메뉴 건너뛰기




Volumn 88, Issue 1, 2012, Pages 98-106

Chemical bonding of chlorophylls and plant aminic axial ligands impact harvesting of visible light and quenching of fluorescence

Author keywords

[No Author keywords available]

Indexed keywords

CHLOROPHYLL; LIGAND;

EID: 84855357649     PISSN: 00318655     EISSN: 17511097     Source Type: Journal    
DOI: 10.1111/j.1751-1097.2011.01003.x     Document Type: Review
Times cited : (6)

References (58)
  • 1
    • 0036150436 scopus 로고    scopus 로고
    • The enigma of the origin of life and its timing
    • Line, M. A., (2002) The enigma of the origin of life and its timing. Microbiology 148, 21-27. (Pubitemid 34083181)
    • (2002) Microbiology , vol.148 , Issue.1 , pp. 21-27
    • Line, M.A.1
  • 2
    • 70350565366 scopus 로고    scopus 로고
    • Functional architecture of higher plant photosystem II supercomplexes
    • Caffarri, S., R. Kouril, S. Kereiche, E. J. Boekema, and, R. Croce, (2009) Functional architecture of higher plant photosystem II supercomplexes. EMBO J. 28, 3052-3063.
    • (2009) EMBO J. , vol.28 , pp. 3052-3063
    • Caffarri, S.1    Kouril, R.2    Kereiche, S.3    Boekema, E.J.4    Croce, R.5
  • 3
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • DOI 10.1038/367614a0
    • Kuhlbrandt, W., D. N. Wang, and, Y. Fujiyoshi, (1994) Atomic model of plant light-harvesting complex by electron crystallography. Nature 367, 614-621. (Pubitemid 24067701)
    • (1994) Nature , vol.367 , Issue.6464 , pp. 614-621
    • Kuhlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 4
    • 66449120007 scopus 로고    scopus 로고
    • Crystallisation, structure and function of plant light-harvesting Complex II
    • Barros, T., and, W. Kühlbrandt, (2009) Crystallisation, structure and function of plant light-harvesting Complex II. Biochim. Biophys. Acta 1787, 753-772.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 753-772
    • Barros, T.1    Kühlbrandt, W.2
  • 5
    • 16344363252 scopus 로고    scopus 로고
    • Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 A resolution
    • DOI 10.1038/sj.emboj.7600585
    • Standfuss, J., A. C. Terwisscha van Scheltinga, M. Lamborghini, and, W. Kühlbrandt, (2005) Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 Å resolution. EMBO J. 24, 919-928. (Pubitemid 40470141)
    • (2005) EMBO Journal , vol.24 , Issue.5 , pp. 919-928
    • Standfuss, J.1    Van Scheltinga, A.C.T.2    Lamborghini, M.3    Kuhlbrandt, W.4
  • 6
    • 0036438486 scopus 로고    scopus 로고
    • Which side of the π-macrocycle plane of (bacterio)chlorophylls is favored for binding of the fifth ligand?
    • DOI 10.1023/A:1020816128794
    • Oba, T., and, H. Tamiaki, (2002) Which side of the π-macrocycle plane of (bacterio)chlorophylls is favored for binding of the fifth ligand? Photosynth. Res. 74, 1-10. (Pubitemid 35399809)
    • (2002) Photosynthesis Research , vol.74 , Issue.1 , pp. 1-10
    • Oba, T.1    Tamiaki, H.2
  • 7
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach major light-harvesting complex at 2.72 A resolution
    • DOI 10.1038/nature02373
    • Liu, Z., H. Yan, K. Wang, T. Kuang, J. Zhang, L. Gui, X. An, and, W. Chang, (2004) Crystal structure of spinach major light-harvesting complex at 2.72 A resolution. Nature 428, 287-292. (Pubitemid 38418793)
    • (2004) Nature , vol.428 , Issue.6980 , pp. 287-292
    • Liu, Z.1    Yan, H.2    Wang, K.3    Kuang, T.4    Zhang, J.5    Gui, L.6    An, X.7    Chang, W.8
  • 8
    • 33748787697 scopus 로고    scopus 로고
    • Axial coordination to metalloporphyrins leading to multinuclear assemblies
    • DOI 10.1007/430-021, Non-Covalent Multi-Porphyrin Assemblies
    • Bouamaied, I., T. Coskun, and, E. Stulz, (2006) Axial coordination to metalloporphyrins leading to multinuclear assemblies. Struct. Bonding 121, 1-47. (Pubitemid 44406285)
    • (2006) Structure and Bonding , vol.121 , pp. 1-47
    • Bouamaied, I.1    Coskun, T.2    Stulz, E.3
  • 10
    • 47249122499 scopus 로고    scopus 로고
    • Polyamines: Essential factors for growth and survival
    • Kusano, T., T. Berberich, C. Tateda, and, Y. Takahashi, (2008) Polyamines: Essential factors for growth and survival. Planta 228, 367-381.
