메뉴 건너뛰기




Volumn 22, Issue 4, 2008, Pages 235-250

Time-resolved step scan FTIR spectroscopy and DFT investigation on triplet formation in peridinin-chlorophyll-a-protein from Amphidinium carterae at low temperature

Author keywords

DFT; Peridinin; Peridinin chlorophyll a protein; Step scan FTIR; Triplet state

Indexed keywords

CHLOROPHYLL; DENSITY FUNCTIONAL THEORY; FOURIER TRANSFORM INFRARED SPECTROSCOPY; TEMPERATURE;

EID: 47749097223     PISSN: 07124813     EISSN: None     Source Type: Journal    
DOI: 10.1155/2008/682046     Document Type: Article
Times cited : (23)

References (70)
  • 2
    • 0017107168 scopus 로고
    • Molecular topology of photosynthetic light-harvesting pigment complex, peridinin-chlorophyll-a-protein, from marine dinoflagellates
    • P.-S. Song, P. Koka, B.B. Prezelin and F.T. Haxo, Molecular topology of photosynthetic light-harvesting pigment complex, peridinin-chlorophyll-a-protein, from marine dinoflagellates, Biochemistry 15 (1976), 4422-4427.
    • (1976) Biochemistry , vol.15 , pp. 4422-4427
    • Song, P.-S.1    Koka, P.2    Prezelin, B.B.3    Haxo, F.T.4
  • 3
    • 0017697816 scopus 로고
    • The chromophore topography and binding environment of peridinin-chlorophyll a-protein complexes from marine dinoflagellate algae
    • P. Koka and P.-S. Song, The chromophore topography and binding environment of peridinin-chlorophyll a-protein complexes from marine dinoflagellate algae, Biochim. Biophys. Acta - General Subjects 495 (1977), 220-231.
    • (1977) Biochim. Biophys. Acta - General Subjects , vol.495 , pp. 220-231
    • Koka, P.1    Song, P.-S.2
  • 4
    • 0000402734 scopus 로고    scopus 로고
    • The electronic states of carotenoids
    • H.A. Frank, A.J. Young, M. Braun and R.J. Cogdell, eds, Kluwer, Dordrecht, The Netherlands
    • R.L. Christensen, The electronic states of carotenoids, in: The Photochemistry of Carotenoids, H.A. Frank, A.J. Young, M. Braun and R.J. Cogdell, eds, Kluwer, Dordrecht, The Netherlands, 1999, pp. 137-159.
    • (1999) The Photochemistry of Carotenoids , pp. 137-159
    • Christensen, R.L.1
  • 5
    • 85184381148 scopus 로고    scopus 로고
    • B.E. Kohler, Electronic structure of carotenoids, in: Carotenoids, 1B, Spectroscopy, G. Britton, S. Liaaen-Jensen and H. Pfanden, eds, Birkhäuser-Verlag, Basel, 1995, pp. 1-12.
    • B.E. Kohler, Electronic structure of carotenoids, in: Carotenoids, Vol. 1B, Spectroscopy, G. Britton, S. Liaaen-Jensen and H. Pfanden, eds, Birkhäuser-Verlag, Basel, 1995, pp. 1-12.
  • 6
    • 0001001551 scopus 로고    scopus 로고
    • Singlet and triplet energy transfer in the peridinin-chlorophyll a protein from Amphidinium carterae
    • J.A. Bautista, R.G. Hiller, F.P. Sharples, D. Gosztola, M. Wasielewski and H.A. Frank, Singlet and triplet energy transfer in the peridinin-chlorophyll a protein from Amphidinium carterae, J. Phys. Chem. A 103 (1999), 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
  • 10
    • 0035731519 scopus 로고    scopus 로고
    • Carotenoids and bacterial photosynthesis: The story so far. .
    • N.J. Fraser, H. Hashimoto and R.J. Cogdell, Carotenoids and bacterial photosynthesis: The story so far. . . , Photosynth. Res. 70 (2001), 249-256.
