scholarly journals The light-harvesting complexes of higher-plant Photosystem I: Lhca1/4 and Lhca2/3 form two red-emitting heterodimers

2011 ◽  
Vol 433 (3) ◽  
pp. 477-485 ◽  
Author(s):  
Emilie Wientjes ◽  
Roberta Croce
Keyword(s):  
Photosystem I ◽  
Light Harvesting ◽  
Fluorescence Emission ◽  
Light Response ◽  
Native State ◽  
Higher Plant ◽  
Light Harvesting Complexes ◽  
Light Harvesting Complex ◽  
Wavelength Emission

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.

scholarly journals Identification of parallel pH- and zeaxanthin-dependent quenching of excess energy in LHCSR3 in Chlamydomonas reinhardtii

2020 ◽  
Author(s):  
Julianne M. Troiano ◽  
Federico Perozeni ◽  
Raymundo Moya ◽  
Luca Zuliani ◽  
Kwangryul Baek ◽  
...  
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Light Harvesting ◽  
Complex Stress ◽  
Excess Energy ◽  
Photochemical Quenching ◽  
Light Harvesting Complexes ◽  
Light Harvesting Complex ◽  
Non Photochemical Quenching

AbstractUnder high light conditions, oxygenic photosynthetic organisms avoid photodamage by thermally dissipating excess absorbed energy, which is called non-photochemical quenching (NPQ). In green algae, a chlorophyll and carotenoid-binding protein, light-harvesting complex stress-related (LHCSR3), detects excess energy via pH and serves as a quenching site. However, the mechanisms by which LHCSR3 functions have not been determined. Using a combined in vivo and in vitro approach, we identify two parallel yet distinct quenching processes, individually controlled by pH and carotenoid composition, and their likely molecular origin within LHCSR3 from Chlamydomonas reinhardtii. The pH-controlled quenching is removed within a mutant LHCSR3 that lacks the protonable residues responsible for sensing pH. Constitutive quenching in zeaxanthin-enriched systems demonstrates zeaxanthin-controlled quenching, which may be shared with other light-harvesting complexes. We show that both quenching processes prevent the formation of damaging reactive oxygen species, and thus provide distinct timescales and mechanisms of protection in a changing environment.

Isolation and characterization of three membranebound chlorophyll-protein complexes from four dinoflagellate species

1993 ◽  
Vol 340 (1294) ◽  
pp. 381-392 ◽  
Keyword(s):  
Energy Transfer ◽  
Photosystem I ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Gradient Centrifugation ◽  
Water Soluble ◽  
Molar Ratio ◽  
Light Harvesting Complexes ◽  
Light Harvesting Complex ◽  
Isolation And Characterization

Employing discontinuous sucrose density gradient centrifugation of n -dodecyl β-d-maltoside-solubilized thylakoid membranes, three chlorophyll (Chl)-protein complexes containing Chl a , Chl c 2 and peridinin in different proportions, were isolated from the dinoflagellates Symbiodinium microadriaticum, S. kawagutii, S. pilosum and Heterocapsa pygmaea . In S. microadriaticum , the first complex, containing 13% of the total cellular Chl a , and minor quantities of Chl c 2 and peridinin, is associated with polypeptides with apparent molecular mass ( M r ) of 8-9 kDa, and demonstrated inefficient energy transfer from the accessory pigments to Chl a . The second complex contains Chl a , Chl c 2 and peridinin in a molar ratio of 1:1:2, associated with two apoproteins of M r 19-20 kDa, and comprises 45%, 75% and 70%, respectively, of the cellular Chl a , Chl c 2 and peridinin. The efficient energy transfer from Chl c 2 and peridinin to Chl a in this complex is supportive of a light-harvesting function. This Chl a - c 2 - peridin-protein complex represents the major light-harvesting complex in dinoflagellates. The third complex obtained contains 12% of the cellular Chl a , and appears to be the core of photosystem I, associated with a light-harvesting complex. This complex is spectroscopically similar to analogous preparations from different taxonomic groups, but demonstrates a unique apoprotein composition. Antibodies against the water-soluble peridinin-Chl a -protein (sPCP) light-harvesting complexes failed to cross-react with any of the thylakoid-associated complexes, as did antibodies against Chl a - c -fucoxanthin apoprotein (from diatoms). Antibodies against the P 700 apoprotein of plants did not cross-react with the photosystem I complex. Similar results were observed in the other dinoflagellates.