    • (2008) Planta , vol.228 , pp. 367-381
    • Kusano, T.1    Berberich, T.2    Tateda, C.3    Takahashi, Y.4
  • 11
    • 79953879400 scopus 로고    scopus 로고
    • Polyamines stimulate nonphotochemical quenching of chlorophyll fluorescence in Scenedesmus obliquus
    • Ioannidis, N., L. Sfichi-Duke, and, K. Kotzabasis, (2011) Polyamines stimulate nonphotochemical quenching of chlorophyll fluorescence in Scenedesmus obliquus. Photosynth. Res. 107, 169-175.
    • (2011) Photosynth. Res. , vol.107 , pp. 169-175
    • Ioannidis, N.1    Sfichi-Duke, L.2    Kotzabasis, K.3
  • 13
    • 0029945527 scopus 로고    scopus 로고
    • Changes in the biosynthesis and catabolism of polyamines in isolated plastids during chloroplast photodevelopment
    • DOI 10.1016/1011-1344(95)07240-3
    • Andreadakis, A., and, K. Kotzabasis, (1996) Changes in the biosynthesis and catabolism of polyamines in isolated plastids during chloroplast photodevelopment. J. Photochem. Photobiol. 33, 163-170. (Pubitemid 26193800)
    • (1996) Journal of Photochemistry and Photobiology B: Biology , vol.33 , Issue.2 , pp. 163-170
    • Andreadakis, A.1    Kotzabasis, K.2
  • 16
    • 0028042505 scopus 로고
    • Identification of chlorophyll-a/b proteins as substrates of transglutaminase activity in isolated chloroplasts of Helianthus tuberosus L
    • Duca, S., V. Tidu, R. Bassi, C. Esposito, and, D. Serafini-Fracassini, (1994) Identification of chlorophyll-a/b proteins as substrates of transglutaminase activity in isolated chloroplasts of Helianthus tuberosus L. Planta 193, 283-289. (Pubitemid 2053693)
    • (1994) Planta , vol.193 , Issue.2 , pp. 283-289
    • Del Duca, S.1    Tidu, V.2    Bassi, R.3    Esposito, C.4    Serafini-Fracassini, D.5
  • 17
    • 4444231661 scopus 로고    scopus 로고
    • A Zea mays 39-kDa thylakoid transglutaminase catalyses the modification by polyamines of light-harvesting complex II in a light-dependent way
    • DOI 10.1007/s00425-004-1278-6
    • Della Mea, M., A. Di Sandro, L. Dondini, S. Del Duca, F. Vantini, C. Bergamini, R. Bassi, and, D. Serafini-Fracassini, (2004) A Zea mays 39-kDa thylakoid transglutaminase catalyses the modification by polyamines of light-harvesting complexII in a light-dependent way. Planta 219, 754-764. (Pubitemid 39282939)
    • (2004) Planta , vol.219 , Issue.5 , pp. 754-764
    • Della Mea, M.1    Di Sandro, A.2    Dondini, L.3    Del Duca, S.4    Vantini, F.5    Bergamini, C.6    Bassi, R.7    Serafini-Fracassini, D.8
  • 18
    • 0031023829 scopus 로고    scopus 로고
    • The effects of spermine and spermidine on the structure of photosystem II proteins in relation to inhibition of electron transport
    • DOI 10.1016/S0014-5793(96)01453-6, PII S0014579396014536
    • Bograh, A., Y. Gingras, H. A. Tajmir-Riahi, and, R. Carpentier, (1997) The effects of spermine and spermidine on the structure of photosystem II proteins in relation to inhibition of electron transport. FEBS Lett. 402, 41-44. (Pubitemid 27056021)
    • (1997) FEBS Letters , vol.402 , Issue.1 , pp. 41-44
    • Bograh, A.1    Gingras, Y.2    Tajmir-Riahi, H.A.3    Carpentier, R.4
  • 21
    • 79958018151 scopus 로고    scopus 로고
    • Polyamines interaction with thylakoid proteins during stress
    • Hamdani, S., H. Yaakoubi, and, R. Carpentier, (2011) Polyamines interaction with thylakoid proteins during stress. J. Photochem. Photobiol. 104, 314-319.