    • (2001) Photosynth. Res , vol.70 , pp. 249-256
    • Fraser, N.J.1    Hashimoto, H.2    Cogdell, R.J.3
  • 11
    • 0030095112 scopus 로고    scopus 로고
    • Carotenoids 3: In vivo function of carotenoids in higher plants
    • B. Demmig-Adams, A.M. Gilmore and W.W. Adams 3rd, Carotenoids 3: in vivo function of carotenoids in higher plants, FASEB J. 10 (1996), 403-412.
    • (1996) FASEB J , vol.10 , pp. 403-412
    • Demmig-Adams, B.1    Gilmore, A.M.2    Adams 3rd, W.W.3
  • 12
    • 16344371211 scopus 로고    scopus 로고
    • Isoprenoids: An evolutionary pool for photoprotection
    • J. Penuelas and S. Munne-Bosch, Isoprenoids: an evolutionary pool for photoprotection, Trends Plant Sci. 10 (2005), 166-169.
    • (2005) Trends Plant Sci , vol.10 , pp. 166-169
    • Penuelas, J.1    Munne-Bosch, S.2
  • 14
    • 0014963512 scopus 로고
    • Chemistry of singlet oxygen. X. Carotenoid quenching parallels biological protection
    • C.S. Foote, Y.C. Chang and R.W. Denny, Chemistry of singlet oxygen. X. Carotenoid quenching parallels biological protection, J. Am. Chem. Soc. 92 (1970), 5216-5218.
    • (1970) J. Am. Chem. Soc , vol.92 , pp. 5216-5218
    • Foote, C.S.1    Chang, Y.C.2    Denny, R.W.3
  • 15
    • 35848956087 scopus 로고    scopus 로고
    • Carotenoids and flavonoids contribute to nutritional protection against skin damage from sunlight
    • W. Stahl and H. Sies, Carotenoids and flavonoids contribute to nutritional protection against skin damage from sunlight, Mol. Biotech. 37 (2007), 26-30.
    • (2007) Mol. Biotech , vol.37 , pp. 26-30
    • Stahl, W.1    Sies, H.2
  • 16
    • 0036277679 scopus 로고    scopus 로고
    • Systemic photoprotection with alpha-tocopherol (vitamin E) and beta-carotene
    • A.V. Anstey, Systemic photoprotection with alpha-tocopherol (vitamin E) and beta-carotene, Clin. Exp. Dermatol. 27 (2002), 170-176.
    • (2002) Clin. Exp. Dermatol , vol.27 , pp. 170-176
    • Anstey, A.V.1
  • 17
    • 0142216401 scopus 로고    scopus 로고
    • Antioxidant activity of carotenoids
    • W. Stahl and H. Sies, Antioxidant activity of carotenoids, Mol. Aspects Med. 24 (2003), 345-351.
    • (2003) Mol. Aspects Med , vol.24 , pp. 345-351
    • Stahl, W.1    Sies, H.2
  • 18
    • 0032543363 scopus 로고    scopus 로고
    • Cancer prevention by carotenoids
    • H. Nishino, Cancer prevention by carotenoids, Mutation Res. 402 (1998), 159-163.
