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Journal articles on the topic 'LHCI'

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Author: Grafiati

Published: 11 March 2023

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1

Rathod, Mithun Kumar, Sreedhar Nellaepalli, Shin-Ichiro Ozawa, Hiroshi Kuroda, Natsumi Kodama, Sandrine Bujaldon, Francis-André Wollman, and Yuichiro Takahashi. "Assembly Apparatus of Light-Harvesting Complexes: Identification of Alb3.1–cpSRP–LHCP Complexes in the Green Alga Chlamydomonas reinhardtii." Plant and Cell Physiology 63, no. 1 (October 1, 2021): 70–81. http://dx.doi.org/10.1093/pcp/pcab146.

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Abstract The unicellular green alga, Chlamydomonas reinhardtii, contains many light-harvesting complexes (LHCs) associating chlorophylls a/b and carotenoids; the major LHCIIs (types I, II, III and IV) and minor light-harvesting complexes, CP26 and CP29, for photosystem II, as well as nine LHCIs (LHCA1–9), for photosystem I. A pale green mutant BF4 exhibited impaired accumulation of LHCs due to deficiency in the Alb3.1 gene, which encodes the insertase involved in insertion, folding and assembly of LHC proteins in the thylakoid membranes. To elucidate the molecular mechanism by which ALB3.1 assists LHC assembly, we complemented BF4 to express ALB3.1 fused with no, single or triple Human influenza hemagglutinin (HA) tag at its C-terminus (cAlb3.1, cAlb3.1-HA or cAlb3.1–3HA). The resulting complemented strains accumulated most LHC proteins comparable to wild-type (WT) levels. The affinity purification of Alb3.1-HA and Alb3.1–3HA preparations showed that ALB3.1 interacts with cpSRP43 and cpSRP54 proteins of the chloroplast signal recognition particle (cpSRP) and several LHC proteins; two major LHCII proteins (types I and III), two minor LHCII proteins (CP26 and CP29) and eight LHCI proteins (LHCA1, 2, 3, 4, 5, 6, 8 and 9). Pulse-chase labeling experiments revealed that the newly synthesized major LHCII proteins were transiently bound to the Alb3.1 complex. We propose that Alb3.1 interacts with cpSRP43 and cpSRP54 to form an assembly apparatus for most LHCs in the thylakoid membranes. Interestingly, photosystem I (PSI) proteins were also detected in the Alb3.1 preparations, suggesting that the integration of LHCIs to a PSI core complex to form a PSI–LHCI subcomplex occurs before assembled LHCIs dissociate from the Alb3.1–cpSRP complex.

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2

Pi, Xiong, Lirong Tian, Huai-En Dai, Xiaochun Qin, Lingpeng Cheng, Tingyun Kuang, Sen-Fang Sui, and Jian-Ren Shen. "Unique organization of photosystem I–light-harvesting supercomplex revealed by cryo-EM from a red alga." Proceedings of the National Academy of Sciences 115, no. 17 (April 9, 2018): 4423–28. http://dx.doi.org/10.1073/pnas.1722482115.

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Photosystem I (PSI) is one of the two photosystems present in oxygenic photosynthetic organisms and functions to harvest and convert light energy into chemical energy in photosynthesis. In eukaryotic algae and higher plants, PSI consists of a core surrounded by variable species and numbers of light-harvesting complex (LHC)I proteins, forming a PSI-LHCI supercomplex. Here, we report cryo-EM structures of PSI-LHCR from the red alga Cyanidioschyzon merolae in two forms, one with three Lhcr subunits attached to the side, similar to that of higher plants, and the other with two additional Lhcr subunits attached to the opposite side, indicating an ancient form of PSI-LHCI. Furthermore, the red algal PSI core showed features of both cyanobacterial and higher plant PSI, suggesting an intermediate type during evolution from prokaryotes to eukaryotes. The structure of PsaO, existing in eukaryotic organisms, was identified in the PSI core and binds three chlorophylls a and may be important in harvesting energy and in mediating energy transfer from LHCII to the PSI core under state-2 conditions. Individual attaching sites of LHCRs with the core subunits were identified, and each Lhcr was found to contain 11 to 13 chlorophylls a and 5 zeaxanthins, which are apparently different from those of LHCs in plant PSI-LHCI. Together, our results reveal unique energy transfer pathways different from those of higher plant PSI-LHCI, its adaptation to the changing environment, and the possible changes of PSI-LHCI during evolution from prokaryotes to eukaryotes.

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3

Wu, Guangxi, Lin Ma, Cai Yuan, Jiahao Dai, Lai Luo, Roshan Sharma Poudyal, Richard T. Sayre, and Choon-Hwan Lee. "Formation of light-harvesting complex II aggregates from LHCII–PSI–LHCI complexes in rice plants under high light." Journal of Experimental Botany 72, no. 13 (May 3, 2021): 4938–48. http://dx.doi.org/10.1093/jxb/erab188.

