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1.
Proc Natl Acad Sci U S A ; 117(26): 15354-15362, 2020 06 30.
Article in English | MEDLINE | ID: mdl-32541018

ABSTRACT

In photosynthetic electron transport, large multiprotein complexes are connected by small diffusible electron carriers, the mobility of which is challenged by macromolecular crowding. For thylakoid membranes of higher plants, a long-standing question has been which of the two mobile electron carriers, plastoquinone or plastocyanin, mediates electron transport from stacked grana thylakoids where photosystem II (PSII) is localized to distant unstacked regions of the thylakoids that harbor PSI. Here, we confirm that plastocyanin is the long-range electron carrier by employing mutants with different grana diameters. Furthermore, our results explain why higher plants have a narrow range of grana diameters since a larger diffusion distance for plastocyanin would jeopardize the efficiency of electron transport. In the light of recent findings that the lumen of thylakoids, which forms the diffusion space of plastocyanin, undergoes dynamic swelling/shrinkage, this study demonstrates that plastocyanin diffusion is a crucial regulatory element of plant photosynthetic electron transport.


Subject(s)
Magnoliopsida/physiology , Photosystem I Protein Complex/metabolism , Photosystem II Protein Complex/metabolism , Plastocyanin/metabolism , Computer Simulation , Electron Transport , Gene Expression Regulation, Plant/physiology , Models, Biological
2.
Photosynth Res ; 142(2): 137-151, 2019 Nov.
Article in English | MEDLINE | ID: mdl-31375979

ABSTRACT

Survival of phototrophic organisms depends on their ability to collect and convert enough light energy to support their metabolism. Phototrophs can extend their absorption cross section by using diverse pigments and by tuning the properties of these pigments via pigment-pigment and pigment-protein interaction. It is well known that some cyanobacteria can grow in heavily shaded habitats by utilizing far-red light harvested with far-red-absorbing chlorophylls d and f. We describe a red-shifted light-harvesting system based on chlorophyll a from a freshwater eustigmatophyte alga Trachydiscus minutus (Eustigmatophyceae, Goniochloridales). A comprehensive characterization of the photosynthetic apparatus of T. minutus is presented. We show that thylakoid membranes of T. minutus contain light-harvesting complexes of several sizes differing in the relative amount of far-red chlorophyll a forms absorbing around 700 nm. The pigment arrangement of the major red-shifted light-harvesting complex is similar to that of the red-shifted antenna of a marine alveolate alga Chromera velia. Evolutionary aspects of the algal far-red light-harvesting complexes are discussed. The presence of these antennas in eustigmatophyte algae opens up new ways to modify organisms of this promising group for effective use of far-red light in mass cultures.


Subject(s)
Fresh Water , Light-Harvesting Protein Complexes/metabolism , Light , Stramenopiles/metabolism , Stramenopiles/radiation effects , Diuron , Membrane Proteins/metabolism , Pigments, Biological/metabolism , Spectrometry, Fluorescence , Temperature , Thylakoids/metabolism
3.
Sci Rep ; 7(1): 11976, 2017 09 20.
Article in English | MEDLINE | ID: mdl-28931902

ABSTRACT

Diatoms greatly contribute to carbon fixation and thus strongly influence the global biogeochemical balance. Capable of chromatic acclimation (CA) to unfavourable light conditions, diatoms often dominate benthic ecosystems in addition to their planktonic lifestyle. Although CA has been studied at the molecular level, our understanding of this phenomenon remains incomplete. Here we provide new data to better explain the acclimation-associated changes under red-enhanced ambient light (RL) in diatom Phaeodactylum tricornutum, known to express a red-shifted antenna complex (F710). The complex was found to be an oligomer of a single polypeptide, Lhcf15. The steady-state spectroscopic properties of the oligomer were also studied. The oligomeric assembly of the Lhcf15 subunits is required for the complex to exhibit a red-shifted absorption. The presence of the red antenna in RL culture coincides with the development of a rounded phenotype of the diatom cell. A model summarizing the modulation of the photosynthetic apparatus during the acclimation response to light of different spectral quality is proposed. Our study suggests that toggling between alternative organizations of photosynthetic apparatus and distinct cell morphologies underlies the remarkable acclimation capacity of diatoms.


