Flavodiiron Proteins Research Articles

Cyclic and pseudo-cyclic electron pathways play antagonistic roles during nitrogen deficiency in Chlamydomonas reinhardtii.

Nitrogen (N) scarcity frequently constrains global biomass productivity. N deficiency halts cell division, downregulates photosynthetic electron transfer, and enhances carbon storage. However, the molecular mechanism downregulating photosynthesis during N deficiency and its relationship with carbon storage are not fully understood. Proton Gradient Regulator-like 1 (PGRL1) controlling cyclic electron flow (CEF) and Flavodiiron proteins (FLV) involved in pseudo-CEF (PCEF) are major players in the acclimation of photosynthesis. To determine the role of PGRL1 or FLV in photosynthesis under N deficiency, we measured photosynthetic electron transfer, oxygen gas exchange, and carbon storage in Chlamydomonas reinhardtii pgrl1 and flvB knockout mutants. Under N deficiency, pgrl1 maintained higher net photosynthesis and O2 photoreduction rates and higher levels of Cytochrome b6f and PSI compared to the control and flvB. The photosynthetic activity of flvB and pgrl1 flvB double mutants decreased in response to N deficiency, similar to the control strains. Furthermore, the preservation of photosynthetic activity in pgrl1 was accompanied by an increased accumulation of triacylglycerol in certain genetic backgrounds but not others, highlighting the importance of gene-environment interaction in determining traits such as oil content. Our results suggest that in the absence of PGRL1-controlled CEF, FLV-mediated PCEF maintains net photosynthesis at a high level and that CEF and PCEF play antagonistic roles during N deficiency. They further illustrate how a strain's nutrient status and genetic makeup can affect regulation of photosynthetic energy conversion in relation to carbon storage and provide additional strategies for improving lipid productivity in algae.

Physcomitrium patens flavodiiron proteins form heterotetrametric complexes

Flavodiiron proteins (FLVs) catalyze the reduction of oxygen to water by using electrons from Photosystem I (PSI). In several photosynthetic organisms such as cyanobacteria, green algae, mosses and gymnosperms, FLV-dependent electron flow protects PSI from over-reduction and consequent damage especially under fluctuating light conditions. In this work we investigated biochemical and structural properties of FLVA and FLVB from the model moss Physcomitrium patens. The two proteins, expressed and purified from Escherichia coli, bind both iron and flavin cofactors and show NAD(P)H oxidase activity as well as oxygen reductase capacities. Moreover, the co-expression of both FLVA and FLVB, coupled to a tandem affinity purification procedure with two different affinity tags, enabled the isolation of the stable and catalytically active FLVA/B hetero tetrameric protein complex with cooperative nature. The multimeric organization was shown to be stabilized by inter-subunit disulfide bonds. This investigation provides valuable new information on the biochemical properties of FLVs, with new insights into their in vivo activity.

Flavodiiron proteins prevent the Mehler reaction in Chlamydomonas reinhardtii

Regulation of photosynthetic electron transfer is fundamental for energetic efficiency and coping with changing environmental factors. All plant groups, except angiosperms, use flavodiiron proteins (FDPs) on the acceptor side of photosystem I (PSI), putatively protecting from PSI photoinhibition under fluctuating light. An alternative electron flow during photosynthesis is the direct reduction of O2 with consequential production of reactive oxygen species (ROS; the Mehler reaction), but to what extent FDPs prevent this is unknown. Here, we quantified O2-dependent electron flow, photosystem activity and the Mehler reaction in Chlamydomonas reinhardtii. Near-infra red absorbance measurement of PSI reaction centre (P700) showed that FDPs remain active long after a dark-to-light transition and their activity increased under hyperoxia. Light-induced hydrogen peroxide (H2O2) production, as a marker of the Mehler reaction, was influenced by O2 concentration, and was up to 67 % higher in an FDP-deficient mutant (flvb) than in the wild-type under saturating constant light. In cultures kept under sub-saturating constant light, flvb produced 315 % more H2O2 and had lower PSII efficiency than wild-type. Inhibiting electron transfer out of photosystem II (PSII) with 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU) only partially blocked H2O2 production, particularly under hyperoxia, indicating that PSII was an additional ROS source. P700+ reduction in the dark in the presence of DCMU was faster in flvb than wild-type, revealing enhanced cyclic electron flow, which may also have led to PSI mediated Mehler reaction. We conclude that FDPs remain active in constant light and can prevent PSI mediated Mehler reaction, with relevance to PSII photoinhibition.