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Abstract During low light- (LL) induced state transitions in dark-adapted rice (Oryza sativa) leaves, light-harvesting complex (LHC) II become phosphorylated and associate with PSI complexes to form LHCII–PSI–LHCI supercomplexes. When the leaves are subsequently transferred to high light (HL) conditions, phosphorylated LHCII complexes are no longer phosphorylated. Under the HL-induced transition in LHC phosphorylation status, we observed a new green band in the stacking gel of native green–PAGE, which was determined to be LHCII aggregates by immunoblotting and 77K chlorophyll fluorescence analysis. Knockout mutants of protein phosphatase 1 (PPH1) which dephosphorylates LHCII failed to form these LHCII aggregates. In addition, the ability to develop non-photochemical quenching in the PPH1 mutant under HL was less than for wild-type plants. As determined by immunoblotting analysis, LHCII proteins present in LHCII–PSI–LHCI supercomplexes included the Lhcb1 and Lhcb2 proteins. In this study, we provide evidence suggesting that LHCII in the LHCII–PSI–LHCI supercomplexes are dephosphorylated and subsequently form aggregates to dissipate excess light energy under HL conditions. We propose that this LHCII aggregation, involving LHCII L-trimers, is a newly observed photoprotective light-quenching process operating in the early stage of acclimation to HL in rice plants.

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4

Schiphorst, Christo, Luuk Achterberg, Rodrigo Gómez, Rob Koehorst, Roberto Bassi, Herbert van Amerongen, Luca Dall’Osto, and Emilie Wientjes. "The role of light-harvesting complex I in excitation energy transfer from LHCII to photosystem I in Arabidopsis." Plant Physiology 188, no. 4 (December 6, 2021): 2241–52. http://dx.doi.org/10.1093/plphys/kiab579.

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Abstract Photosynthesis powers nearly all life on Earth. Light absorbed by photosystems drives the conversion of water and carbon dioxide into sugars. In plants, photosystem I (PSI) and photosystem II (PSII) work in series to drive the electron transport from water to NADP+. As both photosystems largely work in series, a balanced excitation pressure is required for optimal photosynthetic performance. Both photosystems are composed of a core and light-harvesting complexes (LHCI) for PSI and LHCII for PSII. When the light conditions favor the excitation of one photosystem over the other, a mobile pool of trimeric LHCII moves between both photosystems thus tuning their antenna cross-section in a process called state transitions. When PSII is overexcited multiple LHCIIs can associate with PSI. A trimeric LHCII binds to PSI at the PsaH/L/O site to form a well-characterized PSI–LHCI–LHCII supercomplex. The binding site(s) of the “additional” LHCII is still unclear, although a mediating role for LHCI has been proposed. In this work, we measured the PSI antenna size and trapping kinetics of photosynthetic membranes from Arabidopsis (Arabidopsis thaliana) plants. Membranes from wild-type (WT) plants were compared to those of the ΔLhca mutant that completely lacks the LHCI antenna. The results showed that “additional” LHCII complexes can transfer energy directly to the PSI core in the absence of LHCI. However, the transfer is about two times faster and therefore more efficient, when LHCI is present. This suggests LHCI mediates excitation energy transfer from loosely bound LHCII to PSI in WT plants.

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5

Pan, Xiaowei, Jun Ma, Xiaodong Su, Peng Cao, Wenrui Chang, Zhenfeng Liu, Xinzheng Zhang, and Mei Li. "Structure of the maize photosystem I supercomplex with light-harvesting complexes I and II." Science 360, no. 6393 (June 7, 2018): 1109–13. http://dx.doi.org/10.1126/science.aat1156.

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Plants regulate photosynthetic light harvesting to maintain balanced energy flux into photosystems I and II (PSI and PSII). Under light conditions favoring PSII excitation, the PSII antenna, light-harvesting complex II (LHCII), is phosphorylated and forms a supercomplex with PSI core and the PSI antenna, light-harvesting complex I (LHCI). Both LHCI and LHCII then transfer excitation energy to the PSI core. We report the structure of maize PSI-LHCI-LHCII solved by cryo–electron microscopy, revealing the recognition site between LHCII and PSI. The PSI subunits PsaN and PsaO are observed at the PSI-LHCI interface and the PSI-LHCII interface, respectively. Each subunit relays excitation to PSI core through a pair of chlorophyll molecules, thus revealing previously unseen paths for energy transfer between the antennas and the PSI core.

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6

Santabarbara, Stefano, Tania Tibiletti, William Remelli, and Stefano Caffarri. "Kinetics and heterogeneity of energy transfer from light harvesting complex II to photosystem I in the supercomplex isolated from Arabidopsis." Physical Chemistry Chemical Physics 19, no. 13 (2017): 9210–22. http://dx.doi.org/10.1039/c7cp00554g.

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7

Steinbeck, Janina, Ian L. Ross, Rosalba Rothnagel, Philipp Gäbelein, Stefan Schulze, Nichole Giles, Rubbiya Ali, et al. "Structure of a PSI–LHCI–cyt b6f supercomplex in Chlamydomonas reinhardtii promoting cyclic electron flow under anaerobic conditions." Proceedings of the National Academy of Sciences 115, no. 41 (September 25, 2018): 10517–22. http://dx.doi.org/10.1073/pnas.1809973115.

