This study evaluated the efficiency of green manure (+GM) on PSII efficiency throughout the day in Dalbergia ecastophyllum. The experiment was carried out in a disabled clay extraction deposit, located approximately 30 km south of São Mateus city (Espírito Santo State, Brazil). Chlorophyll (Chl) index, Chl a fluorescence, and plant growth were measured in the summer, after 12 months of planting. +GM improved the photochemical performance of D. ecastophyllum, reducing the occurrence of photoinhibition throughout the day. +GM increased the photochemical quantum yield, the probability of a photon absorbed to move beyond quinone QA -, and the total Chl index, resulting in higher plant height and stem diameter (+11.7 and +2.2%, respectively). The number of active reaction centers per cross-section and the performance index of PSII values were unchanged throughout the day. Full recovery of both K and L-bands occurred at night. In contrast, plants growing with -GM had higher energy losses as heat. In conclusion, these results contribute to improving revegetation techniques, to create better conditions for the planting of native tree species in degraded areas.

• Keywords
• chlorophyll a fluorescence transient, photosynthesis, revegetation,
• MeSH
• Chlorophyll A MeSH
• Chlorophyll metabolism   MeSH
• Dalbergia * radiation effects   growth & development   physiology   metabolism   MeSH
• Photosynthesis * MeSH
• Photosystem II Protein Complex metabolism   MeSH
• Manure * MeSH
• Mining * MeSH
• Trees radiation effects   growth & development   MeSH
• Light MeSH
• Publication type
• Journal Article MeSH
• Geographicals
• Brazil MeSH
• Names of Substances
• Chlorophyll A MeSH
• Chlorophyll MeSH
• Photosystem II Protein Complex MeSH
• Manure * MeSH

The growth of plants, algae, and cyanobacteria relies on the catalytic activity of the oxygen-evolving PSII complex, which uses solar energy to extract electrons from water to feed into the photosynthetic electron transport chain. PSII is proving to be an excellent system to study how large multi-subunit membrane-protein complexes are assembled in the thylakoid membrane and subsequently repaired in response to photooxidative damage. Here we summarize recent developments in understanding the biogenesis of PSII, with an emphasis on recent insights obtained from biochemical and structural analysis of cyanobacterial PSII assembly/repair intermediates. We also discuss how chlorophyll synthesis is synchronized with protein synthesis and suggest a possible role for PSI in PSII assembly. Special attention is paid to unresolved and controversial issues that could be addressed in future research.

• MeSH
• Chlorophyll metabolism   MeSH
• Photosynthesis MeSH
• Photosystem II Protein Complex * metabolism   MeSH
• Cyanobacteria * metabolism   MeSH
• Thylakoids metabolism   MeSH
• Publication type
• Journal Article MeSH
• Review MeSH
• Names of Substances
• Chlorophyll MeSH
• Photosystem II Protein Complex * MeSH

To keep up with the growth of human population and to circumvent deleterious effects of global climate change, it is essential to enhance crop yield to achieve higher production. Here we review mathematical models of oxygenic photosynthesis that are extensively used, and discuss in depth a subset that accounts for diverse approaches providing solutions to our objective. These include models (1) to study different ways to enhance photosynthesis, such as fine-tuning antenna size, photoprotection and electron transport; (2) to bioengineer carbon metabolism; and (3) to evaluate the interactions between the process of photosynthesis and the seasonal crop dynamics, or those that have included statistical whole-genome prediction methods to quantify the impact of photosynthesis traits on the improvement of crop yield. We conclude by emphasizing that the results obtained in these studies clearly demonstrate that mathematical modelling is a key tool to examine different approaches to improve photosynthesis for better productivity, while effective multiscale crop models, especially those that also include remote sensing data, are indispensable to verify different strategies to obtain maximized crop yields.