Reduction of molecular oxygen in flavodiiron proteins - Catalytic mechanism and comparison to heme-copper oxidases

The family of flavodiiron proteins (FDPs) plays an important role in the scavenging and detoxification of both molecular oxygen and nitric oxide. Using electrons from a flavin mononucleotide cofactor molecular oxygen is reduced to water and nitric oxide is reduced to nitrous oxide and water. While the mechanism for NO reduction in FDPs has been studied extensively, there is very little information available about O2 reduction. Here we use hybrid density functional theory (DFT) to study the mechanism for O2 reduction in FDPs. An important finding is that a proton coupled reduction is needed after the O2 molecule has bound to the diferrous diiron active site and before the OO bond can be cleaved. This is in contrast to the mechanism for NO reduction, where both NN bond formation and NO bond cleavage occurs from the same starting structure without any further reduction, according to both experimental and computational results. This computational result for the O2 reduction mechanism should be possible to evaluate experimentally. Another difference between the two substrates is that the actual OO bond cleavage barrier is low, and not involved in rate-limiting the reduction process, while the barrier connected with bond cleavage/formation in the NO reduction process is of similar height as the rate-limiting steps. We suggest that these results may be part of the explanation for the generally higher activity for O2 reduction as compared to NO reduction in most FDPs. Comparisons are also made to the O2 reduction reaction in the family of heme‑copper oxidases.

Molecular Genetic Dissection of the Regulatory Network of Proton Motive Force in Chloroplasts.

The proton motive force (pmf) generated across the thylakoid membrane rotates the Fo-ring of ATP synthase in chloroplasts. The pmf comprises two components: membrane potential (∆Ψ) and proton concentration gradient (∆pH). Acidification of the thylakoid lumen resulting from ∆pH downregulates electron transport in the cytochrome b6f complex. This process, known as photosynthetic control, is crucial for protecting photosystem I (PSI) from photodamage in response to fluctuating light. To optimize the balance between efficient photosynthesis and photoprotection, it is necessary to regulate pmf. Cyclic electron transport around PSI and pseudo-cyclic electron transport involving flavodiiron proteins contribute to the modulation of pmf magnitude. By manipulating the ratio between the two components of pmf, it is possible to modify the extent of photosynthetic control without affecting the pmf size. This adjustment can be achieved by regulating the movement of ions (such as K+ and Cl-) across the thylakoid membrane. Since ATP synthase is the primary consumer of pmf in chloroplasts, its activity must be precisely regulated to accommodate other mechanisms involved in pmf optimization. Although fragments of information about each regulatory process have been accumulated, a comprehensive understanding of their interactions is lacking. Here, I summarize current knowledge of the network for pmf regulation, mainly based on genetic studies.

The Tolerance of Gut Commensal Faecalibacterium to Oxidative Stress Is Strain Dependent and Relies on Detoxifying Enzymes.

Obligate anaerobic bacteria in genus Faecalibacterium are among the most dominant taxa in the colon of healthy individuals and contribute to intestinal homeostasis. A decline in the abundance of this genus is associated with the occurrence of various gastrointestinal disorders, including inflammatory bowel diseases. In the colon, these diseases are accompanied by an imbalance between the generation and elimination of reactive oxygen species (ROS), and oxidative stress is closely linked to disruptions in anaerobiosis. In this work, we explored the impact of oxidative stress on several strains of faecalibacteria. An in silico analysis of complete genomes of faecalibacteria revealed the presence of genes encoding O2- and/or ROS-detoxifying enzymes, including flavodiiron proteins, rubrerythrins, reverse rubrerythrins, superoxide reductases, and alkyl peroxidase. However, the presence and the number of these detoxification systems varied greatly among faecalibacteria. These results were confirmed by O2 stress survival tests, in which we found that strains differed widely in their sensitivity. We showed the protective role of cysteine, which limited the production of extracellular O2•- and improved the survival of Faecalibacterium longum L2-6 under high O2 tension. In the strain F. longum L2-6, we observed that the expression of genes encoding detoxifying enzymes was upregulated in the response to O2 or H2O2 stress but with different patterns of regulation. Based on these results, we propose a first model of the gene regulatory network involved in the response to oxidative stress in F. longum L2-6. IMPORTANCE Commensal bacteria in the genus Faecalibacterium have been proposed for use as next-generation probiotics, but efforts to cultivate and exploit the potential of these strains have been limited by their sensitivity to O2. More broadly, little is known about how commensal and health-associated bacterial species in the human microbiome respond to the oxidative stress that occurs as a result of inflammation in the colon. In this work, we provide insights regarding the genes that encode potential mechanisms of protection against O2 or ROS stress in faecalibacteria, which may facilitate future advances in work with these important bacteria.