Subject(s)
Aquatic Organisms/physiology , Aquatic Organisms/radiation effects , Diatoms/physiology , Diatoms/radiation effects , Light-Harvesting Protein Complexes/metabolism , Phenotype , Adaptation, Physiological , Protein Multimerization , Spectrum Analysis
4.
Photosynth Res ; 131(3): 255-266, 2017 Mar.
Article in English | MEDLINE | ID: mdl-27734239

ABSTRACT

Photosystem I (PSI) is a multi-subunit integral pigment-protein complex that performs light-driven electron transfer from plastocyanin to ferredoxin in the thylakoid membrane of oxygenic photoautotrophs. In order to achieve the optimal photosynthetic performance under ambient irradiance, the absorption cross section of PSI is extended by means of peripheral antenna complexes. In eukaryotes, this role is played mostly by the pigment-protein complexes of the LHC family. The structure of the PSI-antenna supercomplexes has been relatively well understood in organisms harboring the primary plastid: red algae, green algae and plants. The secondary endosymbiotic algae, despite their major ecological importance, have so far received less attention. Here we report a detailed structural analysis of the antenna-PSI association in the stramenopile alga Nannochloropsis oceanica (Eustigmatophyceae). Several types of PSI-antenna assemblies are identified allowing for identification of antenna docking sites on the PSI core. Instances of departure of the stramenopile system from the red algal model of PSI-Lhcr structure are recorded, and evolutionary implications of these observations are discussed.


Subject(s)
Photosystem I Protein Complex/metabolism , Plastids/metabolism , Rhodophyta/metabolism , Spectrophotometry, Ultraviolet
5.
Biochim Biophys Acta Bioenerg ; 1858(1): 56-63, 2017 Jan.
Article in English | MEDLINE | ID: mdl-27737767

ABSTRACT

In the present work, we report the first comparative spectroscopic investigation between Photosystem I (PSI) complexes isolated from two red clade algae. Excitation energy transfer was measured in PSI from Chromera velia, an alga possessing a split PsaA protein, and from the model diatom Phaeodactylum tricornutum. In both cases, the estimated effective photochemical trapping time was in the 15-25ps range, i.e. twice as fast as higher plants. In contrast to green phototrophs, the trapping time was rather constant across the whole emission spectrum. The weak wavelength dependence was attributed to the limited presence of long-wavelength emitting chlorophylls, as verified by low temperature spectroscopy. As the trapping kinetics of C. velia PSI were barely distinguishable from those of P. tricornutum PSI, it was concluded that the scission of PsaA protein had no significant impact on the overall PSI functionality. In conclusion, the two red clade algae analysed here, carried amongst the most efficient charge separation so far reported for isolated Photosystems.


Subject(s)
Alveolata/metabolism , Photosystem I Protein Complex/metabolism , Rhodophyta/metabolism , Chlorophyll/metabolism , Diatoms/metabolism , Energy Transfer/physiology , Kinetics , Light-Harvesting Protein Complexes/metabolism , Spectrometry, Fluorescence
6.
Sci Rep ; 6: 25583, 2016 05 05.
Article in English | MEDLINE | ID: mdl-27149693

ABSTRACT

Spatial segregation of photosystems in the thylakoid membrane (lateral heterogeneity) observed in plants and in the green algae is usually considered to be absent in photoautotrophs possessing secondary plastids, such as diatoms. Contrary to this assumption, here we show that thylakoid membranes in the chloroplast of a marine diatom, Phaeodactylum tricornutum, contain large areas occupied exclusively by a supercomplex of photosystem I (PSI) and its associated Lhcr antenna. These membrane areas, hundreds of nanometers in size, comprise hundreds of tightly packed PSI-antenna complexes while lacking other components of the photosynthetic electron transport chain. Analyses of the spatial distribution of the PSI-Lhcr complexes have indicated elliptical particles, each 14 × 17 nm in diameter. On larger scales, the red-enhanced illumination exerts a significant effect on the ultrastructure of chloroplasts, creating superstacks of tens of thylakoid membranes.


