• Title/Summary/Keyword: photosystem II complex

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Differential Recovery of Photosystem II Complex from Low-Temperature Photoinhibition in Plants with Different Chilling Sensitivity

  • Moon, Byoung-Yong;Norio Murata
    • Journal of Photoscience
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    • v.7 no.2
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    • pp.39-44
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    • 2000
  • To examine the chilling tolerance lipids, we compared the chilling susceptibility of photosystem II of wild type tobacco plants with that of transgenic tobacco plants, in which the sensitivity to chilling had been enhanced by genetic modification of fatty acid unsaturation of chloroplast membrane lipids. The transgenic tobacco plants were found to contain reduced levels of unsaturated membrane fatty acids by being tansformed with cDNA for glycerol-3-phosphate acyltransferase from squash. For the purpose of studying on the functional integrity of photosystem II during low-temperature photoinhibition, the photochemical efficiency was measured as the ration of the maximun fluorescence of chlorophyll (Fv/Fm) of photosystem II. In parallel with an investigation on the transgenic plants, susceptibility of chilling-resistant species, such as spinah and pea, and of chilling-sensitive ones, such as squash and sweet potato, to low-temperature photoinhibition was also compared in terms of room temperature-induced chlorophyll fluorescence from photosystem II. When leaf disks from the two genotypes of tobacco plants were exposed to light at 5$^{\circ}C$, the transgenic plants showed more rapid decline in photochemical activity of photosysytme II than wild-type plants. When they were pretreated with lincomycin, an inhibitor of chloroplast-encoded protein synthesis, the extent of photoinhibition was even more accelerated. More impottantly, they showed a comparable extent of photoinhibition in the presence of lincomycin, making a clear contrast to the discrepancy observed in the discrepancy observed in the absence of lincomycin. Restoration of Fv/Fm during recovery from low-temperature photoinhibition occurred more slowly in the transgenic tobacco plants than the wild-type. These findings are discussed in relation to fatty acid unsaturation of membrane phosphatidylglycerol. It appears that the ability of plants to rapidly regenerate the active photosystem II complex from might explain, in part, why chilling-resistant plants can toleratlow-temperature photoinhibition.

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Studies on Inactivation and Reactivation of Isolated Photosystem II Complexes in Spinach (시금치에서 분리한 광계 2 복합체의 불활성화와 재활성화에 대한 연구)

  • 전현식
    • Journal of Plant Biology
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    • v.33 no.4
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    • pp.277-283
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    • 1990
  • Inactivation and reactivation of photosynthetic oxygen evolving complex were studied with isolated spinach (Spinacia oleraceda. L.) photosystem II particles by the activity of oxygen evolution and chlorophyll fluorescence. When the particles were treated with Tris and urea, the oxygen evolution was inactivated and three polypeptides having molecular weights of 33 kDa, 24 kDa and 18 kDa were simultaneously released. But in NaCl-treated particles, two polypeptides of 24 kDa and 18 kDa were removed from PS II particles. The oxygen evolution activities of Tris and urea-treated particles were not restored by adding cation ions (Mg2+, Mn2+ and Ca2+), but the NaCl-treated particles were restored by exogenously added Ca2+. The removal of these extrinsic polypeptides, especially 33 kDa, markedly showed the decrease of the variable fluorescence (Fv). These results are likely to be due to dissipate thermal energy by antenna of photosystem II complexes.

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The first insight into the structure of the Photosystem II reaction centre complex at $6{\AA}$ resolution determined by electron crystallography