    • (1998) Mutation Res , vol.402 , pp. 159-163
    • Nishino, H.1
  • 20
    • 0037168673 scopus 로고    scopus 로고
    • Carotenoid to chlorophyll energy transfer in the peridinin-chlorophylla-protein complex involves an intramolecular charge transfer state
    • D. Zigmantas, R.G. Hiller, V. Sundström and T. Polivka, Carotenoid to chlorophyll energy transfer in the peridinin-chlorophylla-protein complex involves an intramolecular charge transfer state, Proc. Natl. Acad. Sci. USA 99 (2002), 16760-16765.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16760-16765
    • Zigmantas, D.1    Hiller, R.G.2    Sundström, V.3    Polivka, T.4
  • 22
    • 0038613232 scopus 로고    scopus 로고
    • Model for triplet-triplet energy transfer in natural clusters of Peridinin molecules contained in Dinoflagellate's Outer antenna proteins
    • D. Carbonera, G. Giacometti, U. Segre, A. Angerhofer and U. Gross, Model for triplet-triplet energy transfer in natural clusters of Peridinin molecules contained in Dinoflagellate's Outer antenna proteins, J. Phys. Chem. B 103 (1999), 6357-6362.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 6357-6362
    • Carbonera, D.1    Giacometti, G.2    Segre, U.3    Angerhofer, A.4    Gross, U.5
  • 23
    • 34249903331 scopus 로고    scopus 로고
    • The unusually strong hydrogen bond between the carbonyl of Q(A) and His M219 in the Rhodobacter sphaeroides reaction center is not essential for efficient electron transfer from Q(A) (-) to Q(B)
    • J. Breton, J. Lavergne, M.C. Wakeham, E. Nabedryk and M.R. Jones, The unusually strong hydrogen bond between the carbonyl of Q(A) and His M219 in the Rhodobacter sphaeroides reaction center is not essential for efficient electron transfer from Q(A) (-) to Q(B), Biochemistry 46 (2007), 6468-6476.
    • (2007) Biochemistry , vol.46 , pp. 6468-6476
    • Breton, J.1    Lavergne, J.2    Wakeham, M.C.3    Nabedryk, E.4    Jones, M.R.5
  • 24
    • 0035976019 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy of primary electron donors in type I photosynthetic reaction centers
    • J. Breton, Fourier transform infrared spectroscopy of primary electron donors in type I photosynthetic reaction centers, Biochim. Biophys. Acta - Bioenergetics 1507 (2001), 180-193.
    • (2001) Biochim. Biophys. Acta - Bioenergetics , vol.1507 , pp. 180-193
    • Breton, J.1
  • 25
    • 0041622652 scopus 로고    scopus 로고
    • Coupling of light-induced electron transfer to proton uptake in photosynthesis
    • A. Remy and K. Gerwert, Coupling of light-induced electron transfer to proton uptake in photosynthesis, Nat. Struct. Biol. 10 (2003), 637-644.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 637-644
    • Remy, A.1    Gerwert, K.2
  • 26
    • 33947539623 scopus 로고    scopus 로고
    • Light-induced FTIR difference spectroscopy as a powerful tool toward understanding the molecular mechanism of photosynthetic oxygen evolution
    • T. Noguchi, Light-induced FTIR difference spectroscopy as a powerful tool toward understanding the molecular mechanism of photosynthetic oxygen evolution, Photosynth. Res. 91 (2007), 59-69.
    • (2007) Photosynth. Res , vol.91 , pp. 59-69
    • Noguchi, T.1
  • 28
    • 0041322848 scopus 로고    scopus 로고
    • Light-induced changes in the chemical bond structure of light-harvesting complex II probed by FTIR spectroscopy
    • H. Rogl, W. Kühlbrandt and A. Barth, Light-induced changes in the chemical bond structure of light-harvesting complex II probed by FTIR spectroscopy, Biochemistry 42 (2003), 10223-10228.
    • (2003) Biochemistry , vol.42 , pp. 10223-10228
    • Rogl, H.1    Kühlbrandt, W.2    Barth, A.3
  • 30
    • 0037239339 scopus 로고    scopus 로고
    • Time-resolved step-scan FTIR investigation on the primary donor of the reaction center from the green sulfur bacterium Chlorobium tepidum
    • A. Mezzetti, D. Seo, W. Leibl, H. Sakurai and J. Breton, Time-resolved step-scan FTIR investigation on the primary donor of the reaction center from the green sulfur bacterium Chlorobium tepidum, Photosynth. Res. 75 (2003), 161-169.
    • (2003) Photosynth. Res , vol.75 , pp. 161-169
    • Mezzetti, A.1    Seo, D.2    Leibl, W.3    Sakurai, H.4    Breton, J.5
  • 31
    • 0035916249 scopus 로고    scopus 로고
    • Triplet formation on a monomeric chlorophyll in the photosystem II reaction center as studied by time-resolved infrared spectroscopy
    • T. Noguchi, T. Tatsuya and K. Chihiro, Triplet formation on a monomeric chlorophyll in the photosystem II reaction center as studied by time-resolved infrared spectroscopy, Biochemistry 40 (2001), 2176-2185.
