complexes from marine dinoflagellate algae Biochim. Biophys. Acta - General Subjects, 1977, 495, 220-231.
    • (1977) Biochim. Biophys. Acta - General Subjects , vol.495 , pp. 220-231
    • Koka, P.1    Song, P.-S.2
  • 5
    • 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.; Diederichs, K. Structural basis of light harvesting by carotenoids: peridinin-chlorophyll-protein from Amphidinium carterae Science, 1996, 272, 1788-1791.
    • (1996) Science , vol.272 , pp. 1788-1791
    • Hofmann, E.1    Wrench, P.M.2    Sharples, F.P.3    Hiller, R.G.4    Welte, W.5    Diederichs, K.6
  • 7
    • 66349088474 scopus 로고    scopus 로고
    • X-ray structure of the high-salt form of peridinin-chlorophyll-a protein from the Dinoflagellate Amphidinium carterae; modulation of the spectral properties of pigments by the protein environment
    • Schulte, T; Sharples, F.P.; Hiller, R.G.; Hofmann, E. X-ray structure of the high-salt form of peridinin-chlorophyll-a protein from the Dinoflagellate Amphidinium carterae; modulation of the spectral properties of pigments by the protein environment, Biochemistry, 2009, 48, 4466-4475.
    • (2009) Biochemistry , vol.48 , pp. 4466-4475
    • Schulte, T.1    Sharples, F.P.2    Hiller, R.G.3    Hofmann, E.4
  • 8
    • 76749127987 scopus 로고    scopus 로고
    • X-ray structures of the peridinin- chlorophyll-proteins reconstituted with different chlorophylls
    • Schulte, T; Hiller, R.G.; Hofmann, E. X-ray structures of the peridinin- chlorophyll-proteins reconstituted with different chlorophylls, FEBS Lett., 2010, 584, 973-978.
    • (2010) FEBS Lett , vol.584 , pp. 973-978
    • Schulte, T.1    Hiller, R.G.2    Hofmann, E.3
  • 9
    • 7944238095 scopus 로고    scopus 로고
    • A new immunofluorostaining method using red fluorescence of PerCP of formalin-fixed paraffin-embedded tissues
    • Niki, S.; Hosokawa, K.; Nagaike K.; Tagawa, T. A new immunofluorostaining method using red fluorescence of PerCP of formalin-fixed paraffin-embedded tissues, J. Immunol. Methods, 2004, 293, 143-151.
    • (2004) J. Immunol. Methods , vol.293 , pp. 143-151
    • Niki, S.1    Hosokawa, K.2    Nagaike, K.3    Tagawa, T.4
  • 10
    • 84876901346 scopus 로고    scopus 로고
    • Spectroscopic studies of plasmon coupling between photosynthetic complexes and metallic quantum dots
    • Olejnik, M.; Krajnik, B.; Kowalska, D.; Lin, G.; Mackowski, S. Spectroscopic studies of plasmon coupling between photosynthetic complexes and metallic quantum dots. J. Phys. Condens. Matter, 2013, 25, 194103.
    • (2013) J. Phys. Condens. Matter , vol.25 , pp. 194103
    • Olejnik, M.1    Krajnik, B.2    Kowalska, D.3    Lin, G.4    Mackowski, S.5
  • 11
    • 0000402734 scopus 로고    scopus 로고
    • The electronic states of carotenoids
    • Frank, H.A.; Young, A.J.; Britton, G.; Cogdell, R.J. eds. Kluwer Academic Publishers
    • Christensen, R.L. The electronic states of carotenoids, in: The photochemistry of carotenoids, Frank, H.A.; Young, A.J.; Britton, G.; Cogdell, R.J. eds. Kluwer Academic Publishers, 1999, 137-159.
    • (1999) The Photochemistry of Carotenoids , pp. 137-159
    • Christensen, R.L.1
  • 12
    • 2342539764 scopus 로고    scopus 로고
    • Ultrafast dynamics of carotenoid excited States-from solution to natural and artificial systems
    • Polivka, T.; Sundstrom, V. Ultrafast dynamics of carotenoid excited States-from solution to natural and artificial systems, Chem. Rev. 2004, 104, 2021-2071.
    • (2004) Chem. Rev , vol.104 , pp. 2021-2071
    • Polivka, T.1    Sundstrom, V.2
  • 13
    • 0026536764 scopus 로고
    • Molecular structure and optical properties of carotenoids for the in vivo energy transfer function in algal photosynthetic pigment system
    • Mimuro, M.; Nagashima, M.; Takaichi, S.; Nishimura, Y.; Yamazaki, I.; Katoh, T. Molecular structure and optical properties of carotenoids for the in vivo energy transfer function in algal photosynthetic pigment system. Biochim. Biophys. Acta - Bioenergetics, 1992, 1098, 271-274.
    • (1992) Biochim. Biophys. Acta - Bioenergetics , vol.1098 , pp. 271-274
    • Mimuro, M.1    Nagashima, M.2    Takaichi, S.3    Nishimura, Y.4    Yamazaki, I.5    Katoh, T.6
  • 14
    • 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.; Gostzola, D.; Wasielewski, M.R. 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, 1999, 1903, 8751-8758.
    • (1999) J. Phys. Chem. B , vol.1903 , pp. 8751-8758
    • Bautista, J.A.1    Connors, R.E.2    Raju, B.B.3    Hiller, R.G.4    Sharples, F.P.5    Gostzola, D.6    Wasielewski, M.R.7
  • 15
    • 84904460037 scopus 로고    scopus 로고
    • An Approach Based on Synthetic Organic Chemistry Toward Elucidation of Highly Efficient Energy Transfer Ability of Peridinin in Photosynthesis, in Artificial photosynthesis
    • Kajikawa, T.; Katsumu, S. An Approach Based on Synthetic Organic Chemistry Toward Elucidation of Highly Efficient Energy Transfer Ability of Peridinin in Photosynthesis, in Artificial photosynthesis, Mohammad Mahdi Najafpour ed., Intechopen, 2012, pp. 135-152.
    • Intechopen , vol.2012 , pp. 135-152
    • Kajikawa, T.1    Katsumu, S.2
  • 16
    • 84879058314 scopus 로고    scopus 로고
    • Excited states energy and dynamics of peridinin analogues and tyhe nature of the intramolecular charge ttranfer state in carbonyl-containing carotenoids
    • Niedzwiedzki, D.M.; Kajikawa, T.; Aoki, K.; Katsumura, S.; Frank, H.A. Excited states energy and dynamics of peridinin analogues and tyhe nature of the intramolecular charge ttranfer state in carbonyl-containing carotenoids, J. Phys. Chem. B, 2013, 117, 6874-6887.
    • (2013) J. Phys. Chem. B , vol.117 , pp. 6874-6887
    • Niedzwiedzki, D.M.1    Kajikawa, T.2    Aoki, K.3    Katsumura, S.4    Frank, H.A.5
  • 19
    • 70349973221 scopus 로고    scopus 로고
    • Spectroscopic investigation of peridinin analogues having different π-electron conjugated chain length; exploring the nature of the intramolecular charge transfer state
    • Niedzwiedzki, D.M.; Chattarjee, N.; Enriquez, M.M.; Kajikawa, T.; Hasegawa, S.; Katsumura, S.; Frank, H.A. Spectroscopic investigation of peridinin analogues having different π-electron conjugated chain length; exploring the nature of the intramolecular charge transfer state, J. Phys. Chem. B, 2009, 113, 13604-13612.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 13604-13612
    • Niedzwiedzki, D.M.1    Chattarjee, N.2    Enriquez, M.M.3    Kajikawa, T.4    Hasegawa, S.5    Katsumura, S.6    Frank, H.A.7
  • 20
    • 77952663437 scopus 로고    scopus 로고
    • Syntheses of ylidenbutenolide-modicfied derivatives of peridinin and their stereochemical and spectral characteristics
    • Kajikawa, T.; Aoki, K.; Iwashita, T.; Niedzwiedzki, D.M.; Frank, H.A.; Katsumura, S. Syntheses of ylidenbutenolide-modicfied derivatives of peridinin and their stereochemical and spectral characteristics, Org. Biomolec. Chem., 2010, 8, 2513-2516.