• Keywords
• C4 rice, Improving photosynthesis and crop yield, Leaf and crop models, Photorespiration bypasses, Photosynthesis models, Synthetic biology,
• MeSH
• Models, Biological MeSH
• Photosynthesis * physiology   MeSH
• Plant Leaves * physiology   metabolism   growth & development   MeSH
• Models, Theoretical MeSH
• Electron Transport MeSH
• Crops, Agricultural * growth & development   genetics   physiology   MeSH
• Publication type
• Journal Article MeSH
• Review MeSH

Photosystem II (PSII) represents the most vulnerable component of the photosynthetic machinery and its response in plants subjected to abiotic stress has been widely studied over many years. PSII is a thylakoid membrane-located multiprotein pigment complex that catalyses the light-induced electron transfer from water to plastoquinone with the concomitant production of oxygen. PSII is rich in intrinsic (PsbA and PsbD, namely D1 and D2, CP47 or PsbB and CP43 or PsbC) but also extrinsic proteins. The first ones are more largely conserved from cyanobacteria to higher plants while the extrinsic proteins are different among species. It has been found that extrinsic proteins involved in oxygen evolution change dramatically the PSII efficiency and PSII repair systems. However, little information is available on the effects of abiotic stress on their function and structure.

• Keywords
• abiotic stress, extrinsic protein, intrinsic protein, photosynthesis, photosystem II,
• Publication type
• Journal Article MeSH
• Review MeSH

Reactive oxygen species (ROS) are formed in photosystem II (PSII) under various types of abiotic and biotic stresses. It is considered that ROS play a role in chloroplast-to-nucleus retrograde signaling, which changes the nuclear gene expression. However, as ROS lifetime and diffusion are restricted due to the high reactivity towards biomolecules (lipids, pigments, and proteins) and the spatial specificity of signal transduction is low, it is not entirely clear how ROS might transduce signal from the chloroplasts to the nucleus. Biomolecule oxidation was formerly connected solely with damage; nevertheless, the evidence appears that oxidatively modified lipids and pigments are be involved in chloroplast-to-nucleus retrograde signaling due to their long diffusion distance. Moreover, oxidatively modified proteins show high spatial specificity; however, their role in signal transduction from chloroplasts to the nucleus has not been proven yet. The review attempts to summarize and evaluate the evidence for the involvement of ROS in oxidative signaling in PSII.

• Keywords
• Chloroplast-to-nucleus retrograde signaling, Lipid peroxidation, Protein oxidation, Reactive oxygen species,
• MeSH
• Chloroplasts * metabolism   MeSH
• Photosystem II Protein Complex * metabolism   MeSH
• Lipids MeSH
• Oxidative Stress MeSH
• Reactive Oxygen Species metabolism   MeSH
• Signal Transduction physiology   MeSH
• Publication type
• Journal Article MeSH
• Review MeSH
• Names of Substances
• Photosystem II Protein Complex * MeSH
• Lipids MeSH
• Reactive Oxygen Species MeSH

Oxygenic photosynthesis takes place in thylakoid membranes (TM) of cyanobacteria, algae, and higher plants. It begins with light absorption by pigments in large (modular) assemblies of pigment-binding proteins, which then transfer excitation energy to the photosynthetic reaction centers of photosystem (PS) I and PSII. In green algae and plants, these light-harvesting protein complexes contain chlorophylls (Chls) and carotenoids (Cars). However, cyanobacteria, red algae, and glaucophytes contain, in addition, phycobiliproteins in phycobilisomes that are attached to the stromal surface of TM, and transfer excitation energy to the reaction centers via the Chl a molecules in the inner antennas of PSI and PSII. The color and the intensity of the light to which these photosynthetic organisms are exposed in their environment have a great influence on the composition and the structure of the light-harvesting complexes (the antenna) as well as the rest of the photosynthetic apparatus, thus affecting the photosynthetic process and even the entire organism. We present here a perspective on 'Light Quality and Oxygenic Photosynthesis', in memory of George Christos Papageorgiou (9 May 1933-21 November 2020; see notes a and b). Our review includes (1) the influence of the solar spectrum on the antenna composition, and the special significance of Chl a; (2) the effects of light quality on photosynthesis, measured using Chl a fluorescence; and (3) the importance of light quality, intensity, and its duration for the optimal growth of photosynthetic organisms.