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Photosynthetic linear electron flow (LEF) produces ATP and NADPH, while cyclic electron flow (CEF) exclusively drives photophosphorylation to supply extra ATP. The fine-tuning of linear and cyclic electron transport levels allows photosynthetic organisms to balance light energy absorption with cellular energy requirements under constantly changing light conditions. As LEF and CEF share many electron transfer components, a key question is how the same individual structural units contribute to these two different functional modes. Here, we report the structural identification of a photosystem I (PSI)–light harvesting complex I (LHCI)–cytochrome (cyt) b6f supercomplex isolated from the unicellular alga Chlamydomonas reinhardtii under anaerobic conditions, which induces CEF. This provides strong evidence for the model that enhanced CEF is induced by the formation of CEF supercomplexes, when stromal electron carriers are reduced, to generate additional ATP. The additional identification of PSI–LHCI–LHCII complexes is consistent with recent findings that both CEF enhancement and state transitions are triggered by similar conditions, but can occur independently from each other. Single molecule fluorescence correlation spectroscopy indicates a physical association between cyt b6f and fluorescent chlorophyll containing PSI–LHCI supercomplexes. Single particle analysis identified top-view projections of the corresponding PSI–LHCI–cyt b6f supercomplex. Based on molecular modeling and mass spectrometry analyses, we propose a model in which dissociation of LHCA2 and LHCA9 from PSI supports the formation of this CEF supercomplex. This is supported by the finding that a Δlhca2 knockout mutant has constitutively enhanced CEF.

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8

Li, Mei, Xiaowei Pan, Jun Ma, Xiaodong Su, Wenrui Chang, Zhenfeng Liu, and Xinzheng Zhang. "Cryo-EM structure of maize PSI-LHCI-LHCII supercomplex." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1859 (September 2018): e34. http://dx.doi.org/10.1016/j.bbabio.2018.09.109.

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9

Joaquín-Ovalle, Freisa, Grace Guihurt, Vanessa Barcelo-Bovea, Andraous Hani-Saba, Nicole Fontanet-Gómez, Josell Ramirez-Paz, Yasuhiro Kashino, et al. "Oxidative Stress- and Autophagy-Inducing Effects of PSI-LHCI from Botryococcus braunii in Breast Cancer Cells." BioTech 11, no. 2 (March 30, 2022): 9. http://dx.doi.org/10.3390/biotech11020009.

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Botryococcus braunii (B. braunii) is a green microalga primarily found in freshwater, reservoirs, and ponds. Photosynthetic pigments from algae have shown many bioactive molecules with therapeutic potential. Herein, we report the purification, characterization, and anticancer properties of photosystem I light-harvesting complex I (PSI-LHCI) from the green microalga B. braunii UTEX2441. The pigment–protein complex was purified by sucrose density gradient and characterized by its distinctive peaks using absorption, low-temperature (77 K) fluorescence, and circular dichroism (CD) spectroscopic analyses. Protein complexes were resolved by blue native-PAGE and two-dimensional SDS-PAGE. Triple-negative breast cancer MDA-MB-231 cells were incubated with PSI-LHCI for all of our experiments. Cell viability was assessed, revealing a significant reduction in a time- and concentration-dependent manner. We confirmed the internalization of PSI-LHCI within the cytoplasm and nucleus after 12 h of incubation. Cell death mechanism by oxidative stress was confirmed by the production of reactive oxygen species (ROS) and specifically superoxide. Furthermore, we monitored autophagic flux, apoptotic and necrotic features after treatment with PSI-LHCI. Treated MDA-MB-231 cells showed positive autophagy signals in the cytoplasm and nucleus, and necrotic morphology by the permeabilization of the cell membrane. Our findings demonstrated for the first time the cytotoxic properties of B. braunii PSI-LHCI by the induction of ROS and autophagy in breast cancer cells.

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10

Qin, Xiaochun, Wenda Wang, Kebing Wang, Yueyong Xin, and Tingyun Kuang. "Isolation and Characteristics of the PSI-LHCI-LHCII Supercomplex Under High Light." Photochemistry and Photobiology 87, no. 1 (November 15, 2010): 143–50. http://dx.doi.org/10.1111/j.1751-1097.2010.00830.x.

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11

Jennings, Robert C., Giuseppe Zucchelli, Enrico Engelmann, and Flavio M. Garlaschi. "The Long-Wavelength Chlorophyll States of Plant LHCI at Room Temperature: A Comparison with PSI-LHCI." Biophysical Journal 87, no. 1 (July 2004): 488–97. http://dx.doi.org/10.1529/biophysj.103.038117.

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12

Jeong, Jooyeon, Kwangryul Baek, Jihyeon Yu, Henning Kirst, Nico Betterle, Woongghi Shin, Sangsu Bae, Anastasios Melis, and EonSeon Jin. "Deletion of the chloroplast LTD protein impedes LHCI import and PSI–LHCI assembly in Chlamydomonas reinhardtii." Journal of Experimental Botany 69, no. 5 (December 30, 2017): 1147–58. http://dx.doi.org/10.1093/jxb/erx457.