Roles of ApcD and orange carotenoid protein in photoinduction of electron transport upon dark-light transition in the Synechocystis PCC 6803 mutant deficient in flavodiiron protein Flv1.

Flavodiiron proteins Flv1/Flv3 accept electrons from photosystem (PS) I. In this work we investigated light adaptation mechanisms of Flv1-deficient mutant of Synechocystis PCC 6803, incapable to form the Flv1/Flv3 heterodimer. First seconds of dark-light transition were studied by parallel measurements of light-induced changes in chlorophyll fluorescence, P700 redox transformations, fluorescence emission at 77K, and OCP-dependent fluorescence quenching. During the period of Calvin cycle activation upon dark-light transition, the linear electron transport (LET) in wild type is supported by the Flv1/Flv3 heterodimer, whereas in Δflv1 mutant activation of LET upon illumination is preceded by cyclic electron flow that maintains State 2. The State 2-State 1 transition and Orange Carotenoid Protein (OCP)-dependent non-photochemical quenching occur independently of each other, begin in about 10s after the illumination of the cells and are accompanied by a short-term re-reduction of the PSI reaction center (P700+). ApcD is important for the State 2-State 1 transition in the Δflv1 mutant, but S-M rise in chlorophyll fluorescence was not completely inhibited in Δflv1/ΔapcD mutant. LET in Δflv1 mutant starts earlier than the S-M rise in chlorophyll fluorescence, and the oxidation of plastoquinol (PQH2) pool promotes the activation of PSII, transient re-reduction of P700+ and transition to State 1. An attempt to induce state transition in the wild type under high intensity light using methyl viologen, highly oxidizing P700 and PQH2, was unsuccessful, showing that oxidation of intersystem electron-transport carriers might be insufficient for the induction of State 2-State 1 transition in wild type of Synechocystis under high light.

Electron transport in cyanobacterial thylakoid membranes: Are cyanobacteria simple models for photosynthetic organisms?

Cyanobacteria are structurally the simplest oxygenic phototrophs, which makes it difficult to understand the regulation of photosynthesis because the photosynthetic and respiratory processes share the same thylakoid membranes and cytosolic space. This review aimed to summarise the molecular mechanisms and in vivo activities of electron transport in cyanobacterial thylakoid membranes based on the latest progress in photosynthesis research in cyanobacteria. Photosynthetic linear electron transport for CO2 assimilation has the dominant electron flux in the thylakoid membranes. The capacity of O2 photoreduction in cyanobacteria is comparable to the photosynthetic CO2 assimilation, which is mediated by flavodiiron proteins. Additionally, cyanobacterial thylakoid membranes harbour the significant electron flux of respiratory electron transport through a homologue of respiratory complex I, which is also recognized as the part of cyclic electron transport chain if it is coupled with photosystem I in the light. Further, O2-independent alternative electron transports through hydrogenase and nitrate reductase function with reduced ferredoxin as the electron donor. Whereas all these electron transports are recently being understood one by one, the complexity as the whole regulatory system remains to be uncovered in near future.

Reduction of Nitric Oxide to Nitrous Oxide in Flavodiiron Proteins: Catalytic Mechanism and Plausible Intermediates

The flavin dependent nonheme diiron proteins comprise a family of enzymes, which can act as scavengers for both molecular oxygen and nitric oxide. The reduction of nitric oxide to nitrous oxide and water in flavodiiron proteins (FDPs) has been studied both experimentally and computationally, but the reaction mechanism is far from well understood. From experiments, it is known that two NO molecules can bind to the reduced active site, forming an observable diferrous dinitrosyl complex. A main question has been whether nitrous oxide can be formed directly from the diferrous dinitrosyl complex or if further reduction and/or protonation is needed to make this step feasible. Experiments have shown that nitrous oxide can be formed in a deflavinated form of the enzyme, indicating that further reduction is not needed. In the present study, hybrid density functional theory calculations are performed on a cluster model of the Thermotoga maritima FDP active site. We show that nitric oxide can be reduced to nitrous oxide and water using a direct coupling mechanism, i.e., without further additions to the reduced active site. The diferrous dinitrosyl complex can form an unstable N–N bridging hyponitrite intermediate, which can rotate into an N–O bond bridging hyponitrite with a low barrier. From this intermediate, the N–O bond cleavