메뉴 건너뛰기




Volumn 50, Issue 2-3, 1999, Pages 189-196

Light- and heat-induced denaturation of photosystem II core-antenna complexes CP43 and CP47

Author keywords

Absorption fluorescence; Circular dichroism; CP43; CP47; Photosystem II

Indexed keywords

CHLOROPHYLL A; PIGMENT; VEGETABLE PROTEIN;

EID: 0032862297     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1011-1344(99)00091-3     Document Type: Article
Times cited : (21)

References (41)
  • 2
    • 30244551690 scopus 로고
    • The structure and function of Cpa-1 and Cpa-2 in photosystem II
    • [2] T.M. Bricker, The structure and function of Cpa-1 and Cpa-2 in photosystem II, Photosynthesis Res. 24 (1990) 1-13.
    • (1990) Photosynthesis Res. , vol.24 , pp. 1-13
    • Bricker, T.M.1
  • 3
    • 0000223633 scopus 로고    scopus 로고
    • Introduction to oxygen evolution and the oxygen-evolving complex
    • D.R. Ort, C.F. Yocum (Eds.), Kluwer, Dordrecht
    • [3] T.M. Bricker, D.F. Ghanotakis, Introduction to oxygen evolution and the oxygen-evolving complex, in: D.R. Ort, C.F. Yocum (Eds.), Oxygenic Photosynthesis: The Light Reactions, Kluwer, Dordrecht, 1996, pp. 113-136.
    • (1996) Oxygenic Photosynthesis: The Light Reactions , pp. 113-136
    • Bricker, T.M.1    Ghanotakis, D.F.2
  • 4
    • 0028269096 scopus 로고
    • Structure-function relationships in the 47-kDa antenna protein and its complex with the photosystem II reaction center core: Insights from picosecond fluorescence decay kinetics and resonance raman spectroscopy
    • [4] J.C. De Paula, A. Liefshitz, S. Hinsley, W. Lin, V. Chopra, K. Long, S.A. Williams, S. Betts, C.F. Yocum, Structure-function relationships in the 47-kDa antenna protein and its complex with the photosystem II reaction center core: insights from picosecond fluorescence decay kinetics and resonance raman spectroscopy, Biochemistry 33 (1994) 1455-1466.
    • (1994) Biochemistry , vol.33 , pp. 1455-1466
    • De Paula, J.C.1    Liefshitz, A.2    Hinsley, S.3    Lin, W.4    Chopra, V.5    Long, K.6    Williams, S.A.7    Betts, S.8    Yocum, C.F.9
  • 5
    • 45549117331 scopus 로고
    • Disintegration and reconstitution of photosystem II reaction center core complex. I. Preparation and characterization of three different types of subcomplex
    • [5] K. Akabori, H. Tsukamoto, J. Tsukihara, T. Nagatsuka, O. Motokawa, Y. Toyoshima, Disintegration and reconstitution of photosystem II reaction center core complex. I. preparation and characterization of three different types of subcomplex, Biochim. Biophys. Acta 932 (1988) 345-357.
    • (1988) Biochim. Biophys. Acta , vol.932 , pp. 345-357
    • Akabori, K.1    Tsukamoto, H.2    Tsukihara, J.3    Nagatsuka, T.4    Motokawa, O.5    Toyoshima, Y.6
  • 6
    • 0025851076 scopus 로고
    • Chlorophyll levels in the pigment-binding proteins of photosystem II a study based on the chlorophyll to cytochrome ratio in different photosystem II preparations
    • [6] R. Barbato, H.L. Race, G. Friso, J. Barber, Chlorophyll levels in the pigment-binding proteins of photosystem II a study based on the chlorophyll to cytochrome ratio in different photosystem II preparations, FEBS Lett. 286 (1991) 86-90.
    • (1991) FEBS Lett. , vol.286 , pp. 86-90
    • Barbato, R.1    Race, H.L.2    Friso, G.3    Barber, J.4
  • 7
    • 0028141568 scopus 로고
    • Core antenna complexes, CP43 and CP47, of higher plant photosystem II. Spectral properties, pigment stoichiometry, and amino acid composition
    • [7] M. Alfonso, G. Montoya, R. Cases, R. Rodriguez, R. Picorel, Core antenna complexes, CP43 and CP47, of higher plant photosystem II. Spectral properties, pigment stoichiometry, and amino acid composition, Biochemistry 33 (1994) 10494-10500.