    • (2010) Org. Biomolec. Chem , vol.8 , pp. 2513-2516
    • Kajikawa, T.1    Aoki, K.2    Iwashita, T.3    Niedzwiedzki, D.M.4    Frank, H.A.5    Katsumura, S.6
  • 23
    • 40349092954 scopus 로고    scopus 로고
    • Excited state structural dynamics of the charge transfer of peridinin
    • Van Tassle, A.J.; Prantil, M.A.; Hiller, R.G.; Fleming, G.R. Excited state structural dynamics of the charge transfer of peridinin. Isr. J. Chem., 2007, 47, 17-24.
    • (2007) Isr. J. Chem , vol.47 , pp. 17-24
    • van Tassle, A.J.1    Prantil, M.A.2    Hiller, R.G.3    Fleming, G.R.4
  • 24
    • 77955389049 scopus 로고    scopus 로고
    • Identification of excited-state energy transfer and relaxation pathways in the peridinin- chlorophyll complex; an ultrafast mid-infrared study
    • Bonetti, C.; Alexandre, M.T.A.; van Stokkum, I.H.M.; Hiller, R.G.; Groot, M.L.; van Grondelle, R.; Kennis, J.T.M. Identification of excited-state energy transfer and relaxation pathways in the peridinin- chlorophyll complex; an ultrafast mid-infrared study. Phys. Chem. Chem. Phys., 2010, 12, 9256-9266.
    • (2010) Phys. Chem. Chem. Phys , vol.12 , pp. 9256-9266
    • Bonetti, C.1    Alexandre, M.T.A.2    van Stokkum, I.H.M.3    Hiller, R.G.4    Groot, M.L.5    van Grondelle, R.6    Kennis, J.T.M.7
  • 25
    • 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.; Birge, R.R. 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, 2003, 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
  • 26
    • 0041733056 scopus 로고    scopus 로고
    • Quantum chemical evidence for an intramolecular charge-transfer state in the carotenoid peridinin of Peridinin-Chlorophyll-Protein
    • Vaswani, H.M.; Hsu, C.-P.; Head-Gordon, M.; Fleming, G.R. Quantum chemical evidence for an intramolecular charge-transfer state in the carotenoid peridinin of Peridinin-Chlorophyll-Protein. J. Phys. Chem. B, 2003, 107, 7940-7946.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 7940-7946
    • Vaswani, H.M.1    Hsu, C.-P.2    Head-Gordon, M.3    Fleming, G.R.4
  • 27
    • 4344679386 scopus 로고    scopus 로고
    • A DFT study of Low-Lying Singlet Excited States of the all-trans Peridinin in vacuo
    • Spezia, R.; Zazza, C.; Palma, A.; Amadei, A.; Aschi, M. A DFT study of Low-Lying Singlet Excited States of the all-trans Peridinin in vacuo. J. Phys. Chem. A, 2004, 108, 6763-6770.
    • (2004) J. Phys. Chem. A , vol.108 , pp. 6763-6770
    • Spezia, R.1    Zazza, C.2    Palma, A.3    Amadei, A.4    Aschi, M.5
  • 30
    • 59649097830 scopus 로고    scopus 로고
    • Chl-a triplet quenching by peridinin in H-PCP and organic solvent revealed by step-scan FTIR time-resolved spectroscopy
    • Bonetti, C.; Alexandre, M.T.A.; Hiller, R.G.; Kennis, J.T.M.; van Grondelle, R. Chl-a triplet quenching by peridinin in H-PCP and organic solvent revealed by step-scan FTIR time-resolved spectroscopy, Chem. Phys., 2009, 357, 63-69.
    • (2009) Chem. Phys , vol.357 , pp. 63-69
    • Bonetti, C.1    Alexandre, M.T.A.2    Hiller, R.G.3    Kennis, J.T.M.4    van Grondelle, R.5
  • 31
    • 47749097223 scopus 로고    scopus 로고
    • Time-resolved step scan FTIR spectroscopy and DFT investigation on triplet formation in peridininchlorophyll- a-protein from Amphidinium carterae at low temperature
    • Mezzetti, A.; Spezia, R. Time-resolved step scan FTIR spectroscopy and DFT investigation on triplet formation in peridininchlorophyll- a-protein from Amphidinium carterae at low temperature, Spectroscopy Int. J., 2008, 22, 235-250.
    • (2008) Spectroscopy Int. J , vol.22 , pp. 235-250
    • Mezzetti, A.1    Spezia, R.2
  • 32
    • 84877010198 scopus 로고    scopus 로고
    • The nature of the intramolecular charge transfer state in peridinin
    • Wagner, N.L.; Greco, J.A.; Enriquez, M.M.; Frank, H.A.; Birge, R.R. The nature of the intramolecular charge transfer state in peridinin. Biophys. J., 2013, 104, 1314-1325.
    • (2013) Biophys. J , vol.104 , pp. 1314-1325
    • Wagner, N.L.1    Greco, J.A.2    Enriquez, M.M.3    Frank, H.A.4    Birge, R.R.5
  • 33
  • 34
    • 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.; Sundstrom, V. Spectroscopic and Dynamic Properties of the Peridinin Lowest Singlet Excited States. J. Phys. Chem. A, 2001, 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
  • 36
  • 38
    • 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.; Polivka, T. 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., 2002, 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
  • 39
    • 25444446803 scopus 로고    scopus 로고
    • Tuning energy transfer in the peridinin-chlorophyll complex by reconstitution with different chlorophylls
    • Polivka, T.; Pascher, T.; Sundstrom, V.; Hiller, R.G. Tuning energy transfer in the peridinin-chlorophyll complex by reconstitution with different chlorophylls. Photosynth. Res., 2005, 86, 217-227.
    • (2005) Photosynth. Res , vol.86 , pp. 217-227
    • Polivka, T.1    Pascher, T.2    Sundstrom, V.3    Hiller, R.G.4
  • 40
    • 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.; Goszola, D.; Wasielewski, M.; Frank, H.A. Singlet and triplet energy transfer in the Peridinin-Chlorophyll a-Protein from Amphidinium carterae. J. Phys. Chem. A, 1999, 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    Goszola, D.4    Wasielewski, M.5    Frank, H.A.6
  • 41
    • 0038171507 scopus 로고    scopus 로고
    • Dynamics of exicted states of the carotenoid peridinin in polar solvents: Dependence on excitation wavelength, viscosity and temperature
    • Zigmantas, D.; Hiller, R.G.; Yarsev, A.; Sundstrom, V.; Polivka, T. Dynamics of exicted states of the carotenoid peridinin in polar solvents: dependence on excitation wavelength, viscosity and temperature. J. Phys. Chem. B, 2003, 107, 5339-5348.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 5339-5348
    • Zigmantas, D.1    Hiller, R.G.2    Yarsev, A.3    Sundstrom, V.4    Polivka, T.5
  • 42
    • 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.; van Grondelle, R. 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, 2006, 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
  • 43
    • 84856394555 scopus 로고    scopus 로고
    • Quantum chemical description of absorption properties and excited-state processes in photosynthetic systems
    • König, C.; Neugebauer, J. Quantum chemical description of absorption properties and excited-state processes in photosynthetic systems. ChemPhysChem, 2012, 13, 386-425.
    • (2012) ChemPhysChem , vol.13 , pp. 386-425
    • König, C.1    Neugebauer, J.2
  • 44
    • 0031650023 scopus 로고    scopus 로고
    • Reparametrizing MNDO for Excited- State Calculations by Using ab Initio Effective Hamiltonian Theory: Application to the 2,4-Pentadien-1-iminium Cation
    • Martin, C.H.; Birge, R.R. Reparametrizing MNDO for Excited- State Calculations by Using ab Initio Effective Hamiltonian Theory: Application to the 2,4-Pentadien-1-iminium Cation J. Phys. Chem. A, 1998, 102, 852-860.