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13

Bressan, Mauro, Roberto Bassi, and Luca Dall’Osto. "Loss of LHCI system affects LHCII re-distribution between thylakoid domains upon state transitions." Photosynthesis Research 135, no. 1-3 (September 16, 2017): 251–61. http://dx.doi.org/10.1007/s11120-017-0444-1.

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14

Takahashi, Yuichiro, Taka-aki Yasui, Einar J. Stauber, and Michael Hippler. "Comparison of the Subunit Compositions of the PSI−LHCI Supercomplex and the LHCI in the Green AlgaChlamydomonas reinhardtii†." Biochemistry 43, no. 24 (June 2004): 7816–23. http://dx.doi.org/10.1021/bi035988z.

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15

Zada, Ahmad, Ahmad Ali, Dalal Nasser Binjawhar, Usama K. Abdel-Hameed, Azhar Hussain Shah, Shahid Maqsood Gill, Irtiza Hussain, et al. "Molecular and Physiological Evaluation of Bread Wheat (Triticum aestivum L.) Genotypes for Stay Green under Drought Stress." Genes 13, no. 12 (November 30, 2022): 2261. http://dx.doi.org/10.3390/genes13122261.

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Water availability is considered as the main limiting factor of wheat growth illuminating the need of cultivars best adapted to drought situations for better wheat production and yield. Among these, the stay-green trait is thought to be related to the ability of wheat plants to maintain photosynthesis and CO2 assimilation, and a detailed molecular understanding of this trait may help in the selection of high-yielding, drought-tolerant wheats. The current study, therefore, evaluated the physiological responses of the selected wheat genotypes under pot-induced water stress conditions through different field capacities. The study also focused on exploring the molecular mechanisms involved in drought tolerance conferred due to the stay-green trait by studying the expression pattern of the selected PSI-associated light-harvesting complex I (LHC1) and PSII-associated LHCII gene families related to pigment-binding proteins. The results revealed that the studied traits, including relative water content, membrane stability index and chlorophyll, were variably and negatively affected, while the proline content was positively enhanced in the studied wheats under water stress treatments. Molecular diagnosis of the selected wheat genotypes using the expression profile of 06 genes, viz. TaLhca1, TaLhca2, TaLhca3, TaLhcb1, TaLhcb4 and TaLhcb6 that encodes for the LHCI and LHCII proteins, indicated variable responses to different levels of drought stress. The results obtained showed the relation between the genotypes and the severity of the drought stress condition. Among the studied genotypes, Chirya-1 and SD-28 performed well with a higher level of gene expression under drought stress conditions and may be used in genetic crosses to enrich the genetic background of common wheat against drought stress.

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16

van Oort, Bart, Alexey Amunts, Jan Willem Borst, Arie van Hoek, Nathan Nelson, Herbert van Amerongen, and Roberta Croce. "Picosecond Fluorescence of Intact and Dissolved PSI-LHCI Crystals." Biophysical Journal 95, no. 12 (December 2008): 5851–61. http://dx.doi.org/10.1529/biophysj.108.140467.

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17

van Amerongen, Herbert, Bart van Oort, Arie van Hoek, Jan Willem Borst, Alexey Amunts, Nathan Nelson, and Roberta Croce. "Picosecond Fluorescence Of Intact And Dissolved PSI-LHCI Crystals." Biophysical Journal 96, no. 3 (February 2009): 524a. http://dx.doi.org/10.1016/j.bpj.2008.12.2701.

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18

Gáspár, László, Éva Sárvári, Fermín Morales, and Zoltán Szigeti. "Presence of ‘PSI free’ LHCI and monomeric LHCII and subsequent effects on fluorescence characteristics in lincomycin treated maize." Planta 223, no. 5 (November 15, 2005): 1047–57. http://dx.doi.org/10.1007/s00425-005-0149-0.

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19

Garab, G., and L. Mustárdy. "Role of LHCII-containing macrodomains in the structure, function and dynamics of grana." Functional Plant Biology 26, no. 7 (1999): 649. http://dx.doi.org/10.1071/pp99069.

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In higher plants and green algae two types of thylakoids are distinguished, granum (stacked) and stroma (unstacked) thylakoids. They form a three-dimensional (3D) network with large lateral heterogeneity: photosystem II (PSII) and the associated main chlorophyll a/b light-harvesting complex (LHCII) are found predominantly in the stacked region, while PSI and LHCI are located mainly in the unstacked region of the membrane. This picture emerged from the discovery of the physical separation of the two photosystems (Boardman and Anderson 1964). Granal chloroplasts possess significant flexibility, which is essential for optimizing the photosynthetic machinery under various environmental conditions. However, our understanding concerning the assembly, structural dynamics and regulatory functions of grana is far from being complete. In this paper we overview the significance of the three-dimensional structure of grana in the absorption properties, ionic equilibrations, and in the diffusion of membrane components between the stacked and unstacked regions. Further, we discuss the role of chiral macrodomains in the grana. Lateral heterogeneity of thylakoid membranes is proposed to be a consequence of the formation of macrodomains constituted of LHCII and PSII; their long range order permits long distance migration of excitation energy, which explains the energetic connectivity of PSII particles. The ability of macrodomains to undergo light-induced reversible structural changes lends structural flexibility to the granum. In purified LHCII, which has also been shown to form stacked lamellar aggregates with long range chiral order, excitation energy migrates for large distances; these macroaggregates are also capable of undergoing light-induced reversible structural changes and fluorescence quenching. Hence, some basic properties of grana appear to originate from its main constituent, the LHCII.

