• Title/Summary/Keyword: pigment-protein complex

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Effects of Chilling Injury in the Light on Chlorophyll Fluorescence and D1 Protein Turnover in Cucumber and Pea Leaves

  • Eu, Young-Jae;Ha, Suk-Bong;Lee, Choon-Hwan
    • BMB Reports
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    • v.29 no.5
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    • pp.398-404
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    • 1996
  • Light-chilling effects were investigated in chilling-sensitive cucumber (Cucumis sativus L. cv. Ilmichungjang) and chilling-resistant pea (Pisum sativum L. cv. Giant) leaf discs in relation to possible damage in D1 protein. In both plants, dark-chilling did not cause any noticeable changes in (Fv)m/Fm and lincomycin did not affect the decrease in (Fv)m/Fm caused by light-chilling. This result suggests that the de novo synthesis of D1 protein did not occur actively during light-chilling. In pea light-chilled for 6 h. the decreased (Fv)m/Fm was partly recovered in the dark, and almost complete recovery was observed in the light. In cucumber light-chilled for 3 h. the reduced (Fv)m/Fm decreased further for the initial 2 h recovery process in the light regardless of the treatment of lincomycin and recovered very slowly. In both plant species, the treatment of lincomycin inhibited the recovery process in the light, but did not significantly inhibit the process in the dark. In cucumber leaves pulse-labeled with $[^{35}S]Met$, the labeled band intensities of isolated pigment-protein complexes were almost the same during the 6 h light-chilling, but significant decreases in band intensities were observed during the 3 h recovery period. This result suggests that the irreversibly damaged D1 protein was degraded during the recovery period. However, no noticeable changes were observed in the pea leaves during the 12 h chilling and 3 h recovery period. The polyacrylamide gel electrophoresis of the pigment-protein complexes showed that the principal lesion sites of light-chilling were different from those of room temperature photoinhibition.

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Excitonic Energy Transfer of Cryptophyte Phycocyanin 645 Complex in Physiological Temperature by Reduced Hierarchical Equation of Motion

  • Lee, Weon-Gyu;Rhee, Young Min
    • Bulletin of the Korean Chemical Society
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    • v.35 no.3
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    • pp.858-864
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    • 2014
  • Recently, many researches have shown that even photosynthetic light-harvesting pigment-protein complexes can have quantum coherence in their excitonic energy transfer at cryogenic and physiological temperatures. Because the protein supplies such noisy environment around pigments that conventional wisdom expects very short lived quantum coherence, elucidating the mechanism and searching for an applicability of the coherence have become an interesting topic in both experiment and theory. We have previously studied the quantum coherence of a phycocyanin 645 complex in a marine algae harvesting light system, using Poisson mapping bracket equation (PBME). PBME is one of the applicable methods for solving quantum-classical Liouville equation, for following the dynamics of such pigment-protein complexes. However, it may suffer from many defects mostly from mapping quantum degrees of freedom into classical ones. To make improvements against such defects, benchmarking targets with more accurately described dynamics is highly needed. Here, we fall back to reduced hierarchical equation of motion (HEOM), for such a purpose. Even though HEOM is known to applicable only to simplified system that is coupled to a set of harmonic oscillators, it can provide ultimate accuracy within the regime of quantum-classical description, thus providing perfect benchmark targets for certain systems. We compare the evolution of the density matrix of pigment excited states by HEOM against the PBME results at physiological temperature, and observe more sophisticated changes of density matrix elements from HEOM. In PBME, the population of states with intermediate energies display only monotonically increasing behaviors. Most importantly, PBME suffers a serious issue of wrong population in the long time limit, likely generated by the zero-point energy leaking problem. Future prospects for developments are briefly discussed as a concluding remark.

Association between a M-Iacking mutant D75N of pharaonis phoborhodopsin and its transducer is stronger than the complex of the wild-type pigment: Implication of the signal transduction