    • (1998) J. Phys. Chem. A , vol.102 , pp. 852-860
    • Martin, C.H.1    Birge, R.R.2
  • 46
    • 37549014315 scopus 로고    scopus 로고
    • The spin-flip equation-of-motion coupled-cluster electronic structure method for a description of excited states, bond-breaking, diradicals, and triradicals
    • Krylov, A.I. The spin-flip equation-of-motion coupled-cluster electronic structure method for a description of excited states, bond-breaking, diradicals, and triradicals Ann. Rev. Phys Chem., 2008, 59, 433-462.
    • (2008) Ann. Rev. Phys Chem , vol.59 , pp. 433-462
    • Krylov, A.I.1
  • 47
    • 0042813364 scopus 로고
    • Spectra of porphyrins
    • Gouterman, M. Spectra of porphyrins. J. Mol. Spectrosc., 1961, 6, 138-163.
    • (1961) J. Mol. Spectrosc , vol.6 , pp. 138-163
    • Gouterman, M.1
  • 48
  • 49
    • 0034326291 scopus 로고    scopus 로고
    • Spectroscopic properties of Mgchlorin, Mg-porphin and chlorophylls a, b, c1, c2, c3 and d studied by semiempirical MO/CI methods
    • Linnanto, J.; Korppi-Tommola, J. Spectroscopic properties of Mgchlorin, Mg-porphin and chlorophylls a, b, c1, c2, c3 and d studied by semiempirical MO/CI methods. Phys. Chem. Chem. Phys., 2000, 2, 4962-4970.
    • (2000) Phys. Chem. Chem. Phys , vol.2 , pp. 4962-4970
    • Linnanto, J.1    Korppi-Tommola, J.2
  • 50
    • 3142727938 scopus 로고    scopus 로고
    • Structure and Spectroscopic Properties of Mg-Bacteriochlorin, and Methyl Bacteriochlorophyllides a, b, g, and h Studied by Semiempirical, Ab Initio and Density Functional Molecular Orbital Methods
    • Linnanto, J.; Korppi-Tommola, J. Structure and Spectroscopic Properties of Mg-Bacteriochlorin, and Methyl Bacteriochlorophyllides a, b, g, and h Studied by Semiempirical, Ab Initio and Density Functional Molecular Orbital Methods. J. Phys. Chem. A, 2004, 108, 5872-5882.
    • (2004) J. Phys. Chem. A , vol.108 , pp. 5872-5882
    • Linnanto, J.1    Korppi-Tommola, J.2
  • 51
    • 79959732211 scopus 로고    scopus 로고
    • First-Principles Calculation of Light- Harvesting Complex II
    • König C.; Neugebauer J. First-Principles Calculation of Light- Harvesting Complex II. Phys. Chem. Chem. Phys., 2011, 13, 10475-10480.
    • (2011) Phys. Chem. Chem. Phys , vol.13 , pp. 10475-10480
    • König, C.1    Neugebauer, J.2
  • 52
    • 0003975118 scopus 로고
    • CRC Press, Boca Raton
    • Scheer, H. Chlorophylls, CRC Press, Boca Raton, 1991.
    • (1991) Chlorophylls
    • Scheer, H.1
  • 53
    • 0037015749 scopus 로고    scopus 로고
    • Chlorophyll Excitations in Photosystem I of Synechococcus elongates
    • Damjanovic, A.; Vaswani, H.M.; Fromme, P.; Fleming, G.R. Chlorophyll Excitations in Photosystem I of Synechococcus elongates. J. Phys. Chem. B, 2002, 106, 10251-10262.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 10251-10262
    • Damjanovic, A.1    Vaswani, H.M.2    Fromme, P.3    Fleming, G.R.4
  • 54
    • 37749030050 scopus 로고    scopus 로고
    • Calculation of pigment transition energies in the FMO protein
    • Adolphs, J.; Müh, F.; Madjet, M.E.; Renger, T. Calculation of pigment transition energies in the FMO protein. Photosynth. Res., 2008, 95, 197-209.
    • (2008) Photosynth. Res , vol.95 , pp. 197-209
    • Adolphs, J.1    Müh, F.2    Madjet, M.E.3    Renger, T.4
  • 55
    • 77949381093 scopus 로고    scopus 로고
    • Structure-based calculations of optical spectra of photosystem I suggest an asymmetric light-harvesting process
    • Adolphs, J.; Müh, F.; Madjet, M.E.; Schmidt, am Busch, M.S.; Renger, T. Structure-based calculations of optical spectra of photosystem I suggest an asymmetric light-harvesting process. J. Am. Chem. Soc., 2010, 132, 3331-3343.
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 3331-3343
    • Adolphs, J.1    Müh, F.2    Madjet, M.E.3    Schmidt4    Busch, M.S.5    Renger, T.6
  • 56
    • 0000187925 scopus 로고
    • Infrared spectra, molecular weights, and molecular association of chlorophylls a and b, methyl chlorophyllides and pheophytins in various solvents
    • Katz, J.J.; Closs, G.L.; Pennington, F.C.; Thomas, M.R.; Strain, H.H. Infrared spectra, molecular weights, and molecular association of chlorophylls a and b, methyl chlorophyllides and pheophytins in various solvents. J. Am. Chem. Soc., 1963, 85, 3801-3809.
    • (1963) J. Am. Chem. Soc , vol.85 , pp. 3801-3809
    • Katz, J.J.1    Closs, G.L.2    Pennington, F.C.3    Thomas, M.R.4    Strain, H.H.5
  • 57
    • 0001047641 scopus 로고    scopus 로고
    • Transient Hole Burning and Solvation Dynamics of Chlorophyll b Monomers in Various Solvent Environments
    • Oksanen, J.A.I.; Martinsson, P.; Åkesson, E.; Hynninen, P.H.; Sundström, V. Transient Hole Burning and Solvation Dynamics of Chlorophyll b Monomers in Various Solvent Environments. J. Phys. Chem. A, 1998, 102, 4328-4336.
    • (1998) J. Phys. Chem. A , vol.102 , pp. 4328-4336
    • Oksanen, J.A.I.1    Martinsson, P.2    Åkesson, E.3    Hynninen, P.H.4    Sundström, V.5
  • 59
    • 34249009265 scopus 로고    scopus 로고
    • ODMR spectroscopy of molecular functions in photosynthetic membrane proteins
    • Giacometti, G.; Agostini, G.; Santabarbara, S.; Carbonera, D. ODMR spectroscopy of molecular functions in photosynthetic membrane proteins. Appl. Magn. Res., 2007, 31, 179-191.
    • (2007) Appl. Magn. Res , vol.31 , pp. 179-191
    • Giacometti, G.1    Agostini, G.2    Santabarbara, S.3    Carbonera, D.4
  • 60
    • 0026069087 scopus 로고
    • The chlorophyll triplet state as a probe of structure and function in photosynthesis
    • Budil, D.E.; Thurnauer, M.C. The chlorophyll triplet state as a probe of structure and function in photosynthesis. Biochim. Biophys. Acta-Bioenerg., 1991, 1057, 1-41.
    • (1991) Biochim. Biophys. Acta-Bioenerg , vol.1057 , pp. 1-41
    • Budil, D.E.1    Thurnauer, M.C.2
  • 61
    • 4243654362 scopus 로고
    • ESR in zero field of the photoinduced triplet state in isolated reaction centers of rhodopseudomonas sphaeroides R-26 detected by the singlet ground-state absorbance
    • den Blanken, H.J.; van der Zwet, G.P.; Hoff, A.J. ESR in zero field of the photoinduced triplet state in isolated reaction centers of rhodopseudomonas sphaeroides R-26 detected by the singlet ground-state absorbance. Chem. Phys Lett., 1982, 85, 335-338.