    • (2011) J. Photochem. Photobiol. , vol.104 , pp. 314-319
    • Hamdani, S.1    Yaakoubi, H.2    Carpentier, R.3
  • 23
    • 45049086575 scopus 로고    scopus 로고
    • Fast and reversible response of thylakoid-associated polyamines during and after UV-B stress: A comparative study of the wild type and a mutant lacking chlorophyll of unicellular green alga Scenedesmus obliquus
    • Sfichi-Duke, L., N. Ioannidis, and, K. Kotzabasis, (2008) Fast and reversible response of thylakoid-associated polyamines during and after UV-B stress: A comparative study of the wild type and a mutant lacking chlorophyll of unicellular green alga Scenedesmus obliquus. Planta 228, 341-353.
    • (2008) Planta , vol.228 , pp. 341-353
    • Sfichi-Duke, L.1    Ioannidis, N.2    Kotzabasis, K.3
  • 24
    • 12944321372 scopus 로고    scopus 로고
    • Thylakoid-associated polyamines adjust the UV-B sensitivity of the photosynthetic apparatus by means of light-harvesting complex II changes
    • DOI 10.1562/2004-01-RA-130.1
    • Sfichi, L., N. Ioannidis, and, K. Kotzabasis, (2004) Thylakoid-associated polyamines adjust the UV-B sensitivity of the photosynthetic apparatus by means of light-harvesting complex II changes. Photochem. Photobiol. 80, 499-506. (Pubitemid 40174477)
    • (2004) Photochemistry and Photobiology , vol.80 , Issue.3 , pp. 499-506
    • Sfichi, L.1    Ioannidis, N.2    Kotzabasis, K.3
  • 25
    • 79956109906 scopus 로고    scopus 로고
    • Positive charges of polyamines protect PSII in isolated thylakoid membranes during photoinhibitory conditions
    • Hamdani, S., A. Gauthier, N. Msilini, and, R. Carpentier, (2011) Positive charges of polyamines protect PSII in isolated thylakoid membranes during photoinhibitory conditions. Plant Cell Physiol. 52, 866-873.
    • (2011) Plant Cell Physiol. , vol.52 , pp. 866-873
    • Hamdani, S.1    Gauthier, A.2    Msilini, N.3    Carpentier, R.4
  • 26
    • 36549066663 scopus 로고    scopus 로고
    • Effects of polyamines on the functionality of photosynthetic membrane in vivo and in vitro
    • DOI 10.1016/j.bbabio.2007.10.002, PII S0005272807002319
    • Ioannidis, N. E., and, K. Kotzabasis, (2007) Effects of polyamines on the functionality of photosynthetic membrane in vivo and in vitro. Biochim. Biophys. Acta 1767, 1372-1382. (Pubitemid 350179717)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.12 , pp. 1372-1382
    • Ioannidis, N.E.1    Kotzabasis, K.2
  • 27
    • 0343851071 scopus 로고    scopus 로고
    • A pigment-binding protein essential for regulation of photosynthetic light harvesting
    • DOI 10.1038/35000131
    • Li, X.-P., O. Bjorkman, C. Shih, A. R. Grossman, M. Rosenquist, S. Jansson, and, K. K. Niyogi, (2000) A pigment-binding protein essential for regulation of photosynthetic light harvesting. Nature 403, 391-395. (Pubitemid 30073080)
    • (2000) Nature , vol.403 , Issue.6768 , pp. 391-395
    • Li, X.-P.1    Bjorkman, O.2    Shih, C.3    Grossman, A.R.4    Rosenquist, M.5    Jansson, S.6    Niyogi, K.K.7
  • 30
    • 44049086448 scopus 로고    scopus 로고
    • Architecture of a charge-transfer state regulating light harvesting in a plant antenna protein
    • DOI 10.1126/science.1154800
    • Ahn, T. K., T. J. Avenson, M. Ballottari, Y.-C. Cheng, K. K. Niyogi, R. Bassi, and, G. R. Fleming, (2008) Architecture of a charge-transfer state regulating light harvesting in a plant antenna protein. Science 320, 794-797. (Pubitemid 351929628)
    • (2008) Science , vol.320 , Issue.5877 , pp. 794-797
    • Ahn, T.K.1    Avenson, T.J.2    Ballottari, M.3    Cheng, Y.-C.4    Niyogi, K.K.5    Bassi, R.6    Fleming, G.R.7
  • 31
    • 60249092468 scopus 로고    scopus 로고
    • The zeaxanthin-independent and zeaxanthin-dependent qE components of nonphotochemical quenching involve common conformational changes within the photosystem II antenna in arabidopsis
    • Johnson, M. P., M. L. Perez-Bueno, A. Zia, P. Horton, and, A. V. Ruban, (2009) The zeaxanthin-independent and zeaxanthin-dependent qE components of nonphotochemical quenching involve common conformational changes within the photosystem II antenna in arabidopsis. Plant Physiol. 149, 1061-1075.
    • (2009) Plant Physiol. , vol.149 , pp. 1061-1075
    • Johnson, M.P.1    Perez-Bueno, M.L.2    Zia, A.3    Horton, P.4    Ruban, A.V.5
  • 32
    • 58649105358 scopus 로고    scopus 로고
    • Biophysical techniques in photosynthesis
    • In, II (Edited by T. J. Aartsma and J. Matysik), Springer, Dordrecht, The Netherlands
    • Groot, M. L., and, R. Van Grondelle, (2008) Biophysical techniques in photosynthesis. In Advances in Photosynthesis and Respiration, Vol. II (Edited by, T. J. Aartsma, and, J. Matysik,), pp. 191-200. Springer, Dordrecht, The Netherlands.
    • (2008) Advances in Photosynthesis and Respiration , pp. 191-200
    • Groot, M.L.1    Van Grondelle, R.2
  • 34
    • 0035133925 scopus 로고    scopus 로고
    • Acclimation of chloroplast transglutaminase to high NaCI concentration in a polyamine-deficient variant strain of Dunaliella salina and in its wild type
    • Dondini, L., S. Bonazzi, S. Del Duca, A. Bregoli, and, D. Serafini-Fracassini, (2001) Acclimation of chloroplast transglutaminase to high NaCl concentration in a polyamine-deficient variant strain of Dunaliella salina and in its wild type. Plant Physiol. 158, 185-197. (Pubitemid 32161061)
    • (2001) Journal of Plant Physiology , vol.158 , Issue.2 , pp. 185-197
    • Dondini, L.1    Bonazzi, S.2    Del Duca, S.3    Bregoli, A.M.4    Serafini-Fracassini, D.5
  • 35
    • 34250501701 scopus 로고
    • Die Isolierung und quantitative Bestimmung der Carotinoide und Chlorophylle von Blättern, Algen und isolierten Chloroplasten mit Hilfe dünnschichtchromatographischer Methoden
    • Hager, A., and, T. Meyer-Bertenrath, (1966) Die Isolierung und quantitative Bestimmung der Carotinoide und Chlorophylle von Blättern, Algen und isolierten Chloroplasten mit Hilfe dünnschichtchromatographischer Methoden. Planta 69, 198-217.