  • Rhee, Kyong-Hi
    • Proceedings of the Botanical Society of Korea Conference
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    • 1999.08a
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    • pp.83-90
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    • 1999
  • Electron crystallography of two-dimensional crystalsand electron cryo-microscopy is becoming an established method for determining the structure and function of a variety of membrane proteins that are providing difficult to crystallize in three dimension. In this study this technique has been used to investigate the structure of a ~160 kDa reaction centre sub-core complex of photosystem II. Photosystem II is a photosynthetic membrane protein consisting of more than 25 subunits. It uses solar energy to split water releasing molecular oxygen into the atmosphere and creates electrochemical potential across the thylakoid membrane, which is eventually utilized to generate ATP and NADPH. Images were taken using Philips CM200 field emission gun electron microscope with an acceleration voltage of 200kW at liquid nitrogen temperature. In total, 79 images recorded dat tilt angles ranging from 0 to 67 degree yielded amplitudes and phases for a three-dimensional map with an in-plant resolution of 6$\AA$ and 11.4$\AA$ in the third dimension shows at least 23 transmembrane helices resolved in a monomeric complex, of which 18 were able to be assigned to the D1, D2, CP47 , and cytochrome b559 alfa beta-subunits with their associated pigments that ae active in electron transport (Rhee, 1998, Ph.D.thesis). The D1/D2 heterodimer is located in the central position within the complex and its helical scalffold is remarkably similar to that of the reaction centres not only in purple bacteria but also in plant photosystem I (PSI) , indicating a common evoluationary origin of all types of reaction centre in photosynthetic organism known today 9RHee et al. 1998). The structural homology is now extended to the inner antenna subunit, ascribed to CP47 in our map, where the 6 transmembrane helices show a striking structural similarity to the corresponding helices of the PSI reaction centre proteins. The overall arrangement of the chlorophylls in the D1 /D2 heterodimer, and in particular the distance between the central pair, is ocnsistent with the weak exciton coupling of P680 that distinguishes this reaction centre from bacterial counterpart. The map in most progress towards high resolution structure will be presented and discussed.

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Characteristics of Light Harvesting Chlorophyll-Protein Complex and Singlet Oxygen ($^1O_2$) Quenching in Leaf-burning Disease from Panax ginseng C. A. Meyer (인삼 Light Harvesting Chlorophyll Protein의 특성 및 엽소병에서 Singlet Oxygen($^1O_2$) Quenching)

  • 양덕조;이성택
    • Journal of Ginseng Research
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    • v.13 no.2
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    • pp.158-164
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    • 1989
  • In order to determine the relationships between the lea(-burning disease and the light harvesting chlorophyll-protein (LHCP) complex in Panax ginseng C. A. Meyer, we investigated the chlorophyll-protein (CP) complex of the thylakoid membrane and its characteristics. In P. ginseng four Cp-complex bands determined by non-denaturing SDS-PAGE were identified CP I'(containing reaction center of photosystem I and LHCP I antennae), CP I (reaction center of photosystem I) LHCP II** (oligoform of LHCP II), and LHCP II (photosystem II antennae, CP 26 and CP 29) by Bassis and Dunahay's procedures. Under our experimental condition, the CP I band was only observed in P. ginseng and the band intensity of LHCP II** in P ginseng was higher than in spinach and soybean. There were differences in the absorption and fluorescence spectra and chlorophyll a/b ratio of the CP-complex bands between P. ginseng and other Plants. The Polypeptidr content of P. ginseng thylakoid was lower than in spinach and soybean thylakoid, and the Polypeptide profiles of P. ginseng was low band intensity, especially about 29-35 kD, 55 kD, and 60 kD, compared to spinach and soybean. The inhibitory effects of 2,5-dimethylfuran, specific singlet oxygen ($^1O_2$) quencher, showed that singlet oxygen destroyed 60% of chl.a, 90% of chl.b and 70% of carotenoid in bleaching P. ginseng with leaf-burning disease.

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Mobilization of Photosystem II-Light Harvesting Complex II Supercomplexes during High Light Illumination and State Transitions

  • Nath, Krishna;Elizabeth, John;Poudyal, Roshan Sharma;Ko, Su Yeon;Lim, Woon Ki;Lee, Choon-Hwan
    • Rapid Communication in Photoscience
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    • v.2 no.1
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    • pp.18-23
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    • 2013
  • The photosystem II (PSII) light harvesting complex (LHC) consists of a variety of pigment protein complexes which are involved in structural organization and regulation of photosynthetic unit. These LHC proteins encoded by a group of Lhcb genes are essential for the structural integrity of PSII supercomplex, the channeling the excitation energy to the reaction center of PSII and its redistribution to photosystem I by state transitions. Numerous studies with the help of recent technological advancements have enabled a significant progress in our understanding on the structure of PSII-LHCII supercomplexes and their mobilization under various light conditions. Here, we present a mini-review on the latest concepts and models depicting the structure of PSII-LHCII supercomplexes and the role of Lhcb proteins in their supra-molecular organization. Also we will review on the current understandings and remaining problems involved in the mobilization of the supercomplexes during state transitions and during high light illumination for controlling light energy distribution between the two photosystems.

