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Molecules (Basel, Switzerland) Oct 2021Single-walled carbon nanotubes (SWCNT) have recently been attracting the attention of plant biologists as a prospective tool for modulation of photosynthesis in higher...
Polymer-Modified Single-Walled Carbon Nanotubes Affect Photosystem II Photochemistry, Intersystem Electron Transport Carriers and Photosystem I End Acceptors in Pea Plants.
Single-walled carbon nanotubes (SWCNT) have recently been attracting the attention of plant biologists as a prospective tool for modulation of photosynthesis in higher plants. However, the exact mode of action of SWCNT on the photosynthetic electron transport chain remains unknown. In this work, we examined the effect of foliar application of polymer-grafted SWCNT on the donor side of photosystem II, the intersystem electron transfer chain and the acceptor side of photosystem I. Analysis of the induction curves of chlorophyll fluorescence via JIP test and construction of differential curves revealed that SWCNT concentrations up to 100 mg/L did not affect the photosynthetic electron transport chain. SWCNT concentration of 300 mg/L had no effect on the photosystem II donor side but provoked inactivation of photosystem II reaction centres and slowed down the reduction of the plastoquinone pool and the photosystem I end acceptors. Changes in the modulated reflection at 820 nm, too, indicated slower re-reduction of photosystem I reaction centres in SWCNT-treated leaves. We conclude that SWCNT are likely to be able to divert electrons from the photosynthetic electron transport chain at the level of photosystem I end acceptors and plastoquinone pool in vivo. Further research is needed to unequivocally prove if the observed effects are due to specific interaction between SWCNT and the photosynthetic apparatus.
Topics: Chlorophyll; Electron Transport; Fluorescence; Nanotubes, Carbon; Pisum sativum; Photosystem I Protein Complex; Photosystem II Protein Complex; Plant Leaves; Polymers
PubMed: 34641502
DOI: 10.3390/molecules26195958 -
Biochimica Et Biophysica Acta.... Nov 2023Phycobilisomes (PBSs), which are huge pigment-protein complexes displaying distinctive color variations, bind to photosystem cores for excitation-energy transfer. It is...
Phycobilisomes (PBSs), which are huge pigment-protein complexes displaying distinctive color variations, bind to photosystem cores for excitation-energy transfer. It is known that isolation of supercomplexes consisting of PBSs and photosystem I (PSI) or PBSs and photosystem II is challenging due to weak interactions between PBSs and the photosystem cores. In this study, we succeeded in purifying PSI-monomer-PBS and PSI-dimer-PBS supercomplexes from the cyanobacterium Anabaena sp. PCC 7120 grown under iron-deficient conditions by anion-exchange chromatography, followed by trehalose density gradient centrifugation. The absorption spectra of the two types of supercomplexes showed apparent bands originating from PBSs, and their fluorescence-emission spectra exhibited characteristic peaks of PBSs. Two-dimensional blue-native (BN)/SDS-PAGE of the two samples showed a band of CpcL, which is a linker protein of PBS, in addition to PsaA/B. Since interactions of PBSs with PSI are easily dissociated during BN-PAGE using thylakoids from this cyanobacterium grown under iron-replete conditions, it is suggested that iron deficiency for Anabaena induces tight association of CpcL with PSI, resulting in the formation of PSI-monomer-PBS and PSI-dimer-PBS supercomplexes. Based on these findings, we discuss interactions of PBSs with PSI in Anabaena.
Topics: Photosystem I Protein Complex; Thylakoids; Anabaena; Photosystem II Protein Complex; Cyanobacteria; Phycobilisomes; Iron
PubMed: 37321385
DOI: 10.1016/j.bbabio.2023.148993 -
Chemosphere Oct 2023Nitrogen pollution and pesticides such as photosystem II (PSII) inhibitor herbicides have several detrimental impacts on coral reefs, including breakdown of the...
Individual and combined effects of herbicide prometryn and nitrate enrichment at environmentally relevant concentrations on photosynthesis, oxidative stress, and endosymbiont community diversity of coral Acropora hyacinthus.