Subject(s)
Chloroplasts/metabolism , Diatoms/metabolism , Light-Harvesting Protein Complexes/metabolism , Photosystem I Protein Complex/metabolism , Thylakoids/metabolism , Chloroplasts/radiation effects , Chloroplasts/ultrastructure , Diatoms/radiation effects , Diatoms/ultrastructure , Light , Microscopy, Electron, Transmission , Multiprotein Complexes/metabolism , Multiprotein Complexes/ultrastructure , Photosystem II Protein Complex/metabolism , Thylakoids/radiation effects , Thylakoids/ultrastructure
7.
Photosynth Res ; 130(1-3): 137-150, 2016 Dec.
Article in English | MEDLINE | ID: mdl-26913864

ABSTRACT

We present proteomic, spectroscopic, and phylogenetic analysis of light-harvesting protein (Lhc) function in oleaginous Nannochloropsis oceanica (Eustigmatophyta, Stramenopila). N. oceanica utilizes Lhcs of multiple classes: Lhcr-type proteins (related to red algae LHCI), Lhcv (VCP) proteins (violaxanthin-containing Lhcs related to Lhcf/FCP proteins of diatoms), Lhcx proteins (related to Lhcx/LhcSR of diatoms and green algae), and Lhc proteins related to Red-CLH of Chromera velia. Altogether, 17 Lhc-type proteins of the 21 known from genomic data were found in our proteomic analyses. Besides Lhcr-type antennas, a RedCAP protein and a member of the Lhcx protein subfamily were found in association with Photosystem I. The free antenna fraction is formed by trimers of a mixture of Lhcs of varied origins (Lhcv, Lhcr, Lhcx, and relatives of Red-CLH). Despite possessing several proteins of the Red-CLH-type Lhc clade, N. oceanica is not capable of chromatic adaptation under the same conditions as the diatom Phaeodactylum tricornutum or C. velia. In addition, a naming scheme of Nannochloropsis Lhcs is proposed to facilitate further work.


Subject(s)
Light-Harvesting Protein Complexes/chemistry , Stramenopiles/metabolism , Light-Harvesting Protein Complexes/genetics , Light-Harvesting Protein Complexes/metabolism , Photosystem I Protein Complex/metabolism , Phylogeny , Spectrophotometry, Ultraviolet , Stramenopiles/genetics , Tandem Mass Spectrometry
8.
Biochim Biophys Acta ; 1847(6-7): 534-43, 2015.
Article in English | MEDLINE | ID: mdl-25748970

ABSTRACT

The remarkable adaptability of diatoms living in a highly variable environment assures their prominence among marine primary producers. The present study integrates biochemical, biophysical and genomic data to bring new insights into the molecular mechanism of chromatic adaptation of pennate diatoms in model species Phaeodactylum tricornutum, a marine eukaryote alga possessing the capability to shift its absorption up to ~700 nm as a consequence of incident light enhanced in the red component. Presence of these low energy spectral forms of Chl a is manifested by room temperature fluorescence emission maximum at 710 nm (F710). Here we report a successful isolation of the supramolecular protein complex emitting F710 and identify a member of the Fucoxanthin Chlorophyll a/c binding Protein family, Lhcf15, as its key building block. This red-shifted antenna complex of P. tricornutum appears to be functionally connected to photosystem II. Phylogenetic analyses do not support relation of Lhcf15 of P. tricornutum to other known red-shifted antenna proteins thus indicating a case of convergent evolutionary adaptation towards survival in shaded environments.


Subject(s)
Adaptation, Physiological , Chlorophyll/metabolism , Color , Diatoms/physiology , Fluorescence , Light-Harvesting Protein Complexes/metabolism , Photosystem II Protein Complex/metabolism , Chlorophyll A , Light , Phylogeny , Spectrometry, Fluorescence , Spectrometry, Mass, Electrospray Ionization
9.
Biochim Biophys Acta ; 1837(6): 802-10, 2014 Jun.
Article in English | MEDLINE | ID: mdl-24486443

ABSTRACT

A novel chlorophyll a containing pigment-protein complex expressed by cells of Chromera velia adapted to growth under red/far-red illumination [1]. Purification of the complex was achieved by means of anion-exchange chromatography and gel-filtration. The antenna is shown to be an aggregate of ~20kDa proteins of the light-harvesting complex (LHC) family, unstable in the isolated form. The complex possesses an absorption maximum at 705nm at room temperature in addition to the main chlorophyll a maximum at 677nm producing the major emission band at 714nm at room temperature. The far-red absorption is shown to be the property of the isolated aggregate in the intact form and lost upon dissociation. The purified complex was further characterized by circular dichroism spectroscopy and fluorescence spectroscopy. This work thus identified the third different class of antenna complex in C. velia after the recently described FCP-like and LHCr-like antennas. Possible candidates for red antennas are identified in other taxonomic groups, such as eustigmatophytes and the relevance of the present results to other known examples of red-shifted antenna from other organisms is discussed. This work appears to be the first successful isolation of a chlorophyll a-based far-red antenna complex absorbing above 700nm unrelated to LHCI.