    • (1966) Planta , vol.69 , pp. 198-217
    • Hager, A.1    Meyer-Bertenrath, T.2
  • 36
    • 32044447572 scopus 로고    scopus 로고
    • Photosynthetic pigment profile of Cordia myxa L. and its potential in folklore medicinal application
    • Afzal, M., C. Obuekwe, N. Shuaib, and, H. Barakat, (2004) Photosynthetic pigment profile of Cordia myxa L. and its potential in folklore medicinal application. Int. J. Food Agric. Environ. 2, 114-120.
    • (2004) Int. J. Food Agric. Environ. , vol.2 , pp. 114-120
    • Afzal, M.1    Obuekwe, C.2    Shuaib, N.3    Barakat, H.4
  • 37
    • 60549086077 scopus 로고    scopus 로고
    • Complexation of Mg-tetrabenzoporphyrin with pyridine enhances singlet oxygen generation and affects its partitioning into apolar microenvironments
    • Weitman, H., S. Shatz, and, B. Ehrenberg, (2009) Complexation of Mg-tetrabenzoporphyrin with pyridine enhances singlet oxygen generation and affects its partitioning into apolar microenvironments. J. Photochem. Photobiol. 203, 7-12.
    • (2009) J. Photochem. Photobiol. , vol.203 , pp. 7-12
    • Weitman, H.1    Shatz, S.2    Ehrenberg, B.3
  • 38
    • 0016747815 scopus 로고
    • Evidence for 5- and 6-coordinated magnesium in bacteriochlorophyll a from visible absorption spectroscopy
    • Evans, T. A., and, J. J. Katz, (1975) Evidence for 5- and 6-coordinated magnesium in bacteriochlorophyll a from visible absorption spectroscopy. Biochim. Biophys. Acta 396, 414-426.
    • (1975) Biochim. Biophys. Acta , vol.396 , pp. 414-426
    • Evans, T.A.1    Katz, J.J.2
  • 40
    • 65949104816 scopus 로고    scopus 로고
    • Mirror symmetry and vibrational structure in optical spectra of chlorophyll a
    • Rätsep, M., J. Linnanto, and, A. Freiberg, (2009) Mirror symmetry and vibrational structure in optical spectra of chlorophyll a. J. Chem. Phys. 130, 194501.
    • (2009) J. Chem. Phys. , vol.130 , pp. 194501
    • Rätsep, M.1    Linnanto, J.2    Freiberg, A.3
  • 41
    • 3142699106 scopus 로고
    • The reaction of chlorophyll in amines
    • Weller, A., and, R. Livingston, (1954) The reaction of chlorophyll in amines. J. Am. Chem. Soc. 76, 1575-1578.
    • (1954) J. Am. Chem. Soc. , vol.76 , pp. 1575-1578
    • Weller, A.1    Livingston, R.2
  • 42
    • 0008981812 scopus 로고
    • Reaction of chlorophylls a and b with amines. Isocyclic ring rupture and formation of substituted chlorin-6-amides
    • Pennington, F. C., S. D. Boyd, H. Horton, S. W. Taylor, D. G. Wulf, J. J. Katz, and, H. H. Strain, (1967) Reaction of chlorophylls a and b with amines. Isocyclic ring rupture and formation of substituted chlorin-6-amides. J. Am. Chem. Soc. 89, 3871-3875.
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 3871-3875
    • Pennington, F.C.1    Boyd, S.D.2    Horton, H.3    Taylor, S.W.4    Wulf, D.G.5    Katz, J.J.6    Strain, H.H.7
  • 43
    • 3142760767 scopus 로고
    • Ring v reactions of chlorophylls and pheophytins with amines
    • Pennington, F. C., N. B. Boettcher, and, J. J. Katz, (1974) Ring V reactions of chlorophylls and pheophytins with amines. Bioorg. Chem. 3, 204-212.