    • (1994) Biochemistry , vol.33 , pp. 10494-10500
    • Alfonso, M.1    Montoya, G.2    Cases, R.3    Rodriguez, R.4    Picorel, R.5
  • 8
    • 0032568955 scopus 로고    scopus 로고
    • Isolation and characterization of monomeric and dimeric CP47-reaction center photosystem II complexes
    • [8] D. Zheleva, J. Sharma, M. Panico, H.R. Morris, J. Barber, Isolation and characterization of monomeric and dimeric CP47-reaction center photosystem II complexes, J. Biol. Chem. 273 (1998) 16122-16127.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16122-16127
    • Zheleva, D.1    Sharma, J.2    Panico, M.3    Morris, H.R.4    Barber, J.5
  • 9
    • 0029583850 scopus 로고
    • Destruction of a single chlorophyll is correlated with the photoinhibition of photosystem II with a transiently inactive donor side
    • [9] D. Bumann, D. Oesterhelt, Destruction of a single chlorophyll is correlated with the photoinhibition of photosystem II with a transiently inactive donor side, Proc. Natl. Acad. Sci. USA 92 (1995) 12195-12199.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12195-12199
    • Bumann, D.1    Oesterhelt, D.2
  • 10
    • 0025781574 scopus 로고
    • β-Carotene within the isolated photosystem II reaction center: Photooxidation and irreversible bleaching of this chromophore by oxidized P680
    • [10] A. Telfer, J. De Las Rivas, J. Barber, β-Carotene within the isolated photosystem II reaction center: photooxidation and irreversible bleaching of this chromophore by oxidized P680, Biochim. Biophys. Acta 1060 (1991) 106-114.
    • (1991) Biochim. Biophys. Acta , vol.1060 , pp. 106-114
    • Telfer, A.1    De Rivas, J.L.2    Barber, J.3
  • 11
    • 0025034263 scopus 로고
    • In vitro studies on light-induced inhibition of photosystem II and D1-protein degradation at low temperatures
    • [11] E.V. Aro, T. Hundal, I. Carlberg, B. Andersson, In vitro studies on light-induced inhibition of photosystem II and D1-protein degradation at low temperatures, Biochim. Biophys. Acta 1019 (1990) 269-275.
    • (1990) Biochim. Biophys. Acta , vol.1019 , pp. 269-275
    • Aro, E.V.1    Hundal, T.2    Carlberg, I.3    Andersson, B.4
  • 12
    • 0026043886 scopus 로고
    • Photoinduced degradation of the D1 polypeptide in isolated reaction centers of photosystem II: Evidence for an autoproteolytic process triggered by the oxidizing side of the photosystem
    • [12] C.A. Shipton, J. Barber, Photoinduced degradation of the D1 polypeptide in isolated reaction centers of photosystem II: evidence for an autoproteolytic process triggered by the oxidizing side of the photosystem, Proc. Natl. Acad. Sci. USA 88 (1991) 6691-6695.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6691-6695
    • Shipton, C.A.1    Barber, J.2
  • 13
    • 0026695796 scopus 로고
    • On the molecular mechanism of light-induced D1 protein degradation in photosystem II core particles
    • [13] A.H. Salter, I. Virgin, A. Hagman, B. Andersson, On the molecular mechanism of light-induced D1 protein degradation in photosystem II core particles, Biochemistry 31 (1992) 3990-3998.
    • (1992) Biochemistry , vol.31 , pp. 3990-3998
    • Salter, A.H.1    Virgin, I.2    Hagman, A.3    Andersson, B.4
  • 14
    • 0029115182 scopus 로고
    • Degradation of antenna chlorophyll-binding protein CP43 during photoinhibition of photosystem II
    • [14] Y. Yamamoto, T. Akasaka, Degradation of antenna chlorophyll-binding protein CP43 during photoinhibition of photosystem II, Biochemistry 34 (1995) 9038-9045.
    • (1995) Biochemistry , vol.34 , pp. 9038-9045
    • Yamamoto, Y.1    Akasaka, T.2
  • 15
    • 0028859101 scopus 로고
    • Further characterization of the loss of antenna chlorophyll-binding protein CP43 from photosystem II during donor-side photoinhibition
    • [15] H. Mori, Y. Yamashita, T. Akasaka, Y. Yamamoto, Further characterization of the loss of antenna chlorophyll-binding protein CP43 from photosystem II during donor-side photoinhibition, Biochim. Biophys. Acta 1228 (1995) 37-42.