Subject(s)
Apicomplexa/metabolism , Chlorophyll/metabolism , Spectrometry, Fluorescence/methods , Spectrophotometry, Ultraviolet/methods , Anion Exchange Resins , Chlorophyll A , Chromatography, Gel , Chromatography, Ion Exchange , Circular Dichroism
10.
Biochim Biophys Acta ; 1827(6): 723-9, 2013 Jun.
Article in English | MEDLINE | ID: mdl-23428396

ABSTRACT

The structure and composition of the light harvesting complexes from the unicellular alga Chromera velia were studied by means of optical spectroscopy, biochemical and electron microscopy methods. Two different types of antennae systems were identified. One exhibited a molecular weight (18-19kDa) similar to FCP (fucoxanthin chlorophyll protein) complexes from diatoms, however, single particle analysis and circular dichroism spectroscopy indicated similarity of this structure to the recently characterized XLH antenna of xanthophytes. In light of these data we denote this antenna complex CLH, for "Chromera Light Harvesting" complex. The other system was identified as the photosystem I with bound Light Harvesting Complexes (PSI-LHCr) related to the red algae LHCI antennae. The result of this study is the finding that C. velia, when grown in natural light conditions, possesses light harvesting antennae typically found in two different, evolutionary distant, groups of photosynthetic organisms.


Subject(s)
Alveolata/metabolism , Light-Harvesting Protein Complexes/physiology , Photosynthesis , Chlorophyll Binding Proteins/physiology , Circular Dichroism , Photosystem I Protein Complex/physiology
11.
Plant Physiol ; 161(1): 497-507, 2013 Jan.
Article in English | MEDLINE | ID: mdl-23148078

ABSTRACT

The photosynthetic performance of plants is crucially dependent on the mobility of the molecular complexes that catalyze the conversion of sunlight to metabolic energy equivalents in the thylakoid membrane network inside chloroplasts. The role of the extensive folding of thylakoid membranes leading to structural differentiation into stacked grana regions and unstacked stroma lamellae for diffusion-based processes of the photosynthetic machinery is poorly understood. This study examines, to our knowledge for the first time, the mobility of photosynthetic pigment-protein complexes in unstacked thylakoid regions in the C3 plant Arabidopsis (Arabidopsis thaliana) and agranal bundle sheath chloroplasts of the C4 plants sorghum (Sorghum bicolor) and maize (Zea mays) by the fluorescence recovery after photobleaching technique. In unstacked thylakoid membranes, more than 50% of the protein complexes are mobile, whereas this number drops to about 20% in stacked grana regions. The higher molecular mobility in unstacked thylakoid regions is explained by a lower protein-packing density compared with stacked grana regions. It is postulated that thylakoid membrane stacking to form grana leads to protein crowding that impedes lateral diffusion processes but is required for efficient light harvesting of the modularly organized photosystem II and its light-harvesting antenna system. In contrast, the arrangement of the photosystem I light-harvesting complex I in separate units in unstacked thylakoid membranes does not require dense protein packing, which is advantageous for protein diffusion.


Subject(s)
Arabidopsis/metabolism , Photosynthesis , Photosystem I Protein Complex/metabolism , Photosystem II Protein Complex/metabolism , Thylakoids/metabolism , Arabidopsis/physiology , Chlorophyll/metabolism , Chlorophyll A , Diffusion , Electrophoresis, Polyacrylamide Gel , Fluorescence Recovery After Photobleaching , Light , Membrane Lipids/metabolism , Mesophyll Cells/metabolism , Microscopy, Confocal , Plant Leaves/metabolism , Plant Leaves/physiology , Protein Transport , Protoplasts/metabolism , Sorghum/metabolism , Sorghum/physiology , Species Specificity , Thylakoids/physiology , Zea mays/metabolism , Zea mays/physiology
12.
Proc Natl Acad Sci U S A ; 109(49): 20130-5, 2012 Dec 04.
Article in English | MEDLINE | ID: mdl-23169624

ABSTRACT

Unavoidable side reactions of photosynthetic energy conversion can damage the water-splitting photosystem II (PSII) holocomplex embedded in the thylakoid membrane system inside chloroplasts. Plant survival is crucially dependent on an efficient molecular repair of damaged PSII realized by a multistep repair cycle. The PSII repair cycle requires a brisk lateral protein traffic between stacked grana thylakoids and unstacked stroma lamellae that is challenged by the tight stacking and low protein mobility in grana. We demonstrated that high light stress induced two main structural changes that work synergistically to improve the accessibility between damaged PSII in grana and its repair machinery in stroma lamellae: lateral shrinkage of grana diameter and increased protein mobility in grana thylakoids. It follows that high light stress triggers an architectural switch of the thylakoid network that is advantageous for swift protein repair. Studies of the thylakoid kinase mutant stn8 and the double mutant stn7/8 demonstrate the central role of protein phosphorylation for the structural alterations. These findings are based on the elaboration of mathematical tools for analyzing confocal laser-scanning microscopic images to study changes in the sophisticated thylakoid architecture in intact protoplasts.