    • (2001) Biochemistry , vol.40 , pp. 2176-2185
    • Noguchi, T.1    Tatsuya, T.2    Chihiro, K.3
  • 32
    • 0002859824 scopus 로고    scopus 로고
    • Light-induced Fourier trasform infrared difference spectroscopy of the primary electron donor in photosynthetic reaction centers
    • H.H. Mantsch and D. Chapman, eds, Wiley-Liss, New York
    • E. Nabedryk, Light-induced Fourier trasform infrared difference spectroscopy of the primary electron donor in photosynthetic reaction centers, in: Infrared Spectroscopy of Biomolecules, H.H. Mantsch and D. Chapman, eds, Wiley-Liss, New York, 1996, pp. 39-81.
    • (1996) Infrared Spectroscopy of Biomolecules , pp. 39-81
    • Nabedryk, E.1
  • 33
    • 18744379142 scopus 로고    scopus 로고
    • Proteins in action monitored by time-resolved FTIR spectroscopy
    • C. Koetting and K. Gerwert, Proteins in action monitored by time-resolved FTIR spectroscopy, Chem. Phys. Chem. 6 (2005), 881-888.
    • (2005) Chem. Phys. Chem , vol.6 , pp. 881-888
    • Koetting, C.1    Gerwert, K.2
  • 34
    • 26444511079 scopus 로고    scopus 로고
    • Investigation of ubiquinol formation in isolated photosynthetic reaction centers by rapid-scan FTIR spectroscopy
    • A. Mezzetti and W. Leibl, Investigation of ubiquinol formation in isolated photosynthetic reaction centers by rapid-scan FTIR spectroscopy, Eur. Biophys. J. 34 (2005), 921-936.
    • (2005) Eur. Biophys. J , vol.34 , pp. 921-936
    • Mezzetti, A.1    Leibl, W.2
  • 35
    • 33751242792 scopus 로고    scopus 로고
    • Proton uptake in the reaction center mutant L210DN from Rhodobacter sphaeroides via protonated water molecules
    • S. Hermes, J.M. Stachnik, D. Onidas, A. Remy, E. Hofma and K. Gerwert, Proton uptake in the reaction center mutant L210DN from Rhodobacter sphaeroides via protonated water molecules, Biochemistry 45 (2006), 13741-13749.
    • (2006) Biochemistry , vol.45 , pp. 13741-13749
    • Hermes, S.1    Stachnik, J.M.2    Onidas, D.3    Remy, A.4    Hofma, E.5    Gerwert, K.6
  • 36
    • 0001398583 scopus 로고
    • Step-scan FT-IR spectroscopy of electron transfer in the photosynthetic bacterial reaction center
    • J.-R. Burie, W. Leibl, E. Nabedryk and J. Breton, Step-scan FT-IR spectroscopy of electron transfer in the photosynthetic bacterial reaction center, Appl. Spectrosc. 47 (1993), 1401-1404.
    • (1993) Appl. Spectrosc , vol.47 , pp. 1401-1404
    • Burie, J.-R.1    Leibl, W.2    Nabedryk, E.3    Breton, J.4
  • 37
    • 0037085020 scopus 로고    scopus 로고
    • Rapid-scan FTIR spectroscopy shows coupling of Glu-L212 protonation and electron transfer to QB in Rhodobacter sphaeroides reaction centers
    • A. Mezzetti, E. Nabedryk, J. Breton, M.Y. Okamura, M.L. Paddock, G. Giacometti and W. Leibl, Rapid-scan FTIR spectroscopy shows coupling of Glu-L212 protonation and electron transfer to QB in Rhodobacter sphaeroides reaction centers, Biochim. Biophys. Acta - Bioenergetics 1553 (2002), 320-330.