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 37-42
    • Mori, H.1    Yamashita, Y.2    Akasaka, T.3    Yamamoto, Y.4
  • 16
    • 0019873804 scopus 로고
    • Differential scanning calorimetry of chloroplast membranes: Identification of an endothermic transition associated with the water-splitting complex of photosystem II
    • [16] W.A. Cramer, J. Whitmarsh, P.S. Low, Differential scanning calorimetry of chloroplast membranes: identification of an endothermic transition associated with the water-splitting complex of photosystem II, Biochemistry 20 (1981) 157-162.
    • (1981) Biochemistry , vol.20 , pp. 157-162
    • Cramer, W.A.1    Whitmarsh, J.2    Low, P.S.3
  • 17
    • 0026688487 scopus 로고
    • Differential scanning calorimetric investigation of pea chloroplast thylakoids and thylakoid fractions
    • [17] W.G. Nolan, H.P. Hopkins Jr., S.A.M. Kalini Differential scanning calorimetric investigation of pea chloroplast thylakoids and thylakoid fractions, Arch. Biochem. Biophys. 297 (1992) 19-27.
    • (1992) Arch. Biochem. Biophys. , vol.297 , pp. 19-27
    • Nolan, W.G.1    Hopkins H.P., Jr.2    Kalini, S.A.M.3
  • 18
    • 0031670790 scopus 로고    scopus 로고
    • Effects of high temperatures on the photosynthetic systems in spinach: Oxygen-evolving activities, fluorescence characteristics and the denaturation process
    • [18] Y. Yamane, Y. Kashino, H. Koike, K. Satoh, Effects of high temperatures on the photosynthetic systems in spinach: oxygen-evolving activities, fluorescence characteristics and the denaturation process, Photosynth. Res. 57 (1998) 51-59.
    • (1998) Photosynth. Res. , vol.57 , pp. 51-59
    • Yamane, Y.1    Kashino, Y.2    Koike, H.3    Satoh, K.4
  • 19
    • 0023044274 scopus 로고
    • Differential scanning calorimetric studies of photosystem II: Evidence for a structural role for cytochrome b559 in the oxygen-evolving complex
    • [19] L.K. Thompson, J.M. Sturtevant, G.W. Brudvig, Differential scanning calorimetric studies of photosystem II: evidence for a structural role for cytochrome b559 in the oxygen-evolving complex, Biochemistry 25 (1986) 6161-6169.
    • (1986) Biochemistry , vol.25 , pp. 6161-6169
    • Thompson, L.K.1    Sturtevant, J.M.2    Brudvig, G.W.3
  • 21
    • 0028815284 scopus 로고
    • Forces and factors that contribute to the structural stability of membrane proteins
    • [21] T. Haltia, E. Freire, Forces and factors that contribute to the structural stability of membrane proteins, Biochim. Biophys. Acta 1228 (1995) 1-27.
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 1-27
    • Haltia, T.1    Freire, E.2
  • 22
    • 0032550293 scopus 로고    scopus 로고
    • Protein secondary structure and conformational changes of photosystem II during heat denaturation studied by Fourier transform-infrared spectroscopy
    • [22] H. Shi, L. Xiong, K.Y. Yang, C.Q. Tang, T.Y. Kuang, N.M. Zhao, Protein secondary structure and conformational changes of photosystem II during heat denaturation studied by Fourier transform-infrared spectroscopy, J. Mol. Struct. 446 (1998) 137-147.
    • (1998) J. Mol. Struct. , vol.446 , pp. 137-147
    • Shi, H.1    Xiong, L.2    Yang, K.Y.3    Tang, C.Q.4    Kuang, T.Y.5    Zhao, N.M.6
  • 23
    • 0030758135 scopus 로고    scopus 로고
    • Structure and thermal stability of photosystem II reaction centers studied by infrared spectroscopy
    • [23] J. De Las Rivas, J. Barber, Structure and thermal stability of photosystem II reaction centers studied by infrared spectroscopy, Biochemistry 36 (1997) 8897-8903.