Nitrogen pollution and pesticides such as photosystem II (PSII) inhibitor herbicides have several detrimental impacts on coral reefs, including breakdown of the symbiosis between host corals and photosynthetic symbionts. Although nitrogen and PSII herbicide pollution separately cause coral bleaching, the combined effects of these stressors at environmentally relevant concentrations on corals have not been assessed. Here, we report the combined effects of nitrate enrichment and PSII herbicide (prometryn) exposure on photosynthesis, oxidative status and endosymbiont community diversity of the reef-building coral Acropora hyacinthus. Coral fragments were exposed in a mesocosm system to nitrate enrichment (9 μmol/L) and two prometryn concentrations (1 and 5 μg/L). The results showed that sustained prometryn exposure in combination with nitrate enrichment stress had significant detrimental impacts on photosynthetic apparatus [the maximum quantum efficiency of photosystem II (Fv/Fm), nonphotochemical quenching (NPQ) and oxidative status in the short term. Nevertheless, the adaptive mechanism of corals allowed the normal physiological state to be recovered following 1 μg/L prometryn and 9 μmol/L nitrate enrichment individual exposure. Moreover, exposure for 9 days was insufficient to trigger a shift in Symbiodiniaceae community. Most importantly, the negative impact of exposure to the combined environmental concentrations of 1 μg/L prometryn and 9 μmol/L nitrate enrichment was found to be significantly greater on the Fv/Fm, quantum yield of non-regulated energy dissipation [Y(NO)], NPQ, and oxidative status of corals compared to the impact of individual stressors. Our results show that interactions between prometryn stress and nitrate enrichment have a synergistic impact on the photosynthetic and oxidative stress responses of corals. This study provides valuable insights into combined effects of nitrate enrichment and PSII herbicides pollution for coral's physiology. Environmental concentrations of PSII herbicides may be more harmful to photosystems and antioxidant systems of corals under nitrate enrichment stress. Thus, future research and management of seawater quality stressors should consider combined impacts on corals rather than just the impacts of individual stressors alone.
Topics: Animals; Anthozoa; Prometryne; Nitrates; Hyacinthus; Herbicides; Photosystem II Protein Complex; Coral Reefs; Photosynthesis; Oxidative Stress; Symbiosis
PubMed: 37543226
DOI: 10.1016/j.chemosphere.2023.139729 -
Life (Basel, Switzerland) Nov 2021The energetics of photosynthesis in plants have been re-analyzed in a framework that represents the relatively high energy of O correctly. Starting with the photon...
The energetics of photosynthesis in plants have been re-analyzed in a framework that represents the relatively high energy of O correctly. Starting with the photon energy exciting P680 and "loosening an electron", the energy transfer and electron transport are represented in a comprehensive, self-explanatory sequence of redox energy transfer and release diagrams. The resulting expanded Z-scheme explicitly shows charge separation as well as important high-energy species such as O, Tyr˙, and P680˙, whose energies are not apparent in the classical Z-scheme of photosynthesis. Crucially, the energetics of the three important forms of P680 and of P700 are clarified. The relative free energies of oxidized and reduced species are shown explicitly in kJ/mol, not encrypted in volts. Of the chemical energy produced in photosynthesis, more is stored in O than in glucose. The expanded Z-scheme introduced here provides explanatory power lacking in the classical scheme. It shows that P680* is energetically boosted to P680˙ by the favorable electron affinity of pheophytin and that Photosystem I (PSI) has insufficient energy to split HO and produce O because P700* is too easily ionized. It also avoids the Z-scheme's bewildering implication, according to the "electron waterfall" concept, that HO gives off electrons that spontaneously flow to chlorophyll while releasing energy. The new analysis explains convincingly why plants need two different photosystems in tandem: (i) PSII mostly extracts hydrogen from HO, producing PQH (plastoquinol), and generates the energetically expensive product O; this step provides little energy directly to the plant; (ii) PSI produces chemical energy for the organism, by pumping protons against a concentration gradient and producing less reluctant hydrogen donors. It also documents that electron transport and energy transfer occur in opposite directions and do not involve redox voltages. The analysis makes it clear that the high-energy species in photosynthesis are unstable, electron-deficient species such as P680˙ and Tyr˙, not putative high-energy electrons.
PubMed: 34833066
DOI: 10.3390/life11111191 -
ACS Sensors Feb 2021Photosynthetic reactions in plants, algae, and cyanobacteria are driven by photosystem I and photosystem II complexes, which specifically reduce or oxidize partner redox...
Photosynthetic reactions in plants, algae, and cyanobacteria are driven by photosystem I and photosystem II complexes, which specifically reduce or oxidize partner redox biomolecules. Photosynthetic complexes can also bind synthetic organic molecules, which inhibit their photoactivity and can be used both to study the electron transport chain and as herbicides and algicides. Thus, their development, characterization, and sensing bears fundamental and applied interest. Substantial efforts have been devoted to developing photosensors based on photosystem II to detect compounds that bind to the plastoquinone sites of this complex. In comparison, photosystem I based sensors have received less attention and could be used to identify novel substances displaying phytotoxic effects, including those obtained from natural product extracts. We have developed a robust procedure to functionalize gold electrodes with photo- and redox-active photosystem I complexes based on transparent gold and a thiolate self-assembled monolayer, and we have obtained reproducible electrochemical photoresponses. Chronoamperometric recordings have allowed us to measure photocurrents in the presence of the viologen derivative paraquat at concentrations below 100 nM under lock-in operation and a sensor dynamic range spanning six orders of magnitude up to 100 mM. We have modeled their time course to identify the main electrochemical processes and limiting steps in the electron transport chain. Our results allow us to isolate the contributions from photosystem I and the redox mediator, and evaluate photocurrent features (spectral and power dependence, fast transient kinetics) that could be used as a sensing signal to detect other inhibitors and modulators of photosystem I activity.