    • (2002) Biochim. Biophys. Acta - Bioenergetics , vol.1553 , pp. 320-330
    • Mezzetti, A.1    Nabedryk, E.2    Breton, J.3    Okamura, M.Y.4    Paddock, M.L.5    Giacometti, G.6    Leibl, W.7
  • 38
    • 33847221105 scopus 로고    scopus 로고
    • Multivariate curve resolution of rapid-scan FTIR difference spectra of quinone photoreduction in bacterial photosynthetic membranes
    • L. Blanchet, A. Mezzetti, C. Ruckebusch, J.-P. Huvenne and A. de Juan, Multivariate curve resolution of rapid-scan FTIR difference spectra of quinone photoreduction in bacterial photosynthetic membranes, Anal. Bioanal. Chem. 387 (2007), 1863-1874.
    • (2007) Anal. Bioanal. Chem , vol.387 , pp. 1863-1874
    • Blanchet, L.1    Mezzetti, A.2    Ruckebusch, C.3    Huvenne, J.-P.4    de Juan, A.5
  • 39
    • 0040166422 scopus 로고    scopus 로고
    • Error and artefacts in time-resolved step-scan FT-IR spectroscopy
    • C. Rödig and F. Siebert, Error and artefacts in time-resolved step-scan FT-IR spectroscopy, Appl. Spectr. 53 (1999), 893-901.
    • (1999) Appl. Spectr , vol.53 , pp. 893-901
    • Rödig, C.1    Siebert, F.2
  • 40
    • 0002338781 scopus 로고    scopus 로고
    • Improvements in signal acquisition and processing for time-resolved step-scan FT-IR spectroscopy
    • J. De Haseth, ed, American Institute of Physics, Woodbury, NY
    • C. Rödig and F. Siebert, Improvements in signal acquisition and processing for time-resolved step-scan FT-IR spectroscopy, in: Fourier Transform Spectroscopy: Eleventh International Conference, J. De Haseth, ed., American Institute of Physics, Woodbury, NY, 1998, pp. 388-391.
    • (1998) Fourier Transform Spectroscopy: Eleventh International Conference , pp. 388-391
    • Rödig, C.1    Siebert, F.2
  • 41
    • 26844494619 scopus 로고    scopus 로고
    • Temperature effects of excitation laser pulses during step-scan FT-IR experiments
    • C. Rödig, H. Georg, F. Siebert, I. Rousso and M. Sheves, Temperature effects of excitation laser pulses during step-scan FT-IR experiments, Laser Chem. 19 (1999), 169-172.
    • (1999) Laser Chem , vol.19 , pp. 169-172
    • Rödig, C.1    Georg, H.2    Siebert, F.3    Rousso, I.4    Sheves, M.5
  • 42
    • 0031213137 scopus 로고    scopus 로고
    • Noise sources in step-scan FT-IR spectrometry
    • C.J. Manning and P.R. Griffiths, Noise sources in step-scan FT-IR spectrometry, Appl. Spectrosc. 51 (1997), 1092-1101.
    • (1997) Appl. Spectrosc , vol.51 , pp. 1092-1101
    • Manning, C.J.1    Griffiths, P.R.2
  • 43
    • 19144363364 scopus 로고    scopus 로고
    • Instrumental aspects of time-resolved spectra generated using step-scan interometers
    • J.M. Chalmers and P.R. Griffiths, eds, Wiley
    • C. Rödig and F. Siebert, Instrumental aspects of time-resolved spectra generated using step-scan interometers, in: Handbook of Vibrational Spectroscopy, Vol. 2, J.M. Chalmers and P.R. Griffiths, eds, Wiley, 2002, pp. 641-654.
    • (2002) Handbook of Vibrational Spectroscopy , vol.2 , pp. 641-654
    • Rödig, C.1    Siebert, F.2
  • 44
    • 0025339470 scopus 로고
    • Crystallization and preliminary X-ray analysis of a peridinin-chlorophyll a protein from Amphidinium carterae
    • K. Steck, T. Wacker, W. Welte, F.P. Sharples and R.G. Hiller, Crystallization and preliminary X-ray analysis of a peridinin-chlorophyll a protein from Amphidinium carterae, FEBS Lett. 268 (1990), 48-50.
