• Journal of Photoscience
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• v.9 no.2
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• pp.382-384
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• 2002

When illuminated with strong visible light, the reaction center Dl protein of photo system II is photodamage and degraded. Reactive oxygen species and endogenous cationic radicals generated by photochemical reactions are the cause of the damage to the Dl protein. Recently we found that the photodamaged Dl protein cross-links with the surrounding polypeptides such as D2 and CP43 in photosystem II. As the cross-linking reaction is dependent on the presence of oxygen, reactive oxygen species are suggested to be involved. Among the reactive oxygen species examined, ？ OH was most effective in the formation of the cross-linked products. These results indicate that the cross-linking is mostly due to ？ OH generated at photosystem II. The cross-linking site of the Dl protein is not known. As several tyrosine residues exist at the D­E loop of the Dl protein, there is a possibility that di-Tyr is formed between the D­E loop of the Dl protein and surrounding polypeptides during the strong illumination. Therefore, we examined the formation of di-Tyr using the monoclonal antibody against di-Tyr under excess illumination of the photosystem II membranes. The results obtained here suggest that no di-Tyr is formed during the excess illumination of photosystem II.

• BMB Reports
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• v.32 no.2
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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 Photoscience
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• v.9 no.2
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• pp.55-58
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• 2002

The reaction center Dl protein of photosystem II is the target of photodamage by excess illumination. The Dl protein is damaged by reactive oxygen species generated by photochemical reactions and then degraded by specific proteolytic enzymes. We found that the Dl protein also cross-links with the surrounding polypeptides, such as D2 and CP43 in isolated thylakoids or photosystem II-enriched membranes from spinach under the illumination with strong visible light. The cross-linking was observed in spinach leaf discs as well when they were illuminated at higher temperature (40°C). It was also shown that the cross-linked products are digested efficiently by a protease(s) in the stroma. Thus the cross-linking/digestion processes of the Dl protein seem to comprise a new pathway in the turnover of the photodamaged Dl protein. It should be noted, however, that the cross-linked products of the Dl protein and CP43 induced by endogenous cationic radicals in the donor-side photoinhibition are resistant to proteolytic digestion. Accumulation of these cross-linked products in the thylakoids may lead to the decay of the function of chloroplasts and finally to the death of plant cells. Thus, we suggest that the quality control of photosystem II, especially removal of the cross-linked products of the Dl protein, is crucial for the survival of chloroplasts under the light stress.

• Proceedings of the Zoological Society Korea Conference
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• 1995.10b
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• pp.277.2-277
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• 1995

No Abstract, See Full Text

• BMB Reports
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• v.29 no.1
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• pp.58-62
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• 1996

The structural changes in the electron donor side of the PSII reaction center have been monitored since heat treatment ($45^{\circ}C$ for 5 min) of thylakoids is known to decrease the oxygen evolving activity. In heat-treated spinach chloroplast thylakoids, the inhibitory effect of 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU) on the electron transport activity of the PSII reaction center from diphenyl carbazide to dichlorophenolindophenol became reduced approximately 3.8 times and [$^{14}C$]-labeled DCMU binding on the D1 polypeptide decreased to 25~30% that of intact thylakoid membranes, implying that the conformational changes of the DCMU binding pocket, residing on the D1 polypeptide, occur by heat treatment. The accessibility of trypsin to the $NH_2$-terminus of the cytochrome b-559 ${\alpha}$-subunit, assayed with Western blot using an antibody generated against the synthetic peptide (Arg-68 to Arg-80) of the COOH-terminal domain, was also increased, indicating that heat-treatment caused changes in the structural environments near the stromal side of the cytochrome b-559 ${\alpha}$-subunit, allowing trypsin more easily to cleave the $NH_2$-terminal domain. Therefore, the structural changes in the electron donor side of the PSII reaction center complexes could be one of the reasons why the oxygen evolving activity of the heat-treated thylakoid membranes decreased.

• Journal of Photoscience
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• v.9 no.2
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• pp.70-73
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• 2002

A cyanobacteria-like organism Aaryochloris marina performs oxygenic photosynthesis with near far-red light by the use of chlorophyll d. Reaction center chlorophyll (Chl) of Photosystem (PS) II of A. marina was studied by analysis of millisecond-delayed fluorescence. Delayed fluorescence is emitted by Chi d indicating efficient energy transfer between antenna Chi d molecules and the unknown primary electron donor of PS II. P740 a reaction center Chl of PS I of A. marina is shown to give a dimer type cation, and triplet state with a D value of 245xlO$\^$-4/ cm$\^$-l/ in contrast to the 280-290 xlO$\^$-4/cm$\^$-l/ values of P700 suggesting triplet spins interacting at a 5% larger distance in P740 than in P700.

• 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.

• Journal of Practical Agriculture & Fisheries Research
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• v.22 no.1
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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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• v.7 no.3
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• pp.87-95
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• 2000

As sunlight not always optimized for every terrestrial plant in terms of light quality, quantity and duration, some plants suffer detrimental effects of sunlight exposure under certain conditions. Photoinhibition of photosynthesis is a typical phenomenon representing harmful light effects, commonly observed in many photosynthetic organisms. It is generally accepted that functional, structural loss of photosystem II complex(PSII) is the primary event of photoinhibition. Accumulating data also suggest that singlet oxygen($^1$O$_2$) is the main toxic species directly involved in it. There are two different views on the specific site and mechanism of $^1$O$_2$ production in the photosynthetic membrane. One of them favors the PSII reaction center, where the primary charge pairs recombination occurs as a prerequisite for the generation of $^1$O$_2$, and the other inclines to photosensitized $^1$O$_2$ formation by a substance located outside PSII. This article describes how we, as the advocators of the latter concept, have arrived at the conclusion that $^1$O$_2$ immediately involved in PSII photodamage is largely generated from the Rieske center of the cytochrome b$_{6}$/f complex and diffuses into PSII, attacking the reaction center subunits.s.

• 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.