Topics: Biosensing Techniques; Electron Transport; Paraquat; Photosystem I Protein Complex; Photosystem II Protein Complex
PubMed: 33591733
DOI: 10.1021/acssensors.1c00179 -
Postepy Biochemii Jun 2020The light phase of photosynthesis is a key energy process in higher plants. Its purpose is to convert light energy into chemical one stored in ATP and NADPH molecules,... (Review)
Review
The light phase of photosynthesis is a key energy process in higher plants. Its purpose is to convert light energy into chemical one stored in ATP and NADPH molecules, which are then used to assimilate CO2 and in numerous metabolic processes. Maintaining optimal photosynthesis performance requires strict regulation of thylakoid membranes organization and rapid response to changing environmental conditions. The main factor affecting photosynthesis is light, which, if applied in excessive amounts, leads to a slowdown in the process. Therefore, plants have developed many protective mechanisms regulating the light reactions of photosynthesis and operating at the level of light energy absorption, electron transport, and the distribution and use of reducing power. These include, among others: (i) non-photochemical energy quenching regulating the amount of excitation energy delivered to the photosystems; (ii) ‘state transition’ process redistributing excitation energy between photosystems; (iii) redundant electron transport pathways responsible for maintaining redox balance in chloroplasts. All these mechanisms, in combination with antioxidant systems, are designed to maintain the function of the photosynthetic apparatus in adverse growth conditions.
Topics: Chloroplasts; Electron Transport; Oxidation-Reduction; Photosynthesis; Plants
PubMed: 32700507
DOI: 10.18388/pb.2020_325 -
Plant & Cell Physiology Oct 2021Non-photochemical chlorophyll fluorescence quenching (NPQ) remains one of the most studied topics of the 21st century in photosynthesis research. Over the past... (Review)
Review
Non-photochemical chlorophyll fluorescence quenching (NPQ) remains one of the most studied topics of the 21st century in photosynthesis research. Over the past 30 years, profound knowledge has been obtained on the molecular mechanism of NPQ in higher plants. First, the largely overlooked significance of NPQ in protecting the reaction center of photosystem II (RCII) against damage, and the ways to assess its effectiveness are highlighted. Then, the key in vivo signals that can monitor the life of the major NPQ component, qE, are presented. Finally, recent knowledge on the site of qE and the possible molecular events that transmit ΔpH into the conformational change in the major LHCII [the major trimeric light harvesting complex of photosystem II (PSII)] antenna complex are discussed. Recently, number of reports on Arabidopsis mutants lacking various antenna components of PSII confirmed that the in vivo site of qE rests within the major trimeric LHCII complex. Experiments on biochemistry, spectroscopy, microscopy and molecular modeling suggest an interplay between thylakoid membrane geometry and the dynamics of LHCII, the PsbS (PSII subunit S) protein and thylakoid lipids. The molecular basis for the qE-related conformational change in the thylakoid membrane, including the possible onset of a hydrophobic mismatch between LHCII and lipids, potentiated by PsbS protein, begins to unfold.
Topics: Light; Photochemical Processes; Photosynthesis; Photosystem II Protein Complex; Plant Physiological Phenomena; Plants
PubMed: 33351147
DOI: 10.1093/pcp/pcaa155 -
Photosynthesis Research Mar 2023One of the main barriers to making efficient Photosystem I-based biohybrid solar cells is the need for an electrochemical pathway to facilitate electron transfer between...
