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Biochemical Society Transactions Apr 2022Light capture by chlorophylls and photosynthetic electron transport bury the risk of the generation of reactive oxygen species (ROS) including singlet oxygen, superoxide...
Light capture by chlorophylls and photosynthetic electron transport bury the risk of the generation of reactive oxygen species (ROS) including singlet oxygen, superoxide anion radicals and hydrogen peroxide. Rapid changes in light intensity, electron fluxes and accumulation of strong oxidants and reductants increase ROS production. Superoxide is mainly generated at the level of photosystem I while photosystem II is the main source of singlet oxygen. ROS can induce oxidative damage of the photosynthetic apparatus, however, ROS are also important to tune processes inside the chloroplast and participate in retrograde signalling regulating the expression of genes involved in acclimation responses. Under most physiological conditions light harvesting and photosynthetic electron transport are regulated to keep the level of ROS at a non-destructive level. Photosystem II is most prone to photoinhibition but can be quickly repaired while photosystem I is protected in most cases. The size of the transmembrane proton gradient is central for the onset of mechanisms that protect against photoinhibition. The proton gradient allows dissipation of excess energy as heat in the antenna systems and it regulates electron transport. pH-dependent slowing down of electron donation to photosystem I protects it against ROS generation and damage. Cyclic electron transfer and photoreduction of oxygen contribute to the size of the proton gradient. The yield of singlet oxygen production in photosystem II is regulated by changes in the midpoint potential of its primary quinone acceptor. In addition, numerous antioxidants inside the photosystems, the antenna and the thylakoid membrane quench or scavenge ROS.
Topics: Electron Transport; Light; Oxygen; Photosynthesis; Photosystem I Protein Complex; Photosystem II Protein Complex; Protons; Reactive Oxygen Species; Singlet Oxygen
PubMed: 35437580
DOI: 10.1042/BST20211246 -
Biochimica Et Biophysica Acta.... Feb 2020Hetero-oligomeric membrane protein complexes form the electron transport chain (ETC) of oxygenic photosynthesis. The ETC complexes undertake the light-driven vectorial...
Hetero-oligomeric membrane protein complexes form the electron transport chain (ETC) of oxygenic photosynthesis. The ETC complexes undertake the light-driven vectorial electron and proton transport reactions, which generate energy-rich ATP and electron-rich NADPH molecules for carbon fixation. The rate of photosynthetic electron transport depends on the availability of photons and the relative abundance of electron transport complexes. The relative abundance of the two photosystems, critical for the quantum efficiency of photosynthesis in changing light quality conditions, has been determined successfully by optical methods. Due to the lack of spectroscopic signatures, however, relatively little is known about the stoichiometry of other non-photosystem complexes in plant photosynthetic membrane. Here we determine the ratios of all major thylakoid-bound ETC complexes in Arabidopsis by a label-free quantitative mass spectrometry technique. The calculated stoichiometries are consistent with known subunit composition of complexes and current estimates of photosystem and cytochrome bf concentrations. The implications of these stoichiometries for photosynthetic light harvesting and the partitioning of electrons between the linear and cyclic electron transport pathways of photosynthesis are discussed.
Topics: Arabidopsis; Arabidopsis Proteins; Cytochrome b6f Complex; Photosynthesis; Thylakoids
PubMed: 31825808
DOI: 10.1016/j.bbabio.2019.148141 -
Journal of Molecular Biology Mar 2024Light is required for photosynthesis, but plants are often exposed to excess light, which can lead to photodamage and eventually cell death. To prevent this, they... (Review)
Review
Light is required for photosynthesis, but plants are often exposed to excess light, which can lead to photodamage and eventually cell death. To prevent this, they evolved photoprotective feedback mechanisms that regulate photosynthesis and trigger processes that dissipate light energy as heat, called non-photochemical quenching (NPQ). In excess light conditions, the light reaction and activity of Photosystem II (PSII) generates acidification of the thylakoid lumen, which is sensed by special pH-sensitive proteins called Photosystem II Subunit S (PsbS), actuating a photoprotective "switch" in the light-harvesting antenna. Despite its central role in regulating photosynthetic energy conversion, the molecular mechanism of PsbS as well as its interaction with partner proteins are not well understood. This review summarizes the current knowledge on the molecular structure and mechanistic aspects of the light-stress sensor PsbS and addresses open questions and challenges in the field regarding a full understanding of its functional mechanism and role in NPQ.