    • (1990) FEBS Lett , vol.268 , pp. 48-50
    • Steck, K.1    Wacker, T.2    Welte, W.3    Sharples, F.P.4    Hiller, R.G.5
  • 45
    • 0000884183 scopus 로고
    • Time-resolved FT-IR absorption spectroscopy using a step-scan interferometer
    • W. Uhmann, A. Becker, C. Taran and F. Siebert, Time-resolved FT-IR absorption spectroscopy using a step-scan interferometer, Appl. Spectr. 45 (1991), 390-397.
    • (1991) Appl. Spectr , vol.45 , pp. 390-397
    • Uhmann, W.1    Becker, A.2    Taran, C.3    Siebert, F.4
  • 47
    • 0039892284 scopus 로고
    • Density functional calculations of molecular bond energies
    • A.D. Becke, Density functional calculations of molecular bond energies, J. Chem. Phys. 84 (1986), 4524-4529.
    • (1986) J. Chem. Phys , vol.84 , pp. 4524-4529
    • Becke, A.D.1
  • 48
    • 0345491105 scopus 로고
    • Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density
    • C. Lee, W. Yang and R.G. Parr, Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density, Phys. Rev. B 37 (1988), 785-789.
    • (1988) Phys. Rev. B , vol.37 , pp. 785-789
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 49
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • A.D. Becke, Density-functional thermochemistry. III. The role of exact exchange, J. Chem. Phys. 98 (1993), 5648-5652.
    • (1993) J. Chem. Phys , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 50
    • 4344679386 scopus 로고    scopus 로고
    • A DFT study of the low-lying singlet excited states of the all-trans peridinins in vacuo
    • R. Spezia, C. Zazza, A. Palma, A. Amadei and M. Aschi, A DFT study of the low-lying singlet excited states of the all-trans peridinins in vacuo, J. Phys. Chem. A 108 (2004), 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
  • 52
    • 0034673379 scopus 로고    scopus 로고
    • Peridinin as the major biological carotenoid quencher of singlet oxygen in marinae algae Gonyaulax polyedra
    • E. Pinto, L.H. Catalani, N. Peporine Lopes, P. Di Mascio and P. Colepicolo, Peridinin as the major biological carotenoid quencher of singlet oxygen in marinae algae Gonyaulax polyedra, Biochem. Biophys. Res. Comm. 268 (2000), 496-500.
    • (2000) Biochem. Biophys. Res. Comm , vol.268 , pp. 496-500
    • Pinto, E.1    Catalani, L.H.2    Peporine Lopes, N.3    Di Mascio, P.4    Colepicolo, P.5
  • 53
    • 8644283571 scopus 로고    scopus 로고
    • Stereocontrolled total synthesis of a polyfunctional carotenoid, peridinin
    • N. Furuichi, H. Hara, T. Osaki, M. Nakano, H. Mori and S. Katsumura, Stereocontrolled total synthesis of a polyfunctional carotenoid, peridinin, J. Org. Chem. 69 (2004), 7949-7959.
    • (2004) J. Org. Chem , vol.69 , pp. 7949-7959
    • Furuichi, N.1    Hara, H.2    Osaki, T.3    Nakano, M.4    Mori, H.5    Katsumura, S.6
  • 55
    • 47749105883 scopus 로고
    • La microspectrométrie Raman de résonance: Méthode d'investigation in vivo des systèmes pigmentaires
    • J.C. Merlin, La microspectrométrie Raman de résonance: méthode d'investigation in vivo des systèmes pigmentaires, Spectrosc. Int. J. 2 (1983), 52-61.
    • (1983) Spectrosc. Int. J , vol.2 , pp. 52-61
    • Merlin, J.C.1
  • 57
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • A. Barth, The infrared absorption of amino acid side chains, Prog. Biophys. Mol. Biol. 74 (2000), 141-173.