Relationship between Changes in Ion Content of Leaves and Chlorophyll-Protein Composition in Cucumber under Cd and Pb Stress

1999 ◽  
Vol 54 (9-10) ◽  
pp. 746-753 ◽  
Author(s):  
Éva Sárvári ◽  
Ferenc Fodor ◽  
Edit Cseh ◽  
Anita Varga ◽  
Gyula Záray ◽  
...  
Keyword(s):  
Chlorophyll Content ◽  
Chlorophyll A ◽  
Photosystem I ◽  
Light Harvesting ◽  
Fluorescence Emission ◽  
Light Harvesting Complex ◽  
Complex Ii ◽  
Iron Deficient ◽  
Light Harvesting Complex Ii ◽  
Chlorophyll Protein

Hydroponically cultured cucumber plants supplied with 4 μᴍ Fe chelated either with EDTA or citrate and treated with Cd (10 μᴍ) and Pb (10, 50 μᴍ) from their one- or fourleaf stage were grown up to five-week-old age. The decrease in the chlorophyll content was the most pronounced in plants treated with Cd from a younger age, and in the case of Fecitrate. The chlorophyll a/b ratio of Cd stressed plants was also significantly lowered. In later treated plants the accumulation of chlorophyll was inhibited and the chlorophyll a/b ratio decreased only in the vigorously growing young leaves. Pb treatment had only a slight effect on both parameters. The changes in the chlorophyll-protein pattern of thylakoids were strongly related to their chlorophyll content but the response of each complex was different. Cd reduced the amount of chlorophyll containing complexes in the order of photosystem I > light-harvesting complex II > photosystem Il-core, while light-harvesting complex II appeared somewhat more sensitive than photosystem I in Pb treated plants. In accordance, a decline or blue shift of the long wavelength fluorescence emission band of chloroplasts was observed referring to disturbances also in photosystem I antenna assembly. The accumulation of chlorophyll and chlorophyll-proteins did not show close relationship to the heavy metal content of leaves which was the highest in the first of the intensively expanding leaves in the time of the treatment. The extraordinary sensitivity of photosystem I, and the relative stability of photosystem II under Cd treatment were similar to the case found in iron deficient plants. However, the pattern of chlorophyll content of leaf storeys of Cd treated plants rather followed the changes in their Mn content

scholarly journals Unique organization of photosystem I–light-harvesting supercomplex revealed by cryo-EM from a red alga

2018 ◽  
Vol 115 (17) ◽  
pp. 4423-4428 ◽  
Author(s):  
Xiong Pi ◽  
Lirong Tian ◽  
Huai-En Dai ◽  
Xiaochun Qin ◽  
Lingpeng Cheng ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Photosystem I ◽  
Light Harvesting ◽  
Higher Plants ◽  
Red Alga ◽  
Cyanidioschyzon Merolae ◽  
Higher Plant ◽  
Light Harvesting Complex ◽  
Red Algal ◽  
Eukaryotic Organisms

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.

scholarly journals Excitation-Energy Transfer Dynamics of Higher Plant Photosystem I Light-Harvesting Complexes

2011 ◽  
Vol 100 (5) ◽  
pp. 1372-1380 ◽  
Author(s):  
Emilie Wientjes ◽  
Ivo H.M. van Stokkum ◽  
Herbert van Amerongen ◽  
Roberta Croce
Keyword(s):  
Energy Transfer ◽  
Excitation Energy ◽  
Photosystem I ◽  
Light Harvesting ◽  
Excitation Energy Transfer ◽  
Higher Plant ◽  
Light Harvesting Complexes

scholarly journals Metal-Enhanced Fluorescence of Chlorophylls in Single Light-Harvesting Complexes

2009 ◽  
Vol 1208 ◽  
Author(s):  
Sebastian Mackowski ◽  
Dawid Piatkowski ◽  
Stephan Wörmke ◽  
Achim Hartschuh ◽  
Christoph Bräeuchle ◽  
...  
Keyword(s):  
Single Molecule ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Fluorescence Emission ◽  
Fold Increase ◽  
Metal Nanoparticle ◽  
Metal Nanostructures ◽  
Enhanced Fluorescence ◽  
Light Harvesting Complexes ◽  
Light Harvesting Complex