• Keywords
• Chl fluorescence induction, chromatic acclimation of cyanobacteria, photoreceptors, photosynthetic pigments, photosystems I and II, stomatal and chloroplast photoinduced movements,
• Publication type
• Journal Article MeSH
• Review MeSH

Photosystem II (PSII) is an intrinsic membrane protein complex that functions as a light-driven water:plastoquinone oxidoreductase in oxygenic photosynthesis. Electron transport in PSII is associated with formation of reactive oxygen species (ROS) responsible for oxidative modifications of PSII proteins. In this study, oxidative modifications of the D1 and D2 proteins by the superoxide anion (O2•-) and the hydroxyl (HO•) radicals were studied in WT and a tocopherol cyclase (vte1) mutant, which is deficient in the lipid-soluble antioxidant α-tocopherol. In the absence of this antioxidant, high-resolution tandem mass spectrometry was used to identify oxidation of D1:130E to hydroxyglutamic acid by O2•- at the PheoD1 site. Additionally, D1:246Y was modified to either tyrosine hydroperoxide or dihydroxyphenylalanine by O2•- and HO•, respectively, in the vicinity of the nonheme iron. We propose that α-tocopherol is localized near PheoD1 and the nonheme iron, with its chromanol head exposed to the lipid-water interface. This helps to prevent oxidative modification of the amino acid's hydrogen that is bonded to PheoD1 and the nonheme iron (via bicarbonate), and thus protects electron transport in PSII from ROS damage.

• Keywords
• EPR, mass spectrometry, photosystem II, reactive oxygen species, tocopherol,
• MeSH
• alpha-Tocopherol chemistry   metabolism   MeSH
• Amino Acids chemistry   metabolism   MeSH
• Arabidopsis enzymology   genetics   radiation effects   MeSH
• Photosynthesis physiology   radiation effects   MeSH
• Photosystem II Protein Complex chemistry   genetics   metabolism   MeSH
• Hydroxyl Radical chemistry   metabolism   MeSH
• Protein Interaction Domains and Motifs MeSH
• Intramolecular Transferases chemistry   genetics   metabolism   MeSH
• Protein Conformation, alpha-Helical MeSH
• Protein Conformation, beta-Strand MeSH
• Oxygen chemistry   metabolism   MeSH
• Models, Molecular MeSH
• Mutation MeSH
• Oxidation-Reduction MeSH
• Superoxides chemistry   metabolism   MeSH
• Light MeSH
• Thermodynamics MeSH
• Thermosynechococcus enzymology   genetics   radiation effects   MeSH
• Thylakoids enzymology   genetics   radiation effects   MeSH
• Protein Binding MeSH
• Binding Sites MeSH
• Iron chemistry   metabolism   MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Research Support, U.S. Gov't, Non-P.H.S. MeSH
• Names of Substances
• alpha-Tocopherol MeSH
• Amino Acids MeSH
• Photosystem II Protein Complex MeSH
• Hydroxyl Radical MeSH
• Intramolecular Transferases MeSH
• Oxygen MeSH
• Superoxides MeSH
• tocopherol cyclase MeSH Browser
• Iron MeSH

We explored photoprotective strategies in a cryptophyte alga Rhodomonas salina. This cryptophytic alga represents phototrophs where chlorophyll a/c antennas in thylakoids are combined with additional light-harvesting system formed by phycobiliproteins in the chloroplast lumen. The fastest response to excessive irradiation is induction of non-photochemical quenching (NPQ). The maximal NPQ appears already after 20 s of excessive irradiation. This initial phase of NPQ is sensitive to Ca2+ channel inhibitor (diltiazem) and disappears, also, in the presence of non-actin, an ionophore for monovalent cations. The prolonged exposure to high light of R. salina cells causes photoinhibition of photosystem II (PSII) that can be further enhanced when Ca2+ fluxes are inhibited by diltiazem. The light-induced reduction in PSII photochemical activity is smaller when compared with immotile diatom Phaeodactylum tricornutum. We explain this as a result of their different photoprotective strategies. Besides the protective role of NPQ, the motile R. salina also minimizes high light exposure by increased cell velocity by almost 25% percent (25% from 82 to 104 μm/s). We suggest that motility of algal cells might have a photoprotective role at high light because algal cell rotation around longitudinal axes changes continual irradiation to periodically fluctuating light.