    • (1997) Biochemistry , vol.36 , pp. 8897-8903
    • De Las Rivas, J.1    Barber, J.2
  • 24
    • 0000613359 scopus 로고    scopus 로고
    • Secondary structure and thermostability of the photosystem II manganese-stabilizing protein of the thermophilic cyanobacterium Synechococcus elongatus
    • [24] M. Sonoyama, A. Motoki, G. Okamoto, M. Hirano, H. Ishida, S. Katoh, Secondary structure and thermostability of the photosystem II manganese-stabilizing protein of the thermophilic cyanobacterium Synechococcus elongatus, Biochim. Biophys. Acta 1297 (1996) 167-170.
    • (1996) Biochim. Biophys. Acta , vol.1297 , pp. 167-170
    • Sonoyama, M.1    Motoki, A.2    Okamoto, G.3    Hirano, M.4    Ishida, H.5    Katoh, S.6
  • 26
    • 0027231960 scopus 로고
    • Distribution of the chlorophyll spectral forms in the chlorophyll-protein complexes of photosystem II antenna
    • [26] R.C. Jennings, R. Bassi, F.M. Garlaschi, P. Dainese, G. Zucchelli, Distribution of the chlorophyll spectral forms in the chlorophyll-protein complexes of photosystem II antenna, Biochemistry 32 (1993) 3203-3210.
    • (1993) Biochemistry , vol.32 , pp. 3203-3210
    • Jennings, R.C.1    Bassi, R.2    Garlaschi, F.M.3    Dainese, P.4    Zucchelli, G.5
  • 27
  • 28
    • 0030607901 scopus 로고    scopus 로고
    • Matrix and temperature effects on absorption spectra of β-carotene and pheophytin a in solution and in green plant photosystem II
    • [28] I. Renge, R. van Grondelle, J.P. Dekker, Matrix and temperature effects on absorption spectra of β-carotene and pheophytin a in solution and in green plant photosystem II, J. Photochem. Photobiol. A: Chem. 96 (1996) 109-121.
    • (1996) J. Photochem. Photobiol. A: Chem. , vol.96 , pp. 109-121
    • Renge, I.1    Van Grondelle, R.2    Dekker, J.P.3
  • 29
    • 0000946087 scopus 로고
    • Inactivation of photosynthetic oxygen evolution and concomitant release of three polypeptides in the photosystem II particles of spinach chloroplast
    • [29] T. Kuwabara, N. Murata, Inactivation of photosynthetic oxygen evolution and concomitant release of three polypeptides in the photosystem II particles of spinach chloroplast, Plant Cell Physiol. 23 (1982) 533-539.
    • (1982) Plant Cell Physiol. , vol.23 , pp. 533-539
    • Kuwabara, T.1    Murata, N.2
  • 30
    • 84989674854 scopus 로고
    • Organization of pigment-protein complexes into macrodomains in the thylakoid membranes of wild-type and chlorophyll b-less mutant of barley as revealed by circular dichroism
    • [30] G. Garab, J. Kieleczawa, J.C. Sutherland, C. Bustamante, G. Hind, Organization of pigment-protein complexes into macrodomains in the thylakoid membranes of wild-type and chlorophyll b-less mutant of barley as revealed by circular dichroism, Photochem. Photobiol. 54 (1991) 273-281.
    • (1991) Photochem. Photobiol. , vol.54 , pp. 273-281
    • Garab, G.1    Kieleczawa, J.2    Sutherland, J.C.3    Bustamante, C.4    Hind, G.5
  • 31
    • 0030042763 scopus 로고    scopus 로고
    • Methods to estimate the conformation of proteins and polypeptides from circular dichroism data
    • [31] N.J. Greenfield, Methods to estimate the conformation of proteins and polypeptides from circular dichroism data, Anal. Biochem. 235 (1996) 1-10.
    • (1996) Anal. Biochem. , vol.235 , pp. 1-10
    • Greenfield, N.J.1
  • 32
    • 0031004544 scopus 로고    scopus 로고
    • The application of circular dichroism to studies of protein folding and unfolding
    • [32] S.M. Kelly, N.C. Price, The application of circular dichroism to studies of protein folding and unfolding, Biochim. Biophys. Acta 1338 (1997) 161-185.
    • (1997) Biochim. Biophys. Acta , vol.1338 , pp. 161-185
    • Kelly, S.M.1    Price, N.C.2
  • 33
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer disease analysis of circular dichroism spectra
    • [33] C.J. Barrow, A. Yasuda, P.T.M. Kenny, M.G. Zagorski, Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer disease analysis of circular dichroism spectra, J. Mol. Biol. 225 (1992) 1075-1093.