    • (1982) Chem. Phys Lett , vol.85 , pp. 335-338
    • den Blanken, H.J.1    van der Zwet, G.P.2    Hoff, A.J.3
  • 63
    • 0035976019 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy of primary electron donors in type I photosynthetic reaction centers
    • Breton, J. Fourier transform infrared spectroscopy of primary electron donors in type I photosynthetic reaction centers, Biochim. Biophys. Acta - Bioenerg., 2001, 1507, 180-193.
    • (2001) Biochim. Biophys. Acta - Bioenerg , vol.1507 , pp. 180-193
    • Breton, J.1
  • 64
    • 71749099514 scopus 로고    scopus 로고
    • Resonance Raman spectroscopy
    • Robert, B. Resonance Raman spectroscopy. Photosynth. Res. 2009, 101, 147-155.
    • (2009) Photosynth. Res , vol.101 , pp. 147-155
    • Robert, B.1
  • 65
    • 33749008562 scopus 로고    scopus 로고
    • Carotenoid interactions in Peridinin Chlorophyll-a Proteins from Dinoflagellates: Evidence for optical excitons and triplet migration
    • Carbonera, D.; Giacometti, G.; Segre, U. Carotenoid interactions in Peridinin Chlorophyll-a Proteins from Dinoflagellates: evidence for optical excitons and triplet migration J. Chem. Soc. Far. Trans., 1996, 92, 989-993.
    • (1996) J. Chem. Soc. Far. Trans , vol.92 , pp. 989-993
    • Carbonera, D.1    Giacometti, G.2    Segre, U.3
  • 66
    • 84884926529 scopus 로고    scopus 로고
    • Low- Temperature Spectroscopic Properties of the Peridinin-Chlorophyll a-Protein (PCP) Complex from the Coral Symbiotic Dinoflagellate
    • Niedzwiedzki, D.M.; Jiang J.; Lo C.S.; Blankenship R.E. Low- Temperature Spectroscopic Properties of the Peridinin-Chlorophyll a-Protein (PCP) Complex from the Coral Symbiotic Dinoflagellate Symbiodinium. J. Phys. Chem. B, 2013, 117, 11091-11099.
    • (2013) Symbiodinium. J. Phys. Chem. B , vol.117 , pp. 11091-11099
    • Niedzwiedzki, D.M.1    Jiang, J.2    Lo, C.S.3    Blankenship, R.E.4
  • 67
    • 0028172054 scopus 로고
    • A novel peridinin-chlorophyll a protein (PCP) from the marine dinoflagellate Alexandrium cohorticula: A high pigment content and plural spectral forms of peridinin and chlorophyll a
    • Ogata, T.; Kodama, M.; Nomura, S.; Kobayashi, M.; Nozawa, T.; Katoh, T.; Mimuro, M. A novel peridinin-chlorophyll a protein (PCP) from the marine dinoflagellate Alexandrium cohorticula: a high pigment content and plural spectral forms of peridinin and chlorophyll a. FEBS Lett., 1994, 356, 367-371.
    • (1994) FEBS Lett , vol.356 , pp. 367-371
    • Ogata, T.1    Kodama, M.2    Nomura, S.3    Kobayashi, M.4    Nozawa, T.5    Katoh, T.6    Mimuro, M.7
  • 69
    • 47749105883 scopus 로고
    • La microspectrométrie Raman de Résonance: Méthode d'investigation in vivo des systèmes pigmentaires
    • Merlin, J.-C. La microspectrométrie Raman de Résonance: méthode d'investigation in vivo des systèmes pigmentaires. Spectrosc. Int. J., 1983, 2, 52-61.
    • (1983) Spectrosc. Int. J , vol.2 , pp. 52-61
    • Merlin, J.-C.1
  • 71
    • 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.; Hiller, R.G. Reconstitution of the peridinin-chlorophyll-a protein (PCP): evidence for functional flexibility in chlorophyll binding. Photosynth. Res., 2005, 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
  • 72
    • 0038298809 scopus 로고    scopus 로고
    • The effect of protein conformational flexibility on the electronic properties of a chromophore
    • Spezia, R.; Aschi, M.; Di Nola, A.; Di Valentin, M.; Carbonera, D.; Amadei, A. The effect of protein conformational flexibility on the electronic properties of a chromophore. Biophys. J., 2003, 84, 2805-2813.
    • (2003) Biophys. J , vol.84 , pp. 2805-2813
    • Spezia, R.1    Aschi, M.2    Di Nola, A.3    Di Valentin, M.4    Carbonera, D.5    Amadei, A.6
  • 73
    • 1042282952 scopus 로고    scopus 로고
    • π-π stacking interactions in the peridinin- chlorophyll-protein of Amphidinium carterae
    • Mao, L.; Wang, Y.; Hu, X. π-π stacking interactions in the peridinin- chlorophyll-protein of Amphidinium carterae. J. Phys. Chem. B, 2003, 107, 3963-3971.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 3963-3971
    • Mao, L.1    Wang, Y.2    Hu, X.3
  • 75
    • 0001114094 scopus 로고    scopus 로고
    • Structure-based calculations of the optical spectra of the ligthharvesting peridin-chlorophyll-protein complexes from Amphydinium carterae and Heterocapsa pygmaea
    • Carbonera D.; Giacometti, G.; Segre, U.; Hofmann, E.; Hiller, R.G. Structure-based calculations of the optical spectra of the ligthharvesting peridin-chlorophyll-protein complexes from Amphydinium carterae and Heterocapsa pygmaea. J. Phys. Chem. B, 1999, 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
  • 78
    • 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.; Mimuro, M. Excitation energy transfer in carotenoid-chlorophyll protein complexes probed by femtosecond fluorescence decays. Chem. Phys. Lett., 1996, 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
  • 79
    • 0033799023 scopus 로고    scopus 로고
    • Excitation transfer in the Peridinin-Chlorophyll-Protein of Amphidinium carterae
    • Damjanovic, A.; Ritz, T.; Schulten, K. Excitation transfer in the Peridinin-Chlorophyll-Protein of Amphidinium carterae. Biophys. J., 2000, 79, 1695-1705.
    • (2000) Biophys. J , vol.79 , pp. 1695-1705
    • Damjanovic, A.1    Ritz, T.2    Schulten, K.3
  • 80
    • 3042812428 scopus 로고    scopus 로고
    • Redox functions of carotenoids in photosynthesis
    • Frank, H.A.; Brudvig, G.W. Redox functions of carotenoids in photosynthesis, Biochemistry, 2004, 43, 8607-8615.
    • (2004) Biochemistry , vol.43 , pp. 8607-8615
    • Frank, H.A.1    Brudvig, G.W.2
  • 82
    • 18244397526 scopus 로고
    • A theory of sensitized luminescence in solids
    • Dexter, D.L.J. A theory of sensitized luminescence in solids. Chem. Phys., 1953, 21, 836-851.
    • (1953) Chem. Phys , vol.21 , pp. 836-851
    • Dexter, D.L.J.1
  • 83
    • 0000875007 scopus 로고
    • A connection between intramolecular long-range electron, hole, and triplet energy transfers
    • Closs G.I.; Johnson, M.D.; Miller, J.R.; Piotrowiak, P. A connection between intramolecular long-range electron, hole, and triplet energy transfers. J. Am. Chem. Soc., 1989, 111, 3751-3753.
    • (1989) J. Am. Chem. Soc , vol.111 , pp. 3751-3753
    • Closs, G.I.1    Johnson, M.D.2    Miller, J.R.3    Piotrowiak, P.4
  • 84
    • 0001672288 scopus 로고
    • Chemical and Electrochemical electron Transfer Theory
    • Marcus, R.A. Chemical and Electrochemical electron Transfer Theory. Ann. Rev. Phys. Chem., 1964, 15, 155-196.
