• 현장농수산연구지
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• 제22권1호
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• pp.35-42
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• 2020

This study was conducted to investigate the photosystem II activities of Cercis chinensis by soil water condition. Drought stress was induced by withholding water and waterlogging treatments was immerging the pots for 15 days. Results showed that the relative activities per reaction center such as ABS/RC, TRo/RC and Dio/RC were significantly increased compared with the control group after 12 days in waterlogging treatments. Particularly, Dio/RC increased substantially under waterlogging stress, indicating that excessive energy was consumed by heat dissipation. Furthermore, the performance index on absorption basis(PI_abs) and responses to structural and functional PS II(SFI_abs) were dramatically decreased after 15 days in both the drought and waterlogging treatments, which reflects the relative reduction state of the photosystem II. These results of chlorophyll a fluorescence by OKJIP analysis show that the sensitive changes photosystem II activity. Thus, on the basis of our results that Cercis chinensis was exhibited a strong reduction of photosynthetic activity to waterlogging stress, and OKJIP parameters such as ABS/RC, DIo/RC, PI_abs and SFI_abs could be useful indicator to monitor the physiological states of Cercis chinensis under soil water condition.

• Journal of Photoscience
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• 제9권2호
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• pp.367-369
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• 2002

Chlorophyll (ChI) a' is the Cl3$^2$-epimer of ChI a which is the constituent of P700, the primary electron donor of Photosystem (PS) I, of a thrmophilic cyanobacterium, Synechococcus elongatus, whose structure was recently determined by X-ray crystallography. To determine whether PS I of diverse oxygenic photosynthetic organisms universally contain one molecule of ChI a ’, pigment compositions of thylakoid membranes and PS I complexes isolated from cyanobacteria, green algae, red algae and higher plants were determined by reversed-phase HPLC. The results show that involvement of one ChI a'molecule in PS I is the universal feature for Chi a-based PS I of oxygenic photosynthetic organisms.

• BMB Reports
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• 제32권2호
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• pp.189-195
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• 1999

From the Panax ginseng chloroplast, the psbE and psbF genes, encoding the $\alpha$- and $\beta$-subunits of cytochrome b-559 of the photosystem II reaction center, respectively, were cloned and characterized. The psbE and psbF genes were composed of 252 and 117 nucleotides, respectively. The deduced amino acid sequence of the $\alpha$-subunits showed 95%, 93%, and 91% homology to monocots, dicots, and liverwort, respectively, whereas the $\beta$-subunits showed approximately 98% to 95% homology to the same species. Southern blot analysis revealed that a single copy of the psbEF gene exists in the chloroplast plastid. Northern blot analysis indicated that the psbE and psbF genes are cotranscribed as a polycistron.

• Journal of Plant Biology
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• 제33권4호
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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.

• Journal of Photoscience
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• 제8권2호
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• pp.43-53
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• 2001

a, a parameter that describes how effectively photoinactivated PS II units protect their functional neighbours; car, carotenoids; ΔpH, transthylakoid pH difference; D1 protein, psbA gene product in the PS II reaction centre; f, functional fraction of PS II: F$\_$v//F$\_$m/, the ratio of variable to maximum chlorophyll a fluorescence; k$\_$d/, rate coefficient for degradation of D1 protein; k$\_$i/ and k$\_$r/, rate coefficient for photoinactivation and repair of PS II, respectively; NADP+, oxidized nicontinamide adenine dinucleotide phosphate; P680, the primary electron donor in the PSII reaction centre; Ph, pheophytin; PS, photosystem; Q$\_$A/, first quinone acceptor of an electron in PS II; R$\_$s/, the gross rate of D1 protein synthesis.

• Molecules and Cells
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• 제25권2호
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• pp.158-162
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• 2008

Recent molecular genetics studies have revealed that cyclic electron transport around photosystem I is essential for normal photosynthesis and growth of plants. Chloroplastic NAD(P)H dehydorgenase (NDH) complex, a homologue of the complex I in respiratory electron transport, is involved in one of two cyclic pathways. Recent studies on the function and structure of the NDH complex are reviewed.

• 한국식물학회:학술대회논문집
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• 한국식물학회 1999년도 Proceedings of the 17th Symposium on Plant Biology Environmental Stress and Photosynthesis
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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.

• Bulletin of the Korean Chemical Society
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• 제31권6호
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• pp.1479-1484
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• 2010

Photosynthesis uses light energy to drive the oxidation of water at an oxygen-evolving catalytic site within photosystem II (PSII). Chlorophyll binding by the photosystem II subunit S protein, PsbS, was found to be necessary for energy-dependent quenching (qE), the major energy-dependent component of non-photochemical quenching (NPQ) in Arabidopsis thaliana. It is proposed that PsbS acts as a trigger of the conformational change that leads to the establishment of nonphotochemical quenching. However, the exact structure and function of PsbS in PSII are still unknown. Here, we clone and express the recombinant PsbS gene from Arabidopsis thaliana in E. coli and purify the resulting homogeneous protein. We used various biochemical and biophysical techniques to elucidate PsbS structure and function, including circular dichroism (CD), fluorescence, and DSC. The protein shows optimal stability at $4^{\circ}C$ and pH 7.5. The CD spectra of PsbS show that the conformational changes of the protein were strongly dependent on pH conditions. The CD curve for PsbS at pH 10.5 curve had the deepest negative peak and the peak of PsbS at pH 4.5 was the least negative. The fluorescence emission spectrum of the purified PsbS protein was also measured, and the ${\lambda}_{max}$ was found to be at 328 nm. PsbS revealed some structural changes under varying temperature and oxygen gas condition.

• Journal of Photoscience
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• 제9권2호
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• pp.385-387
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• 2002

Direct EPR evidence of the photo-generation of superoxide radicals ( $O_2$$^{-.}$) was obtained by using spin trapping techniques in spinach photosystem II (PSII) membranes. $O_2$$^{-.}$ was detected by following the formation of 5-diethoxyphosphoryl-5-methyl-1 -pyrroline-N-oxide (DEPMPO) superoxide adducts, DEPMPO-OOH. The significant increase of the EPR signal amplitude of DEPMPO-OOH in N$H_2O$H-, CaC $l_2$- and NaCl-treated PSII membranes showed that the oxygen-evolving system has a close relation to the $O_2$$^{-.}$ production. PSII membranes with inactivated donor side could not prevent the $O_2$$^{-.}$ production efficiently. Treatments on PSII donor side also influence the maximum level and the kinetics of Chlorophyll (Chi) a fluorescence. Results suggested that manganese cluster and extrinsic proteins might affect Chi a fluorescence in ways different from that happens at the acceptor side of PSII.SII.SII.

• BMB Reports
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• 제40권5호
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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.