    • (1992) J. Mol. Biol. , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Kenny, P.T.M.3    Zagorski, M.G.4
  • 34
    • 46549092122 scopus 로고
    • Excitation energy transfer, trapping and annihilation in photosynthetic systems
    • [34] R. van Grondelle, Excitation energy transfer, trapping and annihilation in photosynthetic systems, Biochim. Biophys. Acta 811 (1985) 147-195.
    • (1985) Biochim. Biophys. Acta , vol.811 , pp. 147-195
    • Van Grondelle, R.1
  • 36
    • 0028120542 scopus 로고
    • Size dependency of circular dichroism in macroaggregates of photosynthetic pigment-protein complexes
    • [36] V. Barzda, L. Mustardy, G. Garab, Size dependency of circular dichroism in macroaggregates of photosynthetic pigment-protein complexes, Biochemistry 33 (1994) 10837-10841.
    • (1994) Biochemistry , vol.33 , pp. 10837-10841
    • Barzda, V.1    Mustardy, L.2    Garab, G.3
  • 37
    • 0025183698 scopus 로고
    • D1-D2-cytochrome b559 complex from the aquatic plant Spirodela oligorrhiza: Correlation between complex integrity, spectroscopic properties, photochemical activity, and pigment composition
    • [37] P. Braun, B.M. Greenberg, A. Scherz, D1-D2-cytochrome b559 complex from the aquatic plant Spirodela oligorrhiza: correlation between complex integrity, spectroscopic properties, photochemical activity, and pigment composition, Biochemistry 29 (1990) 10376-10387.
    • (1990) Biochemistry , vol.29 , pp. 10376-10387
    • Braun, P.1    Greenberg, B.M.2    Scherz, A.3
  • 38
    • 0028046478 scopus 로고
    • Detergent-induced reversible denaturation of the photosystem II reaction center: Implications for pigment-protein interactions
    • [38] G. Montoya, R. Cases, R. Rodriguez, M. Aured, R. Picorel, Detergent-induced reversible denaturation of the photosystem II reaction center: implications for pigment-protein interactions, Biochemistry 33 (1994) 11798-11804.
    • (1994) Biochemistry , vol.33 , pp. 11798-11804
    • Montoya, G.1    Cases, R.2    Rodriguez, R.3    Aured, M.4    Picorel, R.5
  • 39
    • 0027299939 scopus 로고
    • Functionally important domains of the large hydrophilic loop of CP47 as probed by oligonucleotide-directed mutagenesis in Synechocystis sp. PCC 6803
    • [39] E. Haag, J.J. Eaton-Rye, G. Renger, W.F.J. Vermaas, Functionally important domains of the large hydrophilic loop of CP47 as probed by oligonucleotide-directed mutagenesis in Synechocystis sp. PCC 6803, Biochemistry 32 (1993) 4444-4454.
    • (1993) Biochemistry , vol.32 , pp. 4444-4454
    • Haag, E.1    Eaton-Rye, J.J.2    Renger, G.3    Vermaas, W.F.J.4
  • 40
    • 0028032823 scopus 로고
    • Functional characterization of mutant strains of the cyanobacterium Synechocystis sp. PCC 6803 lacking short domains within the large, lumen-exposed loop of the chlorophyll protein CP47 in photosystem II
    • [40] H.M. Gleiter, E. Haag, J.R. Shen, J.J. Eaton-Rye, Y. Inoue, W.F.J. Vermass, G. Renger, Functional characterization of mutant strains of the cyanobacterium Synechocystis sp. PCC 6803 lacking short domains within the large, lumen-exposed loop of the chlorophyll protein CP47 in photosystem II, Biochemistry 33 (1994) 12063-12701.
    • (1994) Biochemistry , vol.33 , pp. 12063-12701
    • Gleiter, H.M.1    Haag, E.2    Shen, J.R.3    Eaton-Rye, J.J.4    Inoue, Y.5    Vermass, W.F.J.6    Renger, G.7
  • 41
    • 0030852764 scopus 로고    scopus 로고
    • Mutational studies on conserved histidine residues in the chlorophyll-binding protein CP43 of photosystem II
    • [41] P. Manna, W. Vermaas, Mutational studies on conserved histidine residues in the chlorophyll-binding protein CP43 of photosystem II, Eur. J. Biochem. 247 (1997) 666-672.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 666-672
    • Manna, P.1    Vermaas, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.