    • (1964) Ann. Rev. Phys. Chem , vol.15 , pp. 155-196
    • Marcus, R.A.1
  • 87
    • 0000992490 scopus 로고
    • A.J. Hoff, Ed.; Elsevier, Amsterdam
    • Hoff, A.J. In: Advanced EPR, A.J. Hoff, Ed.; Elsevier, Amsterdam, 1989; pp. 633-681.
    • (1989) Advanced EPR , pp. 633-681
    • Hoff, A.J.1
  • 88
    • 76149106835 scopus 로고    scopus 로고
    • Optically detected magnetic resonance (ODMR) of photoexcited triplet states
    • Carbonera, D. Optically detected magnetic resonance (ODMR) of photoexcited triplet states Photosynth. Res., 2009, 102, 403-414.
    • (2009) Photosynth. Res , vol.102 , pp. 403-414
    • Carbonera, D.1
  • 89
    • 20444373404 scopus 로고    scopus 로고
    • Quenching of chlorophyll triplet states by carotenoids in reconstituted Lhca4 subunit of peripheral light-harvesting complex of photosystem I
    • Carbonera, D.; Agostini, G.; Morosinotto, T.; Bassi, R. Quenching of chlorophyll triplet states by carotenoids in reconstituted Lhca4 subunit of peripheral light-harvesting complex of photosystem I. Biochemistry, 2005, 44, 8337-8346.
    • (2005) Biochemistry , vol.44 , pp. 8337-8346
    • Carbonera, D.1    Agostini, G.2    Morosinotto, T.3    Bassi, R.4
  • 90
    • 0001398583 scopus 로고
    • Step-scan FT-IR spectroscopy of electron transfer in the photosynthetic bacterial reaction center
    • Burie, J.R.; Leibl, W.; Nabedryk, E.; Breton, J. Step-scan FT-IR spectroscopy of electron transfer in the photosynthetic bacterial reaction center. Appl. Spectr., 1993, 47, 1401-1404.
    • (1993) Appl. Spectr , vol.47 , pp. 1401-1404
    • Burie, J.R.1    Leibl, W.2    Nabedryk, E.3    Breton, J.4
  • 91
    • 0037239339 scopus 로고    scopus 로고
    • Timeresolved step-scan FTIR investigation on the primary donor of the reaction center from the green sulfur bacterium
    • Mezzetti, A.; Seo, D.; Leibl, W.; Sakurai, H.; Breton, J. Timeresolved step-scan FTIR investigation on the primary donor of the reaction center from the green sulfur bacterium Chlorobium tepidum. Photosynth. Res., 2003, 75, 161-169.
    • (2003) Chlorobium Tepidum. Photosynth. Res , vol.75 , pp. 161-169
    • Mezzetti, A.1    Seo, D.2    Leibl, W.3    Sakurai, H.4    Breton, J.5
  • 92
    • 84901978829 scopus 로고    scopus 로고
    • Time-Resolved FTIR Difference Spectroscopy Reveals the Structure and Dynamics of Carotenoid and Chlorophyll Triplets in Photosynthetic Light-Harvesting Complexes, in Infrared Spectroscopy - Life and Biomedical Sciences, Theophanides ed
    • Alexandre, M.; van Grondelle, R. Time-Resolved FTIR Difference Spectroscopy Reveals the Structure and Dynamics of Carotenoid and Chlorophyll Triplets in Photosynthetic Light-Harvesting Complexes, in Infrared Spectroscopy - Life and Biomedical Sciences, Theophanides ed., InTechopen, 2012, pp. 231-256.
    • InTechopen , vol.2012 , pp. 231-256
    • Alexandre, M.1    van Grondelle, R.2
  • 93
    • 81155151831 scopus 로고    scopus 로고
    • Photo-Induced Electron Spin Polarization in Chemical and Biological Reactions: Probing Structure and Dynamics of Transient Intermediates by Multifrequency EPR Spectroscopy
    • Moebius, K.; Lubitz, W.; Savitsky, A. Photo-Induced Electron Spin Polarization in Chemical and Biological Reactions: Probing Structure and Dynamics of Transient Intermediates by Multifrequency EPR Spectroscopy. Appl. Mag. Res., 2011, 41, 113-143.
    • (2011) Appl. Mag. Res , vol.41 , pp. 113-143
    • Moebius, K.1    Lubitz, W.2    Savitsky, A.3
  • 94
    • 0036434363 scopus 로고    scopus 로고
    • Pulse EPR and ENDOR studies of light-induced radicals and triplet states in photosystem II of oxygenic photosynthesis
    • Lubitz, W. Pulse EPR and ENDOR studies of light-induced radicals and triplet states in photosystem II of oxygenic photosynthesis. Phys. Chem. Chem. Phys., 2002, 4, 5539-5545.
    • (2002) Phys. Chem. Chem. Phys , vol.4 , pp. 5539-5545
    • Lubitz, W.1
  • 95
    • 36849115243 scopus 로고
    • Optical Pumping of the Lowest Triplet State and Multiple Resonance Optical Techniques in Zero Field
    • El-Sayed, M.A. Optical Pumping of the Lowest Triplet State and Multiple Resonance Optical Techniques in Zero Field. J. Chem. Phys., 1971, 54, 680-692.
    • (1971) J. Chem. Phys , vol.54 , pp. 680-692
    • El-Sayed, M.A.1
  • 96
    • 49349118432 scopus 로고
    • Energy exchange in a coherently coupled ensemble
    • Brenner H.C.; Brock, J.C.; Harris, C.B. Energy exchange in a coherently coupled ensemble. Chem. Phys., 1978, 31, 137-164.
    • (1978) Chem. Phys , vol.31 , pp. 137-164
    • Brenner, H.C.1    Brock, J.C.2    Harris, C.B.3
  • 97
    • 80855139863 scopus 로고    scopus 로고
    • Conservation of Spin Polarization during Triplet-Triplet Energy Transfer in Reconstituted Peridinin- Chlorophyll-Protein Complexes
    • Di Valentin M.; Tait, C.; Salvadori, E.; Ceola, S.; Scheer, H.; Hiller, R.G.; Carbonera, D. Conservation of Spin Polarization during Triplet-Triplet Energy Transfer in Reconstituted Peridinin- Chlorophyll-Protein Complexes. J. Phys. Chem. B, 2011, 115, 13371-13380.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 13371-13380
    • Di Valentin, M.1    Tait, C.2    Salvadori, E.3    Ceola, S.4    Scheer, H.5    Hiller, R.G.6    Carbonera, D.7
  • 98
    • 38549111025 scopus 로고    scopus 로고
    • Identification by time-resolved EPR of the peridinins directly involved in chlorophyll triplet quenching in the peridininchlorophyll a-protein from Amphidinium carterae
    • Di Valentin, M.; Ceola, S.; Salvadori, E.; Agostini G.; Carbonera, D. Identification by time-resolved EPR of the peridinins directly involved in chlorophyll triplet quenching in the peridininchlorophyll a-protein from Amphidinium carterae. Biochim. Biophys. Acta - Bioenerg., 2008, 1777, 186-195.
    • (2008) Biochim. Biophys. Acta - Bioenerg , vol.1777 , pp. 186-195
    • Di Valentin, M.1    Ceola, S.2    Salvadori, E.3    Agostini, G.4    Carbonera, D.5
  • 100
    • 0000949148 scopus 로고
    • The orientation of the triplet axes with respect to the optical transition moments in (bacterio) chlorophylls
    • Vrieze J.; Hoff, A.J. The orientation of the triplet axes with respect to the optical transition moments in (bacterio) chlorophylls. Chem. Phys. Lett., 1995, 237, 493-501.