One of the main barriers to making efficient Photosystem I-based biohybrid solar cells is the need for an electrochemical pathway to facilitate electron transfer between the P reaction center of Photosystem I and an electrode. To this end, nature provides inspiration in the form of cytochrome c, a natural electron donor to the P site. Its natural ability to access the P binding pocket and reduce the reaction center can be mimicked by employing cytochrome c, which has a similar protein structure and redox chemistry while also being compatible with a variety of electrode surfaces. Previous research has incorporated cytochrome c to improve the photocurrent generation of Photosystem I using time consuming and/or specialized electrode preparation. While those methods lead to high protein areal density, in this work we use the quick and facile vacuum-assisted drop-casting technique to construct a Photosystem I/cytochrome c photoactive composite film with micron-scale thickness. We demonstrate that this simple fabrication technique can result in high cytochrome c loading and improvement in cathodic photocurrent over a drop-casted Photosystem I film without cytochrome c. In addition, we analyze the behavior of the cytochrome c/Photosystem I system at varying applied potentials to show that the improvement in performance can be attributed to enhancement of the electron transfer rate to P sites and therefore the PSI turnover rate within the composite film.
Topics: Photosystem I Protein Complex; Cytochromes c; Solar Energy; Oxidation-Reduction; Electron Transport
PubMed: 36564600
DOI: 10.1007/s11120-022-00993-w -
Biochimica Et Biophysica Acta.... Apr 2023Knowledge about the exact abundance and ratio of photosynthetic protein complexes in thylakoid membranes is central to understanding structure-function relationships in...
Knowledge about the exact abundance and ratio of photosynthetic protein complexes in thylakoid membranes is central to understanding structure-function relationships in energy conversion. Recent modeling approaches for studying light harvesting and electron transport reactions rely on quantitative information on the constituent complexes in thylakoid membranes. Over the last decades several quantitative methods have been established and refined, enabling precise stoichiometric information on the five main energy-converting building blocks in the thylakoid membrane: Light-harvesting complex II (LHCII), Photosystem II (PSII), Photosystem I (PSI), cytochrome bf complex (cyt bf complex), and ATPase. This paper summarizes a few quantitative spectroscopic and biochemical methods that are currently available for quantification of plant thylakoid protein complexes. Two new methods are presented for quantification of LHCII and the cyt bf complex, which agree well with established methods. In addition, recent improvements in mass spectrometry (MS) allow deeper compositional information on thylakoid membranes. The comparison between mass spectrometric and more classical protein quantification methods shows similar quantities of complexes, confirming the potential of thylakoid protein complex quantification by MS. The quantitative information on PSII, PSI, and LHCII reveal that about one third of LHCII must be associated with PSI for a balanced light energy absorption by the two photosystems.
Topics: Thylakoids; Cytochrome b6f Complex; Cytochromes b; Light-Harvesting Protein Complexes; Photosystem I Protein Complex; Plant Proteins
PubMed: 36442511
DOI: 10.1016/j.bbabio.2022.148945 -
Photosynthesis Research Sep 2020Phycobiliproteins (PBPs) are pigment proteins that comprise phycobilisomes (PBS), major light-harvesting antenna complexes of cyanobacteria and red algae. PBS core...
Phycobiliproteins (PBPs) are pigment proteins that comprise phycobilisomes (PBS), major light-harvesting antenna complexes of cyanobacteria and red algae. PBS core substructures are made up of allophycocyanins (APs), a subfamily of PBPs. Five paralogous AP subunits are encoded by the Far-Red Light Photoacclimation (FaRLiP) gene cluster, which is transcriptionally activated in cells grown in far-red light (FRL; λ = 700 to 800 nm). FaRLiP gene expression enables some terrestrial cyanobacteria to remodel their PBS and photosystems and perform oxygenic photosynthesis in far-red light (FRL). Paralogous AP genes encoding a putative, FRL-absorbing AP (FRL-AP) are also found in an operon associated with improved low-light growth (LL; < 50 μmol photons m s) in some thermophilic Synechococcus spp., a phenomenon termed low-light photoacclimation (LoLiP). In this study, apc genes from FaRLiP and LoLiP gene clusters were heterologously expressed individually and in combinations in Escherichia coli. The resulting novel FRL-APs were characterized and identified as major contributors to the FRL absorbance observed in whole cells after FaRLiP and potentially LoLiP. Post-translational modifications of native FRL-APs from FaRLiP cyanobacterium, Leptolyngbya sp. strain JSC-1, were analyzed by mass spectrometry. The PBP complexes made in two FaRLiP organisms were compared, revealing strain-specific diversity in the FaRLiP responses of cyanobacteria. Through analyses of native and recombinant proteins, we improved our understanding of how different cyanobacterial strains utilize specialized APs to acclimate to FRL and LL. We discuss some insights into structural changes that may allow these APs to absorb longer light wavelengths than their visible-light-absorbing paralogs.
Topics: Bacterial Proteins; Cyanobacteria; Light; Light-Harvesting Protein Complexes; Photosystem I Protein Complex; Phycocyanin
PubMed: 32710194
DOI: 10.1007/s11120-020-00775-2