Subject(s)
Light/adverse effects , Photosynthesis/physiology , Photosystem II Protein Complex/metabolism , Protein Kinases/metabolism , Thylakoids/radiation effects , Arabidopsis , Fluorescence , Fluorescence Recovery After Photobleaching , Image Processing, Computer-Assisted , Immunoblotting , Microscopy, Confocal , Phosphorylation , Photosynthesis/radiation effects , Protein Kinases/genetics , Protein Transport/physiology , Spectrometry, Fluorescence , Thylakoids/metabolism , Time Factors
13.
Proc Natl Acad Sci U S A ; 108(50): 20248-53, 2011 Dec 13.
Article in English | MEDLINE | ID: mdl-22128333

ABSTRACT

The machinery that conducts the light-driven reactions of oxygenic photosynthesis is hosted within specialized paired membranes called thylakoids. In higher plants, the thylakoids are segregated into two morphological and functional domains called grana and stroma lamellae. A large fraction of the luminal volume of the granal thylakoids is occupied by the oxygen-evolving complex of photosystem II. Electron microscopy data we obtained on dark- and light-adapted Arabidopsis thylakoids indicate that the granal thylakoid lumen significantly expands in the light. Models generated for the organization of the oxygen-evolving complex within the granal lumen predict that the light-induced expansion greatly alleviates restrictions imposed on protein diffusion in this compartment in the dark. Experiments monitoring the redox kinetics of the luminal electron carrier plastocyanin support this prediction. The impact of the increase in protein mobility within the granal luminal compartment in the light on photosynthetic electron transport rates and processes associated with the repair of photodamaged photosystem II complexes is discussed.


Subject(s)
Arabidopsis Proteins/metabolism , Arabidopsis/metabolism , Chloroplast Proteins/metabolism , Thylakoids/metabolism , Arabidopsis/ultrastructure , Cytochromes f/metabolism , Darkness , Diffusion , Kinetics , Models, Biological , Oxidation-Reduction , Thylakoids/ultrastructure
14.
J Phys Chem B ; 114(28): 9275-82, 2010 Jul 22.
Article in English | MEDLINE | ID: mdl-20583762

ABSTRACT

Chlorophyll (Chl) a/b-binding proteins from Prochlorothrix hollandica known as Pcb antennae were studied by femtosecond transient absorption technique to identify energy transfer rates and pathways in Pcb and Pcb-PS I complexes. Carotenoids transfer energy to Chl with low efficiency of approximately 25% in Pcb complexes. Interestingly, analysis of transient absorption spectra identified a pathway from the hot S(1) state of zeaxanthin and/or beta-carotene as the major energy transfer channel between carotenoids and chlorophylls in Pcb whereas the S(2) state contributes only marginally to energy transfer. Due to energetic reasons, no energy transfer is possible via the relaxed S(1) state of carotenoids. The low overall energy transfer efficiency of carotenoids recognizes chlorophylls as the main light-harvesting pigments. Besides Chl a, presence of Chl b, which transfers energy to Chl a with nearly 100% efficiency, significantly broadens the spectral range accessible for light-harvesting and improves cross section of Pcb complexes. The major role of carotenoids in Pcb is photoprotection.


Subject(s)
Carotenoids/chemistry , Chlorophyll/chemistry , Photosystem I Protein Complex/chemistry , Prochlorothrix/enzymology , Chlorophyll A , Energy Transfer , Photosystem I Protein Complex/metabolism , Spectrometry, Fluorescence
15.
Am J Bot ; 97(7): 1229-40, 2010 Jul.
Article in English | MEDLINE | ID: mdl-21616874