    • (1995) Chem. Phys. Lett , vol.237 , pp. 493-501
    • Vrieze, J.1    Hoff, A.J.2
  • 101
    • 0011246662 scopus 로고
    • First detection of the (nonphosphorescent) triplet state in single crystals of α- carotene
    • Frick, J.; Von Schutz, J.U.; Wolf, H.C.; Kothe, G. First detection of the (nonphosphorescent) triplet state in single crystals of α- carotene. Mol. Liq. Cryst. Liq. Cryst., 1990, 183, 269-272.
    • (1990) Mol. Liq. Cryst. Liq. Cryst , vol.183 , pp. 269-272
    • Frick, J.1    von Schutz, J.U.2    Wolf, H.C.3    Kothe, G.4
  • 102
    • 71149110868 scopus 로고    scopus 로고
    • Pulsed EPR and ENDOR on the Peridinin Triplet State Involved in the Photoprotective Mechanism in Peridinin-Chlorophyll a-Proteins
    • Di Valentin, M.; Salvadori, E.; Ceola, S.; Carbonera, D. Pulsed EPR and ENDOR on the Peridinin Triplet State Involved in the Photoprotective Mechanism in Peridinin-Chlorophyll a-Proteins. Appl. Mag. Res., 2010, 37, 191-205.
    • (2010) Appl. Mag. Res , vol.37 , pp. 191-205
    • Di Valentin, M.1    Salvadori, E.2    Ceola, S.3    Carbonera, D.4
  • 103
    • 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 aprotein from Amphidinium carterae
    • Di Valentin M., Ceola, S.; Agostini, G.; Giacometti, G.M.; Angerhofer, A.; Crescenzo, O.; Barone, V.; Carbonera, D. Pulse ENDOR and density functional theory on the peridinin triplet state involved in the photo-protective mechanism in the peridinin-chlorophyll aprotein from Amphidinium carterae. Biochim. Biophys. Acta - Bioenerg., 2008, 1777, 295-307.
    • (2008) Biochim. Biophys. Acta - Bioenerg , vol.1777 , pp. 295-307
    • Di Valentin, M.1    Ceola, S.2    Agostini, G.3    Giacometti, G.M.4    Angerhofer, A.5    Crescenzo, O.6    Barone, V.7    Carbonera, D.8
  • 104
    • 84884568582 scopus 로고    scopus 로고
    • Evidence for water-mediated triplet-triplet energy transfer in the photoprotective site of the peridinin-chlorophyll a- protein
    • Di Valentin, M.; Tait, C.E.; Salvadori, E.; Orian, L.; Polimeno, A.; Carbonera, D. Evidence for water-mediated triplet-triplet energy transfer in the photoprotective site of the peridinin-chlorophyll a- protein. Biochim. Biophys. Acta - Bioenerg., 2014, 1837, 85-97.
    • (2014) Biochim. Biophys. Acta - Bioenerg , vol.1837 , pp. 85-97
    • Di Valentin, M.1    Tait, C.E.2    Salvadori, E.3    Orian, L.4    Polimeno, A.5    Carbonera, D.6
  • 105
    • 0029352293 scopus 로고
    • A time-resolved Electron Nuclear Double Resonance (ENDOR) study of the photoexcited triplet state of free-base tetraphenylporphyrin
    • Kay, C.W.M.; Di Valentin, M.; Mobius, K. A time-resolved Electron Nuclear Double Resonance (ENDOR) study of the photoexcited triplet state of free-base tetraphenylporphyrin. Sol. Energy Mater. Sol. Cells, 1995, 38, 111-118.
    • (1995) Sol. Energy Mater. Sol. Cells , vol.38 , pp. 111-118
    • Kay, C.W.M.1    Di Valentin, M.2    Mobius, K.3
  • 106
    • 0002983023 scopus 로고    scopus 로고
    • Time-resolved EPR and ENDOR study of the photoexcited triplet state of free-base tetraphenylchlorin in a crystalline toluene matrix
    • Kay, C.W.M.; Di Valentin, M.; Mobius, K. Time-resolved EPR and ENDOR study of the photoexcited triplet state of free-base tetraphenylchlorin in a crystalline toluene matrix. J. Chem. Soc. Perkin Trans. II, 1997, 12, 2563-2568.
    • (1997) J. Chem. Soc. Perkin Trans. II , vol.12 , pp. 2563-2568
    • Kay, C.W.M.1    Di Valentin, M.2    Mobius, K.3
  • 107
    • 0035921516 scopus 로고    scopus 로고
    • An investigation of the structure of free-base porphycene by time-resolved electron nuclear double resonance and density functional theory on the photoexcited triplet state
    • Kay, C.W.M.; Gromadecki, U.; Törring, J.T.; Weber, S. An investigation of the structure of free-base porphycene by time-resolved electron nuclear double resonance and density functional theory on the photoexcited triplet state. Mol. Phys., 2001, 99, 1413-1420.
    • (2001) Mol. Phys , vol.99 , pp. 1413-1420
    • Kay, C.W.M.1    Gromadecki, U.2    Törring, J.T.3    Weber, S.4
  • 108
    • 67650079218 scopus 로고    scopus 로고
    • Spin Density Distribution of the Excited Triplet State of Bacteriochlorophylls. Pulsed ENDOR and DFT Studies
    • Marchanka, A.; Lubitz, W.; van Gastel, M. Spin Density Distribution of the Excited Triplet State of Bacteriochlorophylls. Pulsed ENDOR and DFT Studies. J. Phys. Chem. B, 2009, 113, 6917-6927.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 6917-6927
    • Marchanka, A.1    Lubitz, W.2    van Gastel, M.3
  • 109
    • 0030593002 scopus 로고    scopus 로고
    • A time resolved Electron Nuclear Double Resonance study of the Photoexcited Triplet State of P680 in Isolated Reaction Centers of Photosystem II
    • Di Valentin, M.; Kay, C.W.M.; Giacometti, G.; Mobius, K. A time resolved Electron Nuclear Double Resonance study of the Photoexcited Triplet State of P680 in Isolated Reaction Centers of Photosystem II. Chem. Phys.Lett., 1996, 248, 434-441.
    • (1996) Chem. Phys.Lett , vol.248 , pp. 434-441
    • Di Valentin, M.1    Kay, C.W.M.2    Giacometti, G.3    Mobius, K.4
  • 110
    • 0031855897 scopus 로고    scopus 로고
    • Pulsed ENDOR of the Photo- Excited Triplet States of Bacteriochlorophyll a and of the Primary Donor P865 in Reaction Centers of Rhodobacter sphaeroides R-26
    • Lendzian, F.; Bittl R.; Lubitz, W. Pulsed ENDOR of the Photo- Excited Triplet States of Bacteriochlorophyll a and of the Primary Donor P865 in Reaction Centers of Rhodobacter sphaeroides R-26. Photosynth. Res., 1998, 55, 189-197.
    • (1998) Photosynth. Res , vol.55 , pp. 189-197
    • Lendzian, F.1    Bittl, R.2    Lubitz, W.3
  • 111
    • 0041592754 scopus 로고    scopus 로고
    • Hyperfine Structure of the Photoexcited Triplet State 3P680 in Plant PS II Reaction Centers as Determined by Pulse ENDOR
    • Lendzian, F.; Bittl, R.; Telfer A.; Lubitz, W. Hyperfine Structure of the Photoexcited Triplet State 3P680 in Plant PS II Reaction Centers as Determined by Pulse ENDOR. Biochim. Biophys. Acta, - Bioenerg., 2003, 1605, 35-46.
    • (2003) Biochim. Biophys. Acta, - Bioenerg , vol.1605 , pp. 35-46
    • Lendzian, F.1    Bittl, R.2    Telfer, A.3    Lubitz, W.4
  • 112
    • 33846372156 scopus 로고    scopus 로고
    • B. Gilbert, M. Davies, D. Murphy, Ed.: Royal Society of Chemistry, Cambdrige, U.K
    • Lubitz, W. In: Electron Paramagnetic Resonance. A specialist periodical report. B. Gilbert, M. Davies, D. Murphy, Ed.: Royal Society of Chemistry, Cambdrige, U.K., 2004, Vol. 19, 5, pp. 174-242.