    • (2000) Prog. Biophys. Mol. Biol , vol.74 , pp. 141-173
    • Barth, A.1
  • 58
    • 0041320844 scopus 로고    scopus 로고
    • Intermolecular interactions in dry and rehydrated pure and mixed bilayers of phosphatidylcholine and digalactosyldiacylglycerol: A Fourier transform infrared spectroscopy study
    • A.V. Popova and D.K. Hincha, Intermolecular interactions in dry and rehydrated pure and mixed bilayers of phosphatidylcholine and digalactosyldiacylglycerol: a Fourier transform infrared spectroscopy study, Biophys. J. 85 (2003), 1682-1690.
    • (2003) Biophys. J , vol.85 , pp. 1682-1690
    • Popova, A.V.1    Hincha, D.K.2
  • 59
    • 0000885678 scopus 로고
    • Vibrational spectroscopy of chlorophylls
    • H. Scheer, ed, CRC Press, Boca Raton
    • M. Lutz and W. Mäntele, Vibrational spectroscopy of chlorophylls, in: Chlorophylls, H. Scheer, ed., CRC Press, Boca Raton, 1991, pp. 855-902.
    • (1991) Chlorophylls , pp. 855-902
    • Lutz, M.1    Mäntele, W.2
  • 60
    • 33749008562 scopus 로고    scopus 로고
    • Carotenoid interactions in peridinin chlorophyll a proteins from dinoflagellates: Evidence for optical excitons and triplet migration
    • D. Carbonera, G. Giacometti and U. Segre, Carotenoid interactions in peridinin chlorophyll a proteins from dinoflagellates: evidence for optical excitons and triplet migration, J. Chem. Soc. Faraday Transactions 92 (1996), 989-993.
    • (1996) J. Chem. Soc. Faraday Transactions , vol.92 , pp. 989-993
    • Carbonera, D.1    Giacometti, G.2    Segre, U.3
  • 61
    • 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
    • M. Di Valentin, S. Ceola, E. Salvadori, G. Agostini and D. Carbonera, 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 - Bioenergetics 1777 (2008), 186-195.
    • (2008) Biochim. Biophys. Acta - Bioenergetics , vol.1777 , pp. 186-195
    • Di Valentin, M.1    Ceola, S.2    Salvadori, E.3    Agostini, G.4    Carbonera, D.5
  • 62
    • 37849032090 scopus 로고    scopus 로고
    • Spin-density of the carotenoid triplet state in the peridinin- chlorophyll-protein antenna. A Q-band pulsed electron-nuclear double resonance and density functional theory study
    • J. Niklas, T. Schulte, S. Prakash, M. van Gastel, E. Hofmann and W. Lubitz, Spin-density of the carotenoid triplet state in the peridinin- chlorophyll-protein antenna. A Q-band pulsed electron-nuclear double resonance and density functional theory study, J. Am. Chem. Soc. 129 (2007), 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
  • 63
    • 0038298809 scopus 로고    scopus 로고
    • The effect of protein conformational flexibility on the electronic properties of a chromophore
    • R. Spezia, M. Aschi, A. Di Nola, M. Di Valentin, D. Carbonera and A. Amadei, The effect of protein conformational flexibility on the electronic properties of a chromophore, Biophys. J. 84 (2003), 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
  • 64
    • 0000261647 scopus 로고
    • S1 and T1 species of β-carotene generated by direct photo-excitation from the all-trans, 9-cis, 13-cis and 15-cis isomers as revealed by picosecond transient absorption and transient Raman spectroscopies
    • H. Hashimoto, Y. Koyama, Y. Hirata and N. Mataga, S1 and T1 species of β-carotene generated by direct photo-excitation from the all-trans, 9-cis, 13-cis and 15-cis isomers as revealed by picosecond transient absorption and transient Raman spectroscopies, J. Phys. Chem. 95 (1991), 3072-3076.