AbstractWe show that the fluorescence of peridinin-chlorophyll a-protein complexes can be strongly enhanced via coupling with plasmon excitations localized in metal nanostructures. The results of ensemble and single-molecule spectroscopy experiments at room temperature demonstrate six-fold increase of the emission intensity of the light-harvesting complex when it is placed in the vicinity of chemically prepared silver islands. Irrespective of the enhancement, we observe no effect of the metal nanoparticle on the fluorescence emission energy of the complex. This observation implies that plasmon excitations may be applied for controlling the optical properties of complex biomolecules.

scholarly journals Identification of distinct pH- and zeaxanthin-dependent quenching in LHCSR3 from Chlamydomonas reinhardtii

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Julianne M Troiano ◽  
Federico Perozeni ◽  
Raymundo Moya ◽  
Luca Zuliani ◽  
Kwangyrul Baek ◽  
...  
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Light Harvesting ◽  
Complex Stress ◽  
Oxygen Species ◽  
Absorbed Energy ◽  
Light Harvesting Complexes ◽  
Light Harvesting Complex ◽  
Photosynthetic Organisms

Under high light, oxygenic photosynthetic organisms avoid photodamage by thermally dissipating absorbed energy, which is called nonphotochemical quenching. In green algae, a chlorophyll and carotenoid-binding protein, light-harvesting complex stress-related (LHCSR3), detects excess energy via a pH drop and serves as a quenching site. Using a combined in vivo and in vitro approach, we investigated quenching within LHCSR3 from Chlamydomonas reinhardtii. In vitro two distinct quenching processes, individually controlled by pH and zeaxanthin, were identified within LHCSR3. The pH-dependent quenching was removed within a mutant LHCSR3 that lacks the residues that are protonated to sense the pH drop. Observation of quenching in zeaxanthin-enriched LHCSR3 even at neutral pH demonstrated zeaxanthin-dependent quenching, which also occurs in other light-harvesting complexes. Either pH- or zeaxanthin-dependent quenching prevented the formation of damaging reactive oxygen species, and thus the two quenching processes may together provide different induction and recovery kinetics for photoprotection in a changing environment.

scholarly journals Plant Physiology, 2021 Functional redox links between lumen thiol oxidoreductase1 and serine/threonine-protein kinase STN7

2021 ◽  
Author(s):  
Jianghao Wu ◽  
Liwei Rong ◽  
Weijun Lin ◽  
Lingxi Kong ◽  
Dengjie Wei ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Disulfide Bonds ◽  
Kinase Activity ◽  
Light Harvesting ◽  
Photosynthetic Electron Transport ◽  
State Transitions ◽  
Light Harvesting Complex ◽  
Light Harvesting Complex Ii

Abstract In response to changing light quantity and quality, photosynthetic organisms perform state transitions, a process which optimizes photosynthetic yield and mitigates photo-damage. The serine/threonine-protein kinase STN7 phosphorylates the light-harvesting complex of photosystem II (PSII; light-harvesting complex II), which then migrates from PSII to photosystem I (PSI), thereby rebalancing the light excitation energy between the photosystems and restoring the redox poise of the photosynthetic electron transport chain. Two conserved cysteines forming intra- or intermolecular disulfide bonds in the lumenal domain (LD) of STN7 are essential for the kinase activity although it is still unknown how activation of the kinase is regulated. In this study, we show lumen thiol oxidoreductase 1 (LTO1) is co-expressed with STN7 in Arabidopsis (Arabidopsis thaliana) and interacts with the LD of STN7 in vitro and in vivo. LTO1 contains thioredoxin (TRX)-like and vitamin K epoxide reductase domains which are related to the disulfide-bond formation system in bacteria. We further show that the TRX-like domain of LTO1 is able to oxidize the conserved lumenal cysteines of STN7 in vitro. In addition, loss of LTO1 affects the kinase activity of STN7 in Arabidopsis. Based on these results, we propose that LTO1 helps to maintain STN7 in an oxidized active state in state 2 through redox interactions between the lumenal cysteines of STN7 and LTO1.

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