    • (2004) Electron Paramagnetic Resonance. a Specialist Periodical Report , vol.19 , Issue.5 , pp. 174-242
    • Lubitz, W.1
  • 113
    • 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.; Schulte, T.; Prakash, S.; van Gastel, M.; Hofmann E.; Lubitz, W. 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., 2007, 129, 15442-15443.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 15442-15443
    • Niklas, J.1    Schulte, T.2    Prakash, S.3    van Gastel, M.4    Hofmann, E.5    Lubitz, W.6
  • 114
    • 0040166422 scopus 로고    scopus 로고
    • Error and Artifacts in time-resolved step-scan FT-IR spectroscopy
    • Rodig, C.; Siebert, F. Error and Artifacts in time-resolved step-scan FT-IR spectroscopy. Appl. Spectr. 1999, 53, 893-90.
    • (1999) Appl. Spectr , vol.53 , pp. 893-990
    • Rodig, C.1    Siebert, F.2
  • 115
    • 19144363364 scopus 로고    scopus 로고
    • Instrumental aspects of time-resolved spectra generated using step-scan interferometers
    • Chandlers J.M.; Griffiths P.R. Eds, Wiley
    • Rodig C.; Siebert F. Instrumental aspects of time-resolved spectra generated using step-scan interferometers, in Handbook of Vibrational Spectroscopy, Vol. 1, Chandlers J.M.; Griffiths P.R. Eds, Wiley, 2002, pp. 641-654.
    • (2002) Handbook of Vibrational Spectroscopy , vol.1 , pp. 641-654
    • Rodig, C.1    Siebert, F.2
  • 116
    • 26844494619 scopus 로고    scopus 로고
    • Temperature effects of excitation laser pulses during step-scan FT-IR experiments
    • Rodig, C.; Georg, H.; Siebert, F.; Rousso, I.; Sheves, M. Temperature effects of excitation laser pulses during step-scan FT-IR experiments, Laser Chem., 1999, 19, 169-172.
    • (1999) Laser Chem , vol.19 , pp. 169-172
    • Rodig, C.1    Georg, H.2    Siebert, F.3    Rousso, I.4    Sheves, M.5
  • 117
    • 0031213137 scopus 로고    scopus 로고
    • Noise Sources in step-scan FT-IR spectrometry
    • Manning, C.J.; Griffiths P.R. Noise Sources in step-scan FT-IR spectrometry, Appl. Spectr. 1997, 51, 1092-1101.
    • (1997) Appl. Spectr , vol.51 , pp. 1092-1101
    • Manning, C.J.1    Griffiths, P.R.2
  • 118
    • 72149119691 scopus 로고    scopus 로고
    • Fourier transform infrared (FTIR) spectroscopy
    • Berthomieu, C.; Hienerwadel, R. Fourier transform infrared (FTIR) spectroscopy. Photosynth. Res. 2009 101, 157-170.
    • (2009) Photosynth. Res , vol.101 , pp. 157-170
    • Berthomieu, C.1    Hienerwadel, R.2
  • 119
    • 0000611288 scopus 로고
    • SoT1 infrared difference spectrum of the triplet state of the primary electron donor in Rb. sphaeroides photo synthetic bacterial reaction centers
    • Breton, J.; Nabedryk, E. SoT1 infrared difference spectrum of the triplet state of the primary electron donor in Rb. sphaeroides photo synthetic bacterial reaction centers. Chem. Phys. Lett., 1993, 213, 571-575.
    • (1993) Hem. Phys. Lett. , vol.13 , pp. 571-575
    • Breton, J.1    Nabedryk, E.2
  • 120
    • 0034673379 scopus 로고    scopus 로고
    • Peridinin as the major biological crotenoid quencher of singlet oxygen in marinae algae Gonyaulax Polyedra
    • Pinto, E.; Catalani, L.H.; Peporine Lopes N.; Di Mascio, P.; Colepicolo, P.; Peridinin as the major biological crotenoid quencher of singlet oxygen in marinae algae Gonyaulax Polyedra. Biochim. Biophys. Res. Comm., 2000, 268, 496-500.
    • (2000) Biochim. Biophys. Res. Comm , vol.268 , pp. 496-500
    • Pinto, E.1    Catalani, L.H.2    Peporine, L.N.3    Di Mascio, P.4    Colepicolo, P.5
  • 121
    • 0040313551 scopus 로고    scopus 로고
    • FTIR study of the primary electron donor of photosystem I (P700) revealing delocalization of the charge in P700(+) and and localization of the triplet state in 3P700
    • Breton, J.; Nabedryk, E.; Leibl, W. FTIR study of the primary electron donor of photosystem I (P700) revealing delocalization of the charge in P700(+) and and localization of the triplet state in 3P700. Biochemistry, 1999, 38, 11585-11592.
    • (1999) Biochemistry , vol.38 , pp. 11585-11592
    • Breton, J.1    Nabedryk, E.2    Leibl, W.3
  • 122
    • 13544256286 scopus 로고    scopus 로고
    • A1 reduction in intact cyanobacterial photosystem I particles studied by time-resolved stepscan Fourier transform infrared difference spectroscopy and isotope labeling
    • Sivakumar, V.; Wang, R.; Hastings, G. A1 reduction in intact cyanobacterial photosystem I particles studied by time-resolved stepscan Fourier transform infrared difference spectroscopy and isotope labeling. Biochemistry, 2005, 44, 1880-1893.
    • (2005) Biochemistry , vol.44 , pp. 1880-1893
    • Sivakumar, V.1    Wang, R.2    Hastings, G.3
  • 123
    • 66349101350 scopus 로고    scopus 로고
    • Monitoring and interpretation of photoinduced biochemical processes by rapid-scan FTIR difference spectroscopy and hybrid hard and soft modeling
    • Blanchet, L.; Ruckebusch, C.; Mezzetti, A.; Huvenne, J.P.; De Juan, A. Monitoring and interpretation of photoinduced biochemical processes by rapid-scan FTIR difference spectroscopy and hybrid hard and soft modeling. J. Phys. Chem. B, 2009, 113, 6031-6040.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 6031-6040
    • Blanchet, L.1    Ruckebusch, C.2    Mezzetti, A.3    Huvenne, J.P.4    de Juan, A.5
  • 124
    • 79951720962 scopus 로고    scopus 로고
    • Ubiquinol formation in isolated photosynthetic reaction centres monitored by time-resolved differential FTIR in combination with 2D correlation spectroscopy and multivariate curve resolution
    • Mezzetti, A.; Blanchet, L.; De Juan, A.; Leibl, W.; Ruckebusch, C. Ubiquinol formation in isolated photosynthetic reaction centres monitored by time-resolved differential FTIR in combination with 2D correlation spectroscopy and multivariate curve resolution, Anal. Bioanal. Chem., 2011, 399, 1999-2014.
    • (2011) Anal. Bioanal. Chem , vol.399 , pp. 1999-2014
    • Mezzetti, A.1    Blanchet, L.2    de Juan, A.3    Leibl, W.4    Ruckebusch, C.5
  • 127
    • 5644303218 scopus 로고
    • Intramolecular Charge Transfer in Aromatic Free Radicals
    • McConnell, H.M. Intramolecular Charge Transfer in Aromatic Free Radicals. J. Chem. Phys., 1961, 35, 508-515.
    • (1961) J. Chem. Phys , vol.35 , pp. 508-515
    • McConnell, H.M.1
  • 128
    • 0034350315 scopus 로고    scopus 로고
    • Electron spin echo envelope modulation (ESEEM) spectroscopy as a tool to investigate the coordination environment of metal centers
    • Deligiannakis, Y.; Louloudi, M.; Hadjiliadis, N. Electron spin echo envelope modulation (ESEEM) spectroscopy as a tool to investigate the coordination environment of metal centers. Coord. Chem. Rev., 2000, 204, 1-112.