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Garab, G., and L. Mustárdy. "Role of LHCII-containing macrodomains in the structure, function and dynamics of grana." Functional Plant Biology 27, no. 7 (2000): 723. http://dx.doi.org/10.1071/pp99069_c1.

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In higher plants and green algae two types of thylakoids are distinguished, granum (stacked) and stroma (unstacked) thylakoids. They form a three-dimensional (3D) network with large lateral heterogeneity: photosystem II (PSII) and the associated main chlorophyll a/b light-harvesting complex (LHCII) are found predominantly in the stacked region, while PSI and LHCI are located mainly in the unstacked region of the membrane. This picture emerged from the discovery of the physical separation of the two photosystems (Boardman and Anderson 1964). Granal chloroplasts possess significant flexibility, which is essential for optimizing the photosynthetic machinery under various environmental conditions. However, our understanding concerning the assembly, structural dynamics and regulatory functions of grana is far from being complete. In this paper we overview the significance of the three-dimensional structure of grana in the absorption properties, ionic equilibrations, and in the diffusion of membrane components between the stacked and unstacked regions. Further, we discuss the role of chiral macrodomains in the grana. Lateral heterogeneity of thylakoid membranes is proposed to be a consequence of the formation of macrodomains constituted of LHCII and PSII; their long range order permits long distance migration of excitation energy, which explains the energetic connectivity of PSII particles. The ability of macrodomains to undergo light-induced reversible structural changes lends structural flexibility to the granum. In purified LHCII, which has also been shown to form stacked lamellar aggregates with long range chiral order, excitation energy migrates for large distances; these macroaggregates are also capable of undergoing light-induced reversible structural changes and fluorescence quenching. Hence, some basic properties of grana appear to originate from its main constituent, the LHCII.

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21

Garab, G., and L. Mustárdy. "Role of LHCII-containing macrodomains in the structure, function and dynamics of grana." Functional Plant Biology 27, no. 3 (2000): 279. http://dx.doi.org/10.1071/pp99069_co.

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In higher plants and green algae two types of thylakoids are distinguished, granum (stacked) and stroma (unstacked) thylakoids. They form a three-dimensional (3D) network with large lateral heterogeneity: photosystem II (PSII) and the associated main chlorophyll a/b light-harvesting complex (LHCII) are found predominantly in the stacked region, while PSI and LHCI are located mainly in the unstacked region of the membrane. This picture emerged from the discovery of the physical separation of the two photosystems (Boardman and Anderson 1964). Granal chloroplasts possess significant flexibility, which is essential for optimizing the photosynthetic machinery under various environmental conditions. However, our understanding concerning the assembly, structural dynamics and regulatory functions of grana is far from being complete. In this paper we overview the significance of the three-dimensional structure of grana in the absorption properties, ionic equilibrations, and in the diffusion of membrane components between the stacked and unstacked regions. Further, we discuss the role of chiral macrodomains in the grana. Lateral heterogeneity of thylakoid membranes is proposed to be a consequence of the formation of macrodomains constituted of LHCII and PSII; their long range order permits long distance migration of excitation energy, which explains the energetic connectivity of PSII particles. The ability of macrodomains to undergo light-induced reversible structural changes lends structural flexibility to the granum. In purified LHCII, which has also been shown to form stacked lamellar aggregates with long range chiral order, excitation energy migrates for large distances; these macroaggregates are also capable of undergoing light-induced reversible structural changes and fluorescence quenching. Hence, some basic properties of grana appear to originate from its main constituent, the LHCII.

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22

Melkozernov, Alexander N., and Robert E. Blankenship. "Structural Modeling of the Lhca4 Subunit of LHCI-730 Peripheral Antenna in Photosystem I Based on Similarity with LHCII." Journal of Biological Chemistry 278, no. 45 (August 15, 2003): 44542–51. http://dx.doi.org/10.1074/jbc.m306777200.

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23

Szalkowski, Marcin, Alessandro Surrente, Kamil Wiwatowski, Zhuo Yang, Nan Zhang, Julian D. Janna Olmos, Joanna Kargul, Paulina Plochocka, and Sebastian Maćkowski. "Spectral Dependence of the Energy Transfer from Photosynthetic Complexes to Monolayer Graphene." International Journal of Molecular Sciences 23, no. 7 (March 23, 2022): 3493. http://dx.doi.org/10.3390/ijms23073493.

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Fluorescence excitation spectroscopy at cryogenic temperatures carried out on hybrid assemblies composed of photosynthetic complexes deposited on a monolayer graphene revealed that the efficiency of energy transfer to graphene strongly depended on the excitation wavelength. The efficiency of this energy transfer was greatly enhanced in the blue-green spectral region. We observed clear resonance-like behavior for both a simple light-harvesting antenna containing only two chlorophyll molecules (PCP) and a large photochemically active reaction center associated with the light-harvesting antenna (PSI–LHCI), which pointed towards the general character of this effect.