    • (1974) Bioorg. Chem. , vol.3 , pp. 204-212
    • Pennington, F.C.1    Boettcher, N.B.2    Katz, J.J.3
  • 44
    • 55049100853 scopus 로고    scopus 로고
    • Interplay between acetate ions, peripheral groups and reactivity of the core nitrogens in transmetalation of tetrapyrroles
    • Orzel, L., L. Fiedor, M. Wolak, A. Kania, R. van Eldik, and, G. Stochel, (2008) Interplay between acetate ions, peripheral groups and reactivity of the core nitrogens in transmetalation of tetrapyrroles. Chem. Eur. J. 14, 9419-9430.
    • (2008) Chem. Eur. J. , vol.14 , pp. 9419-9430
    • Orzel, L.1    Fiedor, L.2    Wolak, M.3    Kania, A.4    Van Eldik, R.5    Stochel, G.6
  • 45
    • 33845676767 scopus 로고    scopus 로고
    • Identification and quantification of valuable plant substances by IR and Raman spectroscopy
    • DOI 10.1016/j.vibspec.2006.06.001, PII S0924203106001263, VIBRATIONAL SPECTROSCOPY
    • Schulz, H., and, M. Baranska, (2007) Identification and quantification of valuable plant substances by IR and Raman spectroscopy. Vib. Spectrosc. 43, 13-25. (Pubitemid 44960690)
    • (2007) Vibrational Spectroscopy , vol.43 , Issue.1 , pp. 13-25
    • Schulz, H.1    Baranska, M.2
  • 46
    • 0024953088 scopus 로고
    • Mechanisms of cooperativity and allosteric regulation in proteins
    • Perutz, M. F., (1989) Mechanisms of cooperativity and allosteric regulation in proteins. Quart. Rev. Biophys. 22, 139-236. (Pubitemid 20121055)
    • (1989) Quarterly Reviews of Biophysics , vol.22 , Issue.2 , pp. 139-236
    • Perutz, M.F.1
  • 47
    • 0035839641 scopus 로고    scopus 로고
    • Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen
    • Trent, J. T., R. A. Watts, and, M. S. Hargrove, (2001) Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen. J. Biol. Chem. 276, 30106-30110.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30106-30110
    • Trent, J.T.1    Watts, R.A.2    Hargrove, M.S.3
  • 48
    • 0039698192 scopus 로고    scopus 로고
    • Mutant trimers of light-harvesting complex II exhibit altered pigment content and spectroscopic features
    • Rogl, H., and, W. Kuehbrandt, (1999) Mutant trimers of light-harvesting complex II exhibit altered pigment content and spectroscopic features. Biochemistry 38, 16214-16222. (Pubitemid 129520542)
    • (1999) Biochemistry , vol.38 , Issue.49 , pp. 16214-16222
    • Rogl, H.1    Kuhlbrandt, W.2
  • 49
    • 0032834609 scopus 로고    scopus 로고
    • The importance of PS I chlorophyll red forms in light-harvesting by leaves
    • Rivadossi, A., G. Zucchelli, F. M. Garlaschi, and, R. C. Jennings, (1999) The importance of PSI chlorophyll red forms in light-harvesting by leaves. Photosynth. Res. 60, 209-215. (Pubitemid 29424757)
    • (1999) Photosynthesis Research , vol.60 , Issue.2-3 , pp. 209-215
    • Rivadossi, A.1    Zucchelli, G.2    Garlaschi, F.M.3    Jennings, R.C.4
  • 50
    • 12944309303 scopus 로고    scopus 로고
    • Light absorption by the chlorophyll a-b complexes of photosystem II in a leaf with special reference to LHCII
    • DOI 10.1562/2004-04-16-RA-14.1
    • Rivadossi, A., G. Zucchelli, F. M. Garlaschi, and, R. C. Jennings, (2004) Light absorption by the chlorophyll a-b complexes of photosystem II in a leaf with special reference to LHCII. Photochem. Photobiol. 80, 492-498. (Pubitemid 40174476)