    • (2000) Coord. Chem. Rev , vol.204 , pp. 1-112
    • Deligiannakis, Y.1    Louloudi, M.2    Hadjiliadis, N.3
  • 129
    • 0003143742 scopus 로고
    • Electron spin echo spectroscopy of organic triplets
    • Lin, T.S. Electron spin echo spectroscopy of organic triplets. Chem. Rev., 1984, 84, 1-15.
    • (1984) Chem. Rev , vol.84 , pp. 1-15
    • Lin, T.S.1
  • 130
    • 66449116600 scopus 로고    scopus 로고
    • The electronic couplings in electron transfer and excitation energy transfer
    • Hsu, C.P. The electronic couplings in electron transfer and excitation energy transfer. Acc. Chem. Res., 2009, 42, 509-518.
    • (2009) Acc. Chem. Res , vol.42 , pp. 509-518
    • Hsu, C.P.1
  • 131
    • 79955456257 scopus 로고    scopus 로고
    • Ab Inito Study on Triplet Excitation Energy Transfer in Photosynthetic Light-Harvesting Complexes
    • You, Z.Q.; Hsu, C.P. Ab Inito Study on Triplet Excitation Energy Transfer in Photosynthetic Light-Harvesting Complexes. J. Phys. Chem. A., 2011, 115, 4092-4100.
    • (2011) J. Phys. Chem. A , vol.115 , pp. 4092-4100
    • You, Z.Q.1    Hsu, C.P.2
  • 133
    • 84860391045 scopus 로고    scopus 로고
    • Absorption enhancement in Peridinin-Chlorophyll-Protein light-harvesting complexes coupled to seemicontinuous Silver Film
    • Czechowski, N.; Nyga, P.; Schmidt, M.; Brotosudarmo, T.; Scheer, H.; Piatkowski, D.; Mackowski, S. Absorption enhancement in Peridinin-Chlorophyll-Protein light-harvesting complexes coupled to seemicontinuous Silver Film. Plasmonics, 2012, 7, 115-121.
    • (2012) Plasmonics , vol.7 , pp. 115-121
    • Czechowski, N.1    Nyga, P.2    Schmidt, M.3    Brotosudarmo, T.4    Scheer, H.5    Piatkowski, D.6    Mackowski, S.7
  • 137
    • 77951591155 scopus 로고    scopus 로고
    • Hybrid nanostructures for efficient light harvesting
    • Mackowski, S. Hybrid nanostructures for efficient light harvesting, J. Phys. Condens. Matter, 2010, 22, 193102.
    • (2010) J. Phys. Condens. Matter , vol.22 , pp. 193102
    • Mackowski, S.1
  • 138
    • 84904459966 scopus 로고    scopus 로고
    • Metallic nanoparticles coupled with photosynthetic complexes
    • Hashim A. (ed), Intechopen
    • Mackowski, S. Metallic nanoparticles coupled with photosynthetic complexes, in Smart Nanoparticles Technology, Hashim A. (ed), Intechopen, 2012, pp. 3-28.
    • (2012) Smart Nanoparticles Technology , pp. 3-28
    • Mackowski, S.1
  • 139
    • 84884263949 scopus 로고    scopus 로고
    • Plasmoncontrolled light-harvesting: Design rules for biohybrid devices via multiscale modeling
    • Andreussi, O.; Biancardi, A.; Corni, S.; Mennucci, B. Plasmoncontrolled light-harvesting: design rules for biohybrid devices via multiscale modeling, Nano Lett., 2013, 13, 4475-4484.
    • (2013) Nano Lett , vol.13 , pp. 4475-4484
    • Andreussi, O.1    Biancardi, A.2    Corni, S.3    Mennucci, B.4
  • 140
    • 0032510091 scopus 로고    scopus 로고
    • Fucoxanthin - and Peridinin - Pheophorbidea molecules as a new light-harvesting model
    • Osuka, A.; Kume, T. Fucoxanthin - and Peridinin - Pheophorbidea molecules as a new light-harvesting model. Tetrahedron Lett., 1998, 39, 655-658.
    • (1998) Tetrahedron Lett , vol.39 , pp. 655-658
    • Osuka, A.1    Kume, T.2
  • 141
    • 0000940394 scopus 로고    scopus 로고
    • Photophysuical characteristics of two antenna systems: A Fucoxanthin -Pheophorbide dyad and its peridinin analogue
    • Osuka, A.; Kume, T.; Haggquist, G.W.; Javorfi, T.; Lima J.C.; Eurico, M.; Razi Naqvi, K. Photophysuical characteristics of two antenna systems: a Fucoxanthin -Pheophorbide dyad and its peridinin analogue, Chem. Phys. Lett., 1999, 313, 499-504.
    • (1999) Chem. Phys. Lett , vol.313 , pp. 499-504
    • Osuka, A.1    Kume, T.2    Haggquist, G.W.3    Javorfi, T.4    Lima, J.C.5    Eurico, M.6    Razi, N.K.7
  • 142
    • 33847659747 scopus 로고    scopus 로고
    • polarity-tuned Energy transfer efficiency in artificial light-harbvestig antenna containing carbonyl carotenoids peridinin and fucoxanthin
    • Polivka, T.; Pellnor, M.; Melo, E.; Pascher, T.; Sundstrom, V.; Osuka, A.; Razi Naqvi, K. polarity-tuned Energy transfer efficiency in artificial light-harbvestig antenna containing carbonyl carotenoids peridinin and fucoxanthin. J. Phys. Chem. C, 2007, 111, 467-476.
    • (2007) J. Phys. Chem. C , vol.111 , pp. 467-476
    • Polivka, T.1    Pellnor, M.2    Melo, E.3    Pascher, T.4    Sundstrom, V.5    Osuka, A.6    Razi, N.K.7
  • 144
    • 0025830889 scopus 로고
    • Detection of Lymphocyte substes using Three-Color/Single Laser flow cytometry and the fluorescent dye Peridinin-Chlorophyll-a-Protein
    • Afar, B.; Merrill, J.; Clark, E.A. Detection of Lymphocyte substes using Three-Color/Single Laser flow cytometry and the fluorescent dye Peridinin-Chlorophyll-a-Protein, J. Clin. Immunol., 1991, 11, 254-261.
    • (1991) J. Clin. Immunol , vol.11 , pp. 254-261
    • Afar, B.1    Merrill, J.2    Clark, E.A.3
  • 145
    • 0030017124 scopus 로고    scopus 로고
    • A strategy for multiple immunophenotyping by image cytometry: Model studies using latex microbeads labeled with seven streptavidin-bound fluorochromes
    • Gothot, A.; Grosdent, J.C.; Paulus, J.M. A strategy for multiple immunophenotyping by image cytometry: model studies using latex microbeads labeled with seven streptavidin-bound fluorochromes. Cytometry, 1996, 24, 214-225.
    • (1996) Cytometry , vol.24 , pp. 214-225
    • Gothot, A.1    Grosdent, J.C.2    Paulus, J.M.3
  • 146
    • 34250797484 scopus 로고    scopus 로고
    • Halocynthiaxanhin and peridinin sensitize colon cancer cells to tumor necrosisfactor- related apoptosis-inducing ligand
    • Yoshida, T.; Maoka, T.; Das, S.K.; Kanazawa, K.; Horinaka, M.; Wakada, M.; Satomi, H.; Nishiçno, H.; Sakai, T. Halocynthiaxanhin and peridinin sensitize colon cancer cells to tumor necrosisfactor- related apoptosis-inducing ligand. Mol. Cancer Res., 2007, 5, 615-625.
    • (2007) Mol. Cancer Res , vol.5 , pp. 615-625
    • Yoshida, T.1    Maoka, T.2    Das, S.K.3    Kanazawa, K.4    Horinaka, M.5    Wakada, M.6    Satomi, H.7    Nishiçno, H.8    Sakai, T.9


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