ABSTRACT

PREMISE OF THE STUDY: Natural hybridization represents an important force driving plant evolution and affecting community structure and functioning. Hybridization may be overlooked, however, among morphologically highly uniform congeners. An excellent example of such a group is Eleocharis subgenus Limnochloa, which has no reliably proven hybrids. Does this reflect biological barriers to interspecific crosses or difficulties in detecting the hybrids? We tested the hypothesis that hybridization occurs among sympatric Eleocharis cellulosa, E. interstincta, and E. mutata in northern Belize, Central America. • METHODS: Morphometric study (407 plants) was followed by examination of inter-simple sequence repeat (ISSR) polymorphisms (44 plants) and ITS sequence variation (33 plants). • KEY RESULTS: Two putatively hybrid morphotypes were discerned-E. cellulosa-resembling and E. interstincta-resembling. DNA markers of E. cellulosa and E. interstincta displayed additive constitution in plants from one E. cellulosa-resembling population only. The other putatively hybrid populations contained ISSR and ITS markers of the species they resembled morphologically, several unique ISSR markers, and ITS sequences of an undescribed South American Limnochloa entity. DNA markers of E. mutata were absent in the putative hybrids. • CONCLUSIONS: Simultaneous use of various types of molecular markers can overcome many pitfalls of investigations concerning hybridization among closely related and morphologically similar species. Northern Belize represents a hybrid zone of E. cellulosa and E. interstincta. A third participant in the hybridization events occurring in this zone is an unknown Limnochloa lineage but is not E. mutata. Interspecific hybridization may play a significant role in the diversification of Eleocharis.

16.
Biochim Biophys Acta ; 1797(1): 89-97, 2010 Jan.
Article in English | MEDLINE | ID: mdl-19761753

ABSTRACT

The freshwater filamentous green oxyphotobacterium Prochlorothrix hollandica is an unusual oxygenic photoautotrophic cyanobacterium differing from most of the others by the presence of light-harvesting Pcb antenna binding both chlorophylls a and b and by the absence of phycobilins. The pigment-protein complexes of P. hollandica SAG 10.89 (CCAP 1490/1) were isolated from dodecylmaltoside solubilized thylakoid membranes on sucrose density gradient and characterized by biochemical, spectroscopic and immunoblotting methods. The Pcb antennae production is suppressed by high light conditions (>200 mumol photons m(-2) s(-1)) in P. hollandica. PcbC protein was found either in higher oligomeric states or coupled to PS I (forming antenna rings around PS I). PcbA and PcbB are most probably only very loosely bound to photosystems; we assume that these pigment-protein complexes function as low light-induced mobile antennae. Further, we have detected alpha-carotene in substantial quantities in P. hollandica thylakoid membranes, indicating the presence of chloroplast-like carotenoid synthetic pathway which is not present in common cyanobacteria.


Subject(s)
Photosynthesis/physiology , Prochlorothrix/metabolism , Chromatography, Gel , Chromatography, High Pressure Liquid , Electrophoresis, Polyacrylamide Gel , Immunoblotting , Light , Photosystem I Protein Complex/isolation & purification , Photosystem I Protein Complex/metabolism , Photosystem II Protein Complex/isolation & purification , Photosystem II Protein Complex/metabolism , Prochlorophytes/metabolism , Thylakoids/metabolism , Thylakoids/ultrastructure
17.
Biochim Biophys Acta ; 1767(6): 725-31, 2007 Jun.
Article in English | MEDLINE | ID: mdl-17346666

ABSTRACT

Structure and organisation of Photosystem I and Photosystem II isolated from red alga Cyanidium caldarium was determined by electron microscopy and single particle image analysis. The overall structure of Photosystem II was found to be similar to that known from cyanobacteria. The location of additional 20 kDa (PsbQ') extrinsic protein that forms part of the oxygen evolving complex was suggested to be in the vicinity of cytochrome c-550 (PsbV) and the 12 kDa (PsbU) protein. Photosystem I was determined as a monomeric unit consisting of PsaA/B core complex with varying amounts of antenna subunits attached. The number of these subunits was seen to be dependent on the light conditions used during cell cultivation. The role of PsaH and PsaG proteins of Photosystem I in trimerisation and antennae complexes binding is discussed.


Subject(s)
Cyanobacteria/chemistry , Photosystem I Protein Complex/chemistry , Photosystem II Protein Complex/chemistry , Rhodophyta/chemistry , Photosystem I Protein Complex/isolation & purification , Photosystem I Protein Complex/metabolism , Photosystem I Protein Complex/ultrastructure , Photosystem II Protein Complex/isolation & purification , Photosystem II Protein Complex/metabolism , Photosystem II Protein Complex/ultrastructure
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