    • (2004) Photochemistry and Photobiology , vol.80 , Issue.3 , pp. 492-498
    • Rivadossi, A.1    Zucchelli, G.2    Garlaschi, F.M.3    Jennings, R.C.4
  • 51
    • 0030668099 scopus 로고    scopus 로고
    • Analysis of some optical properties of a native and reconstituted photosystem II antenna complex, CP29: Pigment binding sites can be occupied by chlorophyll a or chlorophyll b and determine spectral forms
    • DOI 10.1021/bi9711339
    • Giuffra, E., G. Zucchelli, D. Sandona, R. Croce, D. Cugini, F. M. Garlaschi, R. Bassi, and, R. C. Jennings, (1997) Analysis of some optical properties of a native and reconstituted photosystem II antenna complex, CP29: Pigment binding sites can be occupied by chlorophyll a or chlorophyll b and determine spectral forms. Biochemistry 36, 12984-12993. (Pubitemid 27465412)
    • (1997) Biochemistry , vol.36 , Issue.42 , pp. 12984-12993
    • Giuffra, E.1    Zucchelli, G.2    Sandona, D.3    Croce, R.4    Cugini, D.5    Garlaschi, F.M.6    Bassi, R.7    Jennings, R.C.8
  • 52
    • 0031855446 scopus 로고    scopus 로고
    • A diffused-optics flash kinetic spectrophotometer (DOFS) for measurements of absorbance changes in intact plants in the steady-state
    • DOI 10.1023/A:1005968211506
    • Kramer, D. M., and, C. A. Sacksteder, (1998) A diffused-optics flash kinetic spectrophotometer (DOFS) for measurements of absorbance changes in intact plants in the steady-state. Photosynth. Res. 56, 103-112. (Pubitemid 28358503)
    • (1998) Photosynthesis Research , vol.56 , Issue.1 , pp. 103-112
    • Kramer, D.M.1    Sacksteder, C.A.2
  • 53
    • 0001153469 scopus 로고
    • Resonance Raman excitation profiles and structure of a T-shaped chlorophyll dimer in solution
    • Thibodeau, D. L., and, K. JA, (1989) Resonance Raman excitation profiles and structure of a T-shaped chlorophyll dimer in solution. J. Phys. Chem. 93, 7713-7717.
    • (1989) J. Phys. Chem. , vol.93 , pp. 7713-7717
    • Thibodeau, D.L.1    Ja, K.2
  • 54
    • 77950366997 scopus 로고    scopus 로고
    • An arabidopsis mutant with high cyclic electron flow around photosystem i (hcef) involving the NADPH dehydrogenase complex
    • Livingston, A. K., J. A. Cruz, K. Kohzuma, A. Dhingra, and, D. M. Kramer, (2010) An arabidopsis mutant with high cyclic electron flow around photosystem I (hcef) involving the NADPH dehydrogenase complex. Plant Cell 22, 221-233.
    • (2010) Plant Cell , vol.22 , pp. 221-233
    • Livingston, A.K.1    Cruz, J.A.2    Kohzuma, K.3    Dhingra, A.4    Kramer, D.M.5
  • 55
    • 0018789833 scopus 로고
    • Energy conversion in the functional membranes of photosynthesis analysis by light pulse and electric pulse methods
    • Witt, H. T., (1979) Energy conversion in the functional membranes of photosynthesis analysis by light pulse and electric pulse methods. Biochim. Biophys. Acta 505, 355-427.
    • (1979) Biochim. Biophys. Acta , vol.505 , pp. 355-427
    • Witt, H.T.1
  • 57
    • 0000584964 scopus 로고    scopus 로고
    • Plant biology-Retrospect and prospect
    • Galston, A. W., (2001) Plant biology-Retrospect and prospect. Curr. Sci. 80, 143-152.
    • (2001) Curr. Sci. , vol.80 , pp. 143-152
    • Galston, A.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.