Topics: Light; Light-Harvesting Protein Complexes; Photosynthesis; Photosystem II Protein Complex; Plants; Protein Conformation
PubMed: 38109993
DOI: 10.1016/j.jmb.2023.168407 -
Plant Physiology and Biochemistry : PPB Feb 2020Cd, Cu, and Fe were used to reveal the specificity of their toxic actions. We studied the effects of heavy metals on the growth of barley seedlings, contents of cations...
Cd, Cu, and Fe were used to reveal the specificity of their toxic actions. We studied the effects of heavy metals on the growth of barley seedlings, contents of cations in leaves and chloroplasts, induced chlorophyll fluorescence and P light absorption. Differences were found at each level of research. We measured the contents of Cd, Cu, Fe, Mn, Zn, Ca, Mg, and K. The proportion of cations in leaves targeted to chloroplasts varied from 0.1% (K) to >90% (Fe). Their levels changed in different ways. We found no correlation between changes in cation contents in leaves and chloroplasts. Treatment with Cd, Cu, and Fe increased the contents of some cations. The extra portions were targeted primarily out of chloroplasts, which was most noticeable in the case of Cu and Fe. Cd treatment decreased non-photochemical quenching with concomitant increases in closed photosystem II. We introduced new coefficients qC for closed photosystem II and X(II) to compare the yields of photosystem II and photosystem I. Cd likely decreased both PSI content in leaves and its quantum yield. In control plants, the quantum yield ratio of PSI/PSII increased gradually from 1.25 under low light to 4 under high light. Cd treatment prevented the increase under moderate light; under high light the ratio reached 2. Cu treatment increased the acceptor side limitation of photosystem I under low light; components of the Calvin cycle likely demand more light for activation in Cu-treated plants.
Topics: Cadmium; Chlorophyll; Chloroplasts; Copper; Hordeum; Iron; Light; Metals, Heavy; Photosynthesis; Photosystem I Protein Complex; Photosystem II Protein Complex; Plant Leaves
PubMed: 31865165
DOI: 10.1016/j.plaphy.2019.12.006 -
Communications Biology Dec 2021Water molecules play a pivotal functional role in photosynthesis, primarily as the substrate for Photosystem II (PSII). However, their importance and contribution to...
Water molecules play a pivotal functional role in photosynthesis, primarily as the substrate for Photosystem II (PSII). However, their importance and contribution to Photosystem I (PSI) activity remains obscure. Using a high-resolution cryogenic electron microscopy (cryo-EM) PSI structure from a Chlamydomonas reinhardtii temperature-sensitive photoautotrophic PSII mutant (TSP4), a conserved network of water molecules - dating back to cyanobacteria - was uncovered, mainly in the vicinity of the electron transport chain (ETC). The high-resolution structure illustrated that the water molecules served as a ligand in every chlorophyll that was missing a fifth magnesium coordination in the PSI core and in the light-harvesting complexes (LHC). The asymmetric distribution of the water molecules near the ETC branches modulated their electrostatic landscape, distinctly in the space between the quinones and FX. The data also disclosed the first observation of eukaryotic PSI oligomerisation through a low-resolution PSI dimer that was comprised of PSI-10LHC and PSI-8LHC.
Topics: Chlamydomonas; Cryoelectron Microscopy; Mutation; Photosystem I Protein Complex; Photosystem II Protein Complex; Temperature
PubMed: 34887518
DOI: 10.1038/s42003-021-02911-7 -
Nature Communications Jun 2024Cryptophytes are ancestral photosynthetic organisms evolved from red algae through secondary endosymbiosis. They have developed alloxanthin-chlorophyll a/c2-binding...