Photoinhibition Induced Alterations in Energy Transfer Process in Phycobilisomes of PS II in the Cyanobacterium, Spirulina platensis

  • Kumar, Duvvuri Prasanna;Murthy, Sistla D.S.
    • BMB Reports
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    • v.40 no.5
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    • pp.644-648
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    • 2007
  • Exposure of algae or plants to irradiance from above the light saturation point of photosynthesis is known as high light stress. This high light stress induces various responses including photoinhibition of the photosynthetic apparatus. The degree of photoinhibition could be clearly determined by measuring the parameters such as absorption and fluorescence of chromoproteins. In cyanobacteria and red algae, most of the photosystem (PS) II associated light harvesting is performed by a membrane attached complex called the phycobilisome (PBS). The effects of high intensity light (1000-4000 ${\mu}mol$ photons $m^{-2}s^{-1}$) on excitation energy transfer from PBSs to PS II in a cyanobacterium Spirulina platensis were studied by measuring room temperature PC fluorescence emission spectra. High light (3000 ${\mu}mol$ photons $m^{-2}s^{-1}$) stress had a significant effect on PC fluorescence emission spectra. On the other hand, light stress induced an increase in the ratio of PC fluorescence intensity of PBS indicating that light stress inhibits excitation energy transfer from PBS to PS II. The high light treatment to 3000 ${\mu}mol$ photons $m^{-2}s^{-1}$ caused disappearance of 31.5 kDa linker polypeptide which is known to link PC discs together. In addition we observed the similar decrease in the other polypeptide contents. Our data concludes that the Spirulina cells upon light treatment causes alterations in the phycobiliproteins (PBPs) and affects the energy transfer process within the PBSs.

Properties of $Cl^-$ Binding Site in Oxygen-Evolving Complex of Photosystem II Studied by FTIR Spectroscopy

  • Koji Hasegawa;Kim, Yukihiro ura;Asako Ishii;Jun Minagawa;Ono, Taka-aki
    • Journal of Photoscience
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    • v.9 no.2
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    • pp.376-378
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    • 2002
  • Role of cl$^{[-10]}$ in photosynthetic oxygen-evolving complex was studied by light-induced Fourier transform infrared (FTIR) spectroscopy. cl$^{[-10]}$ depletion resulted in the suppression of amide I and amide II IR modes upon S$_1$ to S$_2$ transition. Br$^{[-10]}$ , 1$^{[-10]}$ and N0$_3$$^{[-10]}$ substituted FTIR difference spectra were very similar to that in cl$^{[-10]}$ reconstitution. F$^{[-10]}$ and $CH_3$COO$^{[-10]}$ substituted spectra were largely distorted. We succeeded in detecting the structural change of N0$_3$ $^{[-10]}$ in the cl$^{[-10]}$ site upon the S$_1$ to S$_2$ transition from $^{14}$ N0$_3$$^{[-10]}$ /$^{15}$ N0$_3$$^{[-10]}$ difference spectrum.

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Studies on The Molecular Mechanism of 33 kDa extrinsic Protein in Photosystem II Oxygen-Evolving Complex

  • Xu, Chunhe;Ruan, Kangcheng;Yu, Yong;Weng, Jun
    • Journal of Photoscience
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    • v.9 no.2
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    • pp.82-85
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    • 2002
  • 33kDa extrinsic protein, an important protein in oxygenic photosynthesis, was known to have no fixed configuration in solution. At 20$\^{C}$ and pH 6, 33kDa extrinsic protein showed changes of free energy of -14.6 kJ/mor$\^$-1/ and of standard volume of -120mL/mol, respectively, with increase of hydrostatic pressure, comparatively lower than for most proteins. NBS modification of Trp241 in 33kDa extrinsic protein dramatically changes the secondary protein structure, its affinity to photosystem II as well as photosynthetic oxygen evolution. The relationship between structural change and transport of oxygen, water and proton is deserved a further study.

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