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24

Melkozernov, Alexander N., Joanna Kargul, Su Lin, James Barber, and Robert E. Blankenship. "Energy Coupling in the PSI−LHCI Supercomplex from the Green AlgaChlamydomonas reinhardtii†,‖." Journal of Physical Chemistry B 108, no. 29 (July 2004): 10547–55. http://dx.doi.org/10.1021/jp049375n.

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25

Qin, X., M. Suga, T. Kuang, and J. R. Shen. "Structural basis for energy transfer pathways in the plant PSI-LHCI supercomplex." Science 348, no. 6238 (May 28, 2015): 989–95. http://dx.doi.org/10.1126/science.aab0214.

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26

Suga, Michihiro, Xiaochun Qin, Tingyun Kuang, and Jian-Ren Shen. "Structure and energy transfer pathways of the plant photosystem I-LHCI supercomplex." Current Opinion in Structural Biology 39 (August 2016): 46–53. http://dx.doi.org/10.1016/j.sbi.2016.04.004.

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27

Melkozernov, Alexander N., Volkmar H. R. Schmid, Gregory W. Schmidt, and Robert E. Blankenship. "Energy Redistribution in Heterodimeric Light-Harvesting Complex LHCI-730 of Photosystem I." Journal of Physical Chemistry B 102, no. 42 (October 1998): 8183–89. http://dx.doi.org/10.1021/jp9810466.

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28

Wientjes, Emilie, and Roberta Croce. "The light-harvesting complexes of higher-plant Photosystem I: Lhca1/4 and Lhca2/3 form two red-emitting heterodimers." Biochemical Journal 433, no. 3 (January 14, 2011): 477–85. http://dx.doi.org/10.1042/bj20101538.

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The outer antenna of higher-plant PSI (Photosystem I) is composed of four complexes [Lhc (light-harvesting complex) a1–Lhca4] belonging to the light-harvesting protein family. Difficulties in their purification have so far prevented the determination of their properties and most of the knowledge about Lhcas has been obtained from the study of the in vitro reconstituted antennas. In the present study we were able to purify the native complexes, showing that Lhca2/3 and Lhca1/4 form two functional heterodimers. Both dimers show red-fluorescence emission with maxima around 730 nm, as in the intact PSI complex. This indicates that the dimers are in their native state and that LHCI-680, which was previously assumed to be part of the PSI antenna, does not represent the native state of the system. The data show that the light-harvesting properties of the two dimers are functionally identical, concerning absorption, long-wavelength emission and fluorescence quantum yield, whereas they differ in their high-light response. Implications of the present study for the understanding of the energy transfer process in PSI are discussed. Finally, the comparison of the properties of the native dimers with those of the reconstituted complexes demonstrates that all of the major properties of the Lhcas are reproduced in the in vitro systems.

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Le Quiniou, Clotilde, Lijin Tian, Bartlomiej Drop, Emilie Wientjes, Ivo H. M. van Stokkum, Bart van Oort, and Roberta Croce. "PSI–LHCI of Chlamydomonas reinhardtii : Increasing the absorption cross section without losing efficiency." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1847, no. 4-5 (April 2015): 458–67. http://dx.doi.org/10.1016/j.bbabio.2015.02.001.

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Su, Xiaodong, Jun Ma, Xiaowei Pan, Xuelin Zhao, Wenrui Chang, Zhenfeng Liu, Xinzheng Zhang, and Mei Li. "Antenna arrangement and energy transfer pathways of a green algal photosystem-I–LHCI supercomplex." Nature Plants 5, no. 3 (March 2019): 273–81. http://dx.doi.org/10.1038/s41477-019-0380-5.

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Jennings, Robert C., Giuseppe Zucchelli, and Stefano Santabarbara. "Photochemical trapping heterogeneity as a function of wavelength, in plant photosystem I (PSI–LHCI)." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1827, no. 6 (June 2013): 779–85. http://dx.doi.org/10.1016/j.bbabio.2013.03.008.

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Kowalska, Dorota, Marcin Szalkowski, Karolina Sulowska, Dorota Buczynska, Joanna Niedziolka-Jonsson, Martin Jonsson-Niedziolka, Joanna Kargul, Heiko Lokstein, and Sebastian Mackowski. "Silver Island Film for Enhancing Light Harvesting in Natural Photosynthetic Proteins." International Journal of Molecular Sciences 21, no. 7 (April 1, 2020): 2451. http://dx.doi.org/10.3390/ijms21072451.

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The effects of combining naturally evolved photosynthetic pigment–protein complexes with inorganic functional materials, especially plasmonically active metallic nanostructures, have been a widely studied topic in the last few decades. Besides other applications, it seems to be reasonable using such hybrid systems for designing future biomimetic solar cells. In this paper, we describe selected results that point out to various aspects of the interactions between photosynthetic complexes and plasmonic excitations in Silver Island Films (SIFs). In addition to simple light-harvesting complexes, like peridinin-chlorophyll-protein (PCP) or the Fenna–Matthews–Olson (FMO) complex, we also discuss the properties of large, photosynthetic reaction centers (RCs) and Photosystem I (PSI)—both prokaryotic PSI core complexes and eukaryotic PSI supercomplexes with attached antenna clusters (PSI-LHCI)—deposited on SIF substrates.

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Croce, Roberta, Giuseppe Zucchelli, Flavio M. Garlaschi, and Robert C. Jennings. "A Thermal Broadening Study of the Antenna Chlorophylls in PSI-200, LHCI, and PSI Core." Biochemistry 37, no. 50 (December 1998): 17355–60. http://dx.doi.org/10.1021/bi9813227.

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Jennings, Robert C., Flavio M. Garlaschi, Enrico Engelmann, and Giuseppe Zucchelli. "The room temperature emission band shape of the lowest energy chlorophyll spectral form of LHCI." FEBS Letters 547, no. 1-3 (June 20, 2003): 107–10. http://dx.doi.org/10.1016/s0014-5793(03)00687-2.

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Abram, Mateusz, Rafał Białek, Sebastian Szewczyk, Jerzy Karolczak, Krzysztof Gibasiewicz, and Joanna Kargul. "Remodeling of excitation energy transfer in extremophilic red algal PSI-LHCI complex during light adaptation." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1861, no. 1 (January 2020): 148093. http://dx.doi.org/10.1016/j.bbabio.2019.148093.

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36

Subramanyam, Rajagopal, Craig Jolley, Daniel C. Brune, Petra Fromme, and Andrew N. Webber. "Characterization of a novel Photosystem I-LHCI supercomplex isolated fromChlamydomonas reinhardtiiunder anaerobic (State II) conditions." FEBS Letters 580, no. 1 (December 12, 2005): 233–38. http://dx.doi.org/10.1016/j.febslet.2005.12.003.

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37

Allen, K. D., M. E. Duysen, and L. A. Staehelin. "Biogenesis of thylakoid membranes is controlled by light intensity in the conditional chlorophyll b-deficient CD3 mutant of wheat." Journal of Cell Biology 107, no. 3 (September 1, 1988): 907–19. http://dx.doi.org/10.1083/jcb.107.3.907.

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Biogenesis of thylakoid membranes in the conditional chlorophyll b-deficient CD3 mutant of wheat is dramatically altered by relatively small differences in the light intensity under which seedlings are grown. When the CD3 mutant is grown at 400 microE/m2 S (high light, about one-fifth full sunlight) plants are deficient in chlorophyll b (chlorophyll a/b ratio greater than 6.0) and lack or contain greatly reduced amounts of the chlorophyll a/b-binding complexes CPII/CPII (mobile or peripheral LHCII), CP29, CP24 and LHCI, as shown by mildly denaturing 'green gel' electrophoresis, by fully denaturing SDS-PAGE, and by Western blot analysis. High light CD3 chloroplasts display an unusual morphology characterized by large, sheet-like stromal thylakoids formed into parallel unstacked arrays and a limited number of small grana stacks displaced toward the edges of the arrays. Changes in the supramolecular organization of CD3 thylakoids, seen with freeze-fracture electron microscopy, include a reduction in the size of EFs particles, which correspond to photosystem II centers with variable amounts of attached LHCII, and a redistribution of EF particles from the stacked to the unstacked regions. When CD3 seedlings are grown at 150 microE/m2 S (low light) there is a substantial reversal of all of these effects. Thus, chlorophyll b and the chlorophyll a/b-binding proteins accumulate to near wild-type levels (chlorophyll a/b ratio = 3.5-4.5) and thylakoid morphology is more nearly wild type in appearance. Growth of the CD3 mutant in the presence of chloramphenicol stimulates the accumulation of chlorophyll b and its binding proteins (Duysen, M. E., T. P. Freeman, N. D. Williams, and L. L. Huckle. 1985. Plant Physiol. 78:531-536). We show that this partial rescue of the CD3 high light phenotype is accompanied by large changes in thylakoid structure. The CD3 mutant, which defines a new class of chlorophyll b-deficient phenotype, is discussed in the more general context of chlorophyll b deficiency.

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Yadavalli, Venkateswarlu, Chandramouli Malleda, and Rajagopal Subramanyam. "Protein–protein interactions by molecular modeling and biochemical characterization of PSI-LHCI supercomplexes from Chlamydomonas reinhardtii." Molecular BioSystems 7, no. 11 (2011): 3143. http://dx.doi.org/10.1039/c1mb05218g.

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39

Doan, Jean-Michel, Benoı̂t Schoefs, Alexander V. Ruban, and Anne-Lise Etienne. "Changes in the LHCI aggregation state during iron repletion in the unicellular red alga Rhodella violacea." FEBS Letters 533, no. 1 (December 4, 2002): 59–62. http://dx.doi.org/10.1016/s0014-5793(02)03748-1.

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Gibasiewicz, Krzysztof, Anna Szrajner, Janne A. Ihalainen, Marta Germano, Jan P. Dekker, and Rienk van Grondelle. "Characterization of Low-Energy Chlorophylls in the PSI-LHCI Supercomplex fromChlamydomonasreinhardtii. A Site-Selective Fluorescence Study." Journal of Physical Chemistry B 109, no. 44 (November 2005): 21180–86. http://dx.doi.org/10.1021/jp0530909.