Cryptophytes are ancestral photosynthetic organisms evolved from red algae through secondary endosymbiosis. They have developed alloxanthin-chlorophyll a/c2-binding proteins (ACPs) as light-harvesting complexes (LHCs). The distinctive properties of cryptophytes contribute to efficient oxygenic photosynthesis and underscore the evolutionary relationships of red-lineage plastids. Here we present the cryo-electron microscopy structure of the Photosystem II (PSII)-ACPII supercomplex from the cryptophyte Chroomonas placoidea. The structure includes a PSII dimer and twelve ACPII monomers forming four linear trimers. These trimers structurally resemble red algae LHCs and cryptophyte ACPI trimers that associate with Photosystem I (PSI), suggesting their close evolutionary links. We also determine a Chl a-binding subunit, Psb-γ, essential for stabilizing PSII-ACPII association. Furthermore, computational calculation provides insights into the excitation energy transfer pathways. Our study lays a solid structural foundation for understanding the light-energy capture and transfer in cryptophyte PSII-ACPII, evolutionary variations in PSII-LHCII, and the origin of red-lineage LHCIIs.
Topics: Photosystem II Protein Complex; Light-Harvesting Protein Complexes; Cryptophyta; Cryoelectron Microscopy; Photosynthesis; Models, Molecular; Energy Transfer; Photosystem I Protein Complex; Chlorophyll A
PubMed: 38866834
DOI: 10.1038/s41467-024-49453-0 -
Photochemical & Photobiological... May 2020The photosystems (PS), catalyzing the photosynthetic reactions of higher plants, are unevenly distributed in the thylakoid membrane: PSII, together with its light... (Review)
Review
The photosystems (PS), catalyzing the photosynthetic reactions of higher plants, are unevenly distributed in the thylakoid membrane: PSII, together with its light harvesting complex (LHC)II, is enriched in the appressed grana stacks, while PSI-LHCI resides in the non-appressed stroma thylakoids, which wind around the grana stacks. The two photosystems interact in a third membrane domain, the grana margins, which connect the grana and stroma thylakoids and allow the loosely bound LHCII to serve as an additional antenna for PSI. The light harvesting is balanced by reversible phosphorylation of LHCII proteins. Nevertheless, light energy also damages PSII and the repair process is regulated by reversible phosphorylation of PSII core proteins. Here, we discuss the detailed composition and organization of PSII-LHCII and PSI-LHCI (super)complexes in the thylakoid membrane of angiosperm chloroplasts and address the role of thylakoid protein phosphorylation in dynamics of the entire protein complex network of the photosynthetic membrane. Finally, we scrutinize the phosphorylation-dependent dynamics of the protein complexes in context of thylakoid ultrastructure and present a model on the reorganization of the entire thylakoid network in response to changes in thylakoid protein phosphorylation.
Topics: Arabidopsis; Phosphorylation; Photosystem I Protein Complex; Photosystem II Protein Complex; Thylakoids
PubMed: 32297616
DOI: 10.1039/d0pp00025f -
Photosynthesis Research Mar 2023Oxygenic photosynthesis is driven by the coupled action of the light-dependent pigment-protein complexes, photosystem I and II, located within the internal thylakoid...
Oxygenic photosynthesis is driven by the coupled action of the light-dependent pigment-protein complexes, photosystem I and II, located within the internal thylakoid membrane system. However, photosystem II is known to be prone to photooxidative damage. Thus, photosynthetic organisms have evolved a repair cycle to continuously replace the damaged proteins in photosystem II. However, it has remained difficult to deconvolute the damage and repair processes using traditional ensemble approaches. Here, we demonstrate an automated approach using time-lapse fluorescence microscopy and computational image analysis to study the dynamics and effects of photodamage in single cells at subcellular resolution in cyanobacteria. By growing cells in a two-dimensional layer, we avoid shading effects, thereby generating uniform and reproducible growth conditions. Using this platform, we analyzed the growth and physiology of multiple strains simultaneously under defined photoinhibitory conditions stimulated by UV-A light. Our results reveal an asymmetric cellular response to photodamage between sibling cells and the generation of an elusive subcellular structure, here named a 'photoendosome,' derived from the thylakoid which could indicate the presence of a previously unknown photoprotective mechanism. We anticipate these results to be a starting point for further studies to better understand photodamage and repair at the single-cell level.
Topics: Photosystem II Protein Complex; Light; Cell Lineage; Photosynthesis; Cyanobacteria
PubMed: 36581718
DOI: 10.1007/s11120-022-00986-9 -
Plant Physiology and Biochemistry : PPB May 2022Photosynthesis is crucial for the survival of all living biota, playing a key role in plant productivity by generating the carbon skeleton that is the primary component...
Photosynthesis is crucial for the survival of all living biota, playing a key role in plant productivity by generating the carbon skeleton that is the primary component of all biomolecules. Salinity stress is a major threat to agricultural productivity and sustainability as it can cause irreversible damage to photosynthetic apparatus at any developmental stage. However, the capacity of plants to become photosynthetically active under adverse saline conditions remains largely untapped. This study addresses this discrepancy by exploring the current knowledge on the impact of salinity on chloroplast operation, metabolism, chloroplast ultrastructure, and leaf anatomy, and highlights the dire consequences for photosynthetic machinery and stomatal conductance. We also discuss enhancing photosynthetic capacity by modifying and redistributing electron transport between photosystems and improving photosystem stability using genetic approaches, beneficial microbial inoculations, and root architecture changes to improve salt stress tolerance under field conditions. Understanding chloroplast operations and molecular engineering of photosynthetic genes under salinity stress will pave the way for developing salt-tolerant germplasm to ensure future sustainability by rehabilitating saline areas.
Topics: Chloroplasts; Photosynthesis; Salinity; Salt Stress; Salt Tolerance
PubMed: 35276596
DOI: 10.1016/j.plaphy.2022.03.003 -
Plant Cell Reports Apr 2022Glycinebetaine alleviates chilling stress by protecting photosystems I and II in BADH-transgenic and GB-treated tomato plants, which can be an effective strategy for...
Glycinebetaine alleviates chilling stress by protecting photosystems I and II in BADH-transgenic and GB-treated tomato plants, which can be an effective strategy for improving crop chilling tolerance. Tomato (Solanum lycopersicum) is one of the most cultivated vegetables in the world, but is highly susceptible to chilling stress and does not naturally accumulate glycinebetaine (GB), one of the most effective stress protectants. The protective mechanisms of GB on photosystem I (PSI) and photosystem II (PSII) against chilling stress, however, remain poorly understood. Here, we address this problem through exogenous GB application and generation of transgenic tomatoes (Moneymaker) with a gene encoding betaine aldehyde dehydrogenase (BADH), which is the key enzyme in the synthesis of GB, from spinach. Our results demonstrated that GB can protect chloroplast ultramicrostructure, alleviate PSII photoinhibition and maintain PSII stability under chilling stress. More importantly, GB increased the electron transfer between Q and Q and the redox potential of Q and maintained a high rate of cyclic electron flow around PSI, contributing to reduced production of reactive oxygen species, thereby mitigating PSI photodamage under chilling stress. Our results highlight the novel roles of GB in enhancing chilling tolerance via the protection of PSI and PSII in BADH transgenic and GB-treated tomato plants under chilling stress. Thus, introducing GB-biosynthetic pathway into tomato and exogenous GB application are effective strategies for improving chilling tolerance.
Topics: Betaine; Betaine-Aldehyde Dehydrogenase; Electrons; Solanum lycopersicum; Photosynthesis; Photosystem I Protein Complex; Photosystem II Protein Complex; Plants, Genetically Modified
PubMed: 35150305
DOI: 10.1007/s00299-022-02839-0