    • (1991) J. Phys. Chem , vol.95 , pp. 3072-3076
    • Hashimoto, H.1    Koyama, Y.2    Hirata, Y.3    Mataga, N.4
  • 65
    • 4344685544 scopus 로고    scopus 로고
    • Insights into the molecular dynamics of plant light-harvesting proteins in vivo
    • B. Robert, P. Horton, A.A. Pascal and A.V. Ruban, Insights into the molecular dynamics of plant light-harvesting proteins in vivo, Trends Plant Sci. 9 (2004), 385-390.
    • (2004) Trends Plant Sci , vol.9 , pp. 385-390
    • Robert, B.1    Horton, P.2    Pascal, A.A.3    Ruban, A.V.4
  • 66
    • 33645239498 scopus 로고    scopus 로고
    • Resonance Raman detection of carotenoid antioxidants in living human tissue
    • I.V. Ermakov, M. Sharifzadeh, M. Ermakova and W. Gellermann, Resonance Raman detection of carotenoid antioxidants in living human tissue, J. Biomed. Opt. 10 (2005), 064028.
    • (2005) J. Biomed. Opt , vol.10 , pp. 064028
    • Ermakov, I.V.1    Sharifzadeh, M.2    Ermakova, M.3    Gellermann, W.4
  • 67
    • 34250797484 scopus 로고    scopus 로고
    • Halocynthiaxanthin and peridinin sensitize colon cancer cell lines to tumor necrosis factor-related apoptosis-inducing ligand
    • T. Yoshida, T. Maoka, S.K. Das, K. Kanazawa, M. Horinaka, M. Wakada, Y. Satomi, H. Nishino and T Sakai, Halocynthiaxanthin and peridinin sensitize colon cancer cell lines to tumor necrosis factor-related apoptosis-inducing ligand, Mol. Cancer Res. 5 (2007), 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, Y.7    Nishino, H.8    Sakai, T.9
  • 68
    • 34247478146 scopus 로고    scopus 로고
    • Induction of apoptosis in DLD-1 human colon cancer cells by peridinin isolated from the dinoflagellate, Heterocapsa triquetra
    • T. Sugawara, K. Yamashita, S. Sakai, A. Asai, A. Nagao, T. Shiraishi, I. Imai and T. Hirata, Induction of apoptosis in DLD-1 human colon cancer cells by peridinin isolated from the dinoflagellate, Heterocapsa triquetra, Biosci. Biotechnol. Biochem. 71 (2007), 1069-1072.
    • (2007) Biosci. Biotechnol. Biochem , vol.71 , pp. 1069-1072
    • Sugawara, T.1    Yamashita, K.2    Sakai, S.3    Asai, A.4    Nagao, A.5    Shiraishi, T.6    Imai, I.7    Hirata, T.8
  • 69
    • 0027071866 scopus 로고
    • A simultaneous three-color T cell subsets analysis with single laser flow cytometers using T cell gating protocol. Comparison with conventional two-color immunophenotyping method
    • F.F. Mandy, M. Bergeron, D. Recktenwald and C.A. Izaguirre, A simultaneous three-color T cell subsets analysis with single laser flow cytometers using T cell gating protocol. Comparison with conventional two-color immunophenotyping method, J. Immunol. Methods 156 (1992), 151-162.
    • (1992) J. Immunol. Methods , vol.156 , pp. 151-162
    • Mandy, F.F.1    Bergeron, M.2    Recktenwald, D.3    Izaguirre, C.A.4
  • 70
    • 7944238095 scopus 로고    scopus 로고
    • A new immunofluorostaining method using red fluorescence of PerCP on formalin-fixed paraffin-embedded tissues
    • H. Niki, S. Hosokawa, K. Nagaike and T. Tagawa, A new immunofluorostaining method using red fluorescence of PerCP on formalin-fixed paraffin-embedded tissues, J. Immunol. Methods 293 (2004), 143-151.
    • (2004) J. Immunol. Methods , vol.293 , pp. 143-151
    • Niki, H.1    Hosokawa, S.2    Nagaike, K.3    Tagawa, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.