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Barbato, R., G. Friso, F. Rigoni, F. Dalla Vecchia, and G. M. Giacometti. "Structural changes and lateral redistribution of photosystem II during donor side photoinhibition of thylakoids." Journal of Cell Biology 119, no. 2 (October 15, 1992): 325–35. http://dx.doi.org/10.1083/jcb.119.2.325.

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The structural and topological stability of thylakoid components under photoinhibitory conditions (4,500 microE.m-2.s-1 white light) was studied on Mn depleted thylakoids isolated from spinach leaves. After various exposures to photoinhibitory light, the chlorophyll-protein complexes of both photosystems I and II were separated by sucrose gradient centrifugation and analysed by Western blotting, using a set of polyclonals raised against various apoproteins of the photosynthetic apparatus. A series of events occurring during donor side photoinhibition are described for photosystem II, including: (a) lowering of the oligomerization state of the photosystem II core; (b) cleavage of 32-kD protein D1 at specific sites; (c) dissociation of chlorophyll-protein CP43 from the photosystem II core; and (d) migration of damaged photosystem II components from the grana to the stroma lamellae. A tentative scheme for the succession of these events is illustrated. Some effects of photoinhibition on photosystem I are also reported involving dissociation of antenna chlorophyll-proteins LHCI from the photosystem I reaction center.

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Ballottari, Matteo, Chiara Govoni, Stefano Caffarri, and Tomas Morosinotto. "Stoichiometry of LHCI antenna polypeptides and characterization of gap and linker pigments in higher plants Photosystem I." European Journal of Biochemistry 271, no. 23-24 (December 2004): 4659–65. http://dx.doi.org/10.1111/j.1432-1033.2004.04426.x.

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43

Stauber, Einar J., Andreas Busch, Bianca Naumann, Aleš Svatoš, and Michael Hippler. "Proteotypic profiling of LHCI from Chlamydomonas reinhardtii provides new insights into structure and function of the complex." PROTEOMICS 9, no. 2 (January 2009): 398–408. http://dx.doi.org/10.1002/pmic.200700620.

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Subramanyam, Rajagopal, Craig Jolley, Balakumar Thangaraj, Sreedhar Nellaepalli, Andrew N. Webber, and Petra Fromme. "Structural and functional changes of PSI-LHCI supercomplexes of Chlamydomonas reinhardtii cells grown under high salt conditions." Planta 231, no. 4 (January 10, 2010): 913–22. http://dx.doi.org/10.1007/s00425-009-1097-x.

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45

Peng, Lianwei, Yoichiro Fukao, Masayuki Fujiwara, Tsuneaki Takami, and Toshiharu Shikanai. "Efficient Operation of NAD(P)H Dehydrogenase Requires Supercomplex Formation with Photosystem I via Minor LHCI in Arabidopsis." Plant Cell 21, no. 11 (November 2009): 3623–40. http://dx.doi.org/10.1105/tpc.109.068791.

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46

Tian, Lirong, Zheyi Liu, Fangjun Wang, Liangliang Shen, Jinghua Chen, Lijing Chang, Songhao Zhao, et al. "Isolation and characterization of PSI–LHCI super-complex and their sub-complexes from a red alga Cyanidioschyzon merolae." Photosynthesis Research 133, no. 1-3 (April 12, 2017): 201–14. http://dx.doi.org/10.1007/s11120-017-0384-9.

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47

Kargul, Joanna, Jon Nield, and James Barber. "Three-dimensional Reconstruction of a Light-harvesting Complex I- Photosystem I (LHCI-PSI) Supercomplex from the Green AlgaChlamydomonas reinhardtii." Journal of Biological Chemistry 278, no. 18 (February 14, 2003): 16135–41. http://dx.doi.org/10.1074/jbc.m300262200.

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48

Jennings, Robert C., Flavio M. Garlaschi, Tomas Morosinotto, Enrico Engelmann, and Giuseppe Zucchelli. "Corrigendum to: The room temperature emission band shape of the lowest energy chlorophyll spectral form of LHCI (FEBS 27430)." FEBS Letters 549, no. 1-3 (July 22, 2003): 181. http://dx.doi.org/10.1016/s0014-5793(03)00790-7.

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Thangaraj, Balakumar, Craig C. Jolley, Iosifina Sarrou, Jelle B. Bultema, Jason Greyslak, Julian P. Whitelegge, Su Lin, et al. "Efficient Light Harvesting in a Dark, Hot, Acidic Environment: The Structure and Function of PSI-LHCI from Galdieria sulphuraria." Biophysical Journal 100, no. 1 (January 2011): 135–43. http://dx.doi.org/10.1016/j.bpj.2010.09.069.

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Yamatani, Hiroshi, Kaori Kohzuma, Michiharu Nakano, Tsuneaki Takami, Yusuke Kato, Yoriko Hayashi, Yuki Monden, et al. "Impairment of Lhca4, a subunit of LHCI, causes high accumulation of chlorophyll and the stay-green phenotype in rice." Journal of Experimental Botany 69, no. 5 (January 3, 2018): 1027–35. http://dx.doi.org/10.1093/jxb/erx468.

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