  • Sudo, Yuki;Iwamoto, Masayuki;Shimono, Kazumi;Kamo, Naoki
    • Journal of Photoscience
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    • v.9 no.2
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    • pp.314-316
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    • 2002
  • In halobacterial membrane, pharaonis phoborhodopsin (or pharaonis sensory rhdopsin II, psRII) forms a complex with its transducer pHtrII. Flash-photolyis of D75N mutant did not yield M-intermediate but an O-like intermediate is observed. We examined the interaction between D75N of ppR and t-Htr (truncated pHtrII). These formed a complex in the presence of n-dodecyl-$\beta$-D-maltoside, and the association accelerated the decay of the 0 of D75N from 15 to 56 s$\^$-1/. From the decay time constants under varying ratios of D75N and t-Htr, n, the molar ratio of D75N/t-Htr in the complex, and K$\_$D/, the dissociation constant, were estimated. The value of n was unity and K$\_$D/ was estimated to 146 nM. This K$\_$D/ value can be considered as the association between the photo-intermediate and t-Htr, which is deduced by the method of estimation. Previously we (Photochem. Photobiol. 74, 489-494 (2001)) reported K$\_$D/ of 15 $\mu$M for the interaction between the wild-type and t-Htr by means of the change of M-decay rates. Therefore, this value should be the K$\_$D/ value for the interaction between M of the wild-type and t-Htr.

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Comparative modeling of human tyrosinase - An important target for developing skin whitening agents (사람 티로시나제의 3차원 구조 상동 모델링)

  • Choi, Jong-Keun;Suh, Joo-Won
    • Proceedings of the KAIS Fall Conference
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    • 2012.05a
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    • pp.182-186
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    • 2012
  • human tyrosinase (hTyr) catalyzes first and the rate limiting step in the synthesis of polymerized pigment, melanin which determines skin, hair and eye colors. Mutation of hTyr often brings about decrease of melanin production and further albinism. Meanwhile, a number of cosmetic companies providing skincare products for woman in Asia-Pacific region have tried to develop inhibitors to bright skin color for several decades. In this study, we built a 3D structure by comparative modeling technique based on the crystal structure of tyrosinase from bacillus megaterium as a template to serve structural information of hTyr. According to our model and sequence analysis of type 3 copper protein family proteins, two copper atoms of active site located deep inside are coordinated with six strictly conserved histidine residues coming from four-helix-bundle. Cavity which accommodates substrates was like funnel shape of which entrance was wide and expose to solvent. In addition, protein-substrate and protein-inhibitor complex were modeled with the guide of van der waals surface generated by in house software. Our model suggested that only phenol group or its analogs can fill the binding site near nuclear copper center because inside of binding site has narrow shape relatively. In conclusion, the results of this study may provide helpful information for designing and screening new anti-melanogensis agents.

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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.

Effect of Lipid on the Protein Denaturation in Cooking Fish Meat (어육 조리시 지질이 단백질 변성에 미치는 영향)

  • LEE Kang-Ho;CHOI Byeong-Dae;RYU Hong-Soo
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.19 no.5
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    • pp.493-501
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    • 1986
  • The present work aims to estimate the effect of heat treatment on the in vitro protein digestibility and formation of trypsin inhibitor or trypsin indigestible substrate(TIS) of raw and defatted flounder. It was also carried out to assess the formation of lipid-protein complexes under the conditions of different ratio of lipid addition. The in vitro protein digestibility increased when steamed for 5 min showing $88.09\%$ in raw and $90.56\%$ in defatted samples, respectively. After 40 min steaming, the digestibility decreased by $2{\sim}4\%$. As for microwaving, heating for 1 min resulted in slight increase of digestibility, however, heating for 7 min did decrease of digestibility by $3{\sim}4\%$ for both raw and defatted materials. There was no difference in fatty acid composition found with heat treatment. The major fatty acids of flounder meat were $C_{16:0},\;C_{16:1},\;C_{18:1},\;C_{20:5},\;C_{22:6}$ and the ratio of the unsaturated to saturated was 67.3:32.6. Fat oxidation and nonenzymatic browning were enhanced by heat treatment and protein solubility decreased necessarily as the brown pigment formation increased. On the other hand, the effects on the digestibility and TIS of the complexes formed from interaction of lipid and myofibrillar or meat protein of flounder were examined. The interaction of protein with lipid was considered to mostly contribute to the drop of digestibility of fish products. The digestibility of myofibrillar protein was $93.72\%$ for flounder, and it generally decreased as the amount of lipid added to protein and reaction time increased. Also mixed and heated samples were more active in digestibility decline than those mixed after heating. The result probably indicated that lipid-protein interaction was involved in the drop of digestibility which coincided with protein denaturation.