• MeSH
• Chlorophyll A metabolism   MeSH
• Chlorophyll metabolism   MeSH
• Cryptophyta cytology   metabolism   radiation effects   MeSH
• Photosystem II Protein Complex metabolism   MeSH
• Cell Movement radiation effects   MeSH
• Light MeSH
• Calcium metabolism   MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Chlorophyll A MeSH
• Chlorophyll MeSH
• chlorophyll c MeSH Browser
• Photosystem II Protein Complex MeSH
• Calcium MeSH

Oxidative modification of proteins in photosystem II (PSII) exposed to high light has been studied for a few decades, but the characterization of protein radicals formed by protein oxidation is largely unknown. Protein oxidation is induced by the direct reaction of proteins with reactive oxygen species known to form highly reactive protein radicals comprising carbon-centered (alkyl) and oxygen-centered (peroxyl and alkoxyl) radicals. In this study, protein radicals were monitored in Arabidopsis exposed to high light by immuno-spin trapping technique based on the detection of 5,5-dimethyl-1-pyrroline N-oxide (DMPO) nitrone adducts using the anti-DMPO antibody. Protein radicals were imaged in Arabidopsis leaves and chloroplasts by confocal laser scanning microscopy using fluorescein conjugated with the anti-DMPO antibody. Characterization of protein radicals by standard blotting techniques using PSII protein specific antibodies shows that protein radicals are formed on D1, D2, CP43, CP47, and Lhcb3 proteins. Protein oxidation reflected by the appearance/disappearance of the protein bands reveals that formation of protein radicals was associated with protein fragmentation (cleavage of the D1 peptide bonds) and aggregation (cross-linking with another PSII subunits). Characterization of protein radical formation is important for better understating of the mechanism of oxidative modification of PSII proteins under high light.

• Keywords
• aggregate, fragment, hydroxyl radical, photosystem II, protein, protein radical, reactive oxygen species, singlet oxygen,
• Publication type
• Journal Article MeSH

It is well known that biological systems, such as microorganisms, plants, and animals, including human beings, form spontaneous electronically excited species through oxidative metabolic processes. Though the mechanism responsible for the formation of electronically excited species is still not clearly understood, several lines of evidence suggest that reactive oxygen species (ROS) are involved in the formation of electronically excited species. This review attempts to describe the role of ROS in the formation of electronically excited species during oxidative metabolic processes. Briefly, the oxidation of biomolecules, such as lipids, proteins, and nucleic acids by ROS initiates a cascade of reactions that leads to the formation of triplet excited carbonyls formed by the decomposition of cyclic (1,2-dioxetane) and linear (tetroxide) high-energy intermediates. When chromophores are in proximity to triplet excited carbonyls, the triplet-singlet and triplet-triplet energy transfers from triplet excited carbonyls to chromophores result in the formation of singlet and triplet excited chromophores, respectively. Alternatively, when molecular oxygen is present, the triplet-singlet energy transfer from triplet excited carbonyls to molecular oxygen initiates the formation of singlet oxygen. Understanding the mechanism of the formation of electronically excited species allows us to use electronically excited species as a marker for oxidative metabolic processes in cells.

• Keywords
• chromophores, electronically excited species, hydrogen peroxide, hydroxyl radical, oxidative radical reactions, reactive oxygen species, singlet oxygen, superoxide anion radical,
• MeSH
• Oxygen metabolism   MeSH
• Humans MeSH
• Oxidation-Reduction MeSH
• Energy Transfer MeSH
• Reactive Oxygen Species metabolism   MeSH
• Animals MeSH
• Check Tag
• Humans MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Review MeSH
• Names of Substances
• Oxygen MeSH
• Reactive Oxygen Species MeSH