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Variation in the Size of Light Harvesting 1 of Purple Bacteria

  • Akiyama, Machiko;Nagashima, Kenji V.P.;Inoue, Ryouji;Wakayama, Tatsuki;Kise, Hideo;Hara, Masayuki;Kobayashi, Masami
    • Journal of Photoscience
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    • v.9 no.2
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    • pp.350-352
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    • 2002
  • We examined the bacteriochlorophyill/bacteriopheophytin ratios in several species of purple bacteria containing only LHI. The pigment ratios depended greatly on species. Further, Rhodospirillum rubrum showed wide variation when grown under different light intensity, and Rhodobium marinum showed significant variation from culture to culture even under the same light conditions. The protein ratios of a/RC and $\beta$/RC estimated by SDS-PAGE of chromatophores of Rsp. rubrum and Rbi. marinum exhibited the ratio of $\beta$/$\alpha$ > 1. These findings gave us the novel idea that there are two types of LHl; one is a C-shaped open antenna composed by $\alpha$$\beta$ units surrounding a RC, and another is a small closed ring antenna composed by $\alpha$$\beta$ units located peripherally in a variable ratio to the core complex like LH2.

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A Strategy for Quality Poultry Egg Production II. Egg Interior Quality; Cholesterol Content, Egg Yolk Pigmentation, Controlling Egg weight and Organic Eggs (양질의 계란 생산전략 II. 계란내용물의 질, 콜레스테롤 함량, 난황색, 난중조절, 유기란)

  • 남기홍
    • Korean Journal of Poultry Science
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    • v.27 no.2
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    • pp.133-153
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    • 2000
  • The egg's interior quality is one of the most important criteria for commercial producers and consumers. Internal quality is complex, including aesthetic factors such as taste, freshness, nutritional and processing values, and the genetic influences upon these upon these factors ranges from none to considerable. The rate of cholesterol synthesis in the hen is very high compared to other animals and humans. Genetic selection, diet drugs and other chemicals can alter cholesterol concentration in the plasma of laying hen, but attempts to manipulate the cholesterol concentration in the egg yolk are generally unsuccessful since the cholesterol can only be changed to a small extent. Factors which may affect the degree of pigmentation of the yolk include the type of xanthophyll and its concentration in the feed, the feed composition, and the health of the hen. Several feed ingredients interact with carotenoid pigment to improve or reduce their deposition rates in yolks. Egg weight is determined by genetics, body size prior to first egg housing density, environmental temperature, lighting program, total feed consumption, calcium, phosphorus, niacin, water, methionine, total sulfur amino acids, energy, linoleic acid, fat and protein levels. Eggs need to be promote levels. Eggs need to be promoted a versatile commodity and new processed egg items need to be developed. Organic eggs are laid by hens which were raised in chemical and drug frdd environments. There are still difficulties in producing these eggs due to the availability of organic poultry feeds and cost of organic grains.

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Comparative proteome profiling in the storage root of sweet potato during curing-mediated wound healing (큐어링 후 저장에 따른 고구마 저장뿌리 단백질체의 비교분석)

  • Ho Yong Shin;Chang Yoon Ji;Ho Soo Kim;Jung-Sung Chung;Sung Hwan Choi;Sang-Soo Kwak;Yun-Hee Kim;Jeung Joo Lee
    • Journal of Plant Biotechnology
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    • v.50
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    • pp.1-10
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    • 2023
  • Sweet potato (Ipomoea batatas L. Lam) is an economically important root crop and a valuable source of nutrients, processed foods, animal feeds, and pigment materials. However, during post-harvest storage, storage roots of sweet potatoes are susceptible to decay caused by various microorganisms and diseases. Post-harvest curing is the most effective means of healing wounds and preventing spoilage by microorganisms during storage. In this study, we aimed to identify proteins involved in the molecular mechanisms related to curing and study proteomic changes during the post-curing storage period. For this purpose, changes in protein spots were analyzed through 2D-electrophoresis after treatment at 33℃ (curing) and 15℃ (control) for three days, followed by a storage period of eight weeks. As a result, we observed 31 differentially expressed protein spots between curing and control groups, among which 15 were identified. Among the identified proteins, the expression level of 'alpha-amylase (spot 1)' increased only after the curing treatment, whereas the expression levels of 'probable aldo-keto reductase 2-like (spot 3)' and 'hypothetical protein CHGG_01724 (spot 4)' increased in both the curing and control groups. However, the expression level of 'sporamin A (spot 10)' decreased in both the curing and control treatments. In the control treatment, the expression level of 'enolase (spot 14)' increased, but the expression levels of 'chain A of actinidin-E-64 complex+ (spot 19)', 'ascorbate peroxidase (spot 22)', and several 'sporamin proteins (spot 20, 21, 23, 24, 27, 29, 30, and 31)' decreased. These results are expected to help identify proteins related to the curing process in sweet potato storage roots, understand the mechanisms related to disease resistance during post-harvest storage, and derive candidate genes to develop new varieties with improved low-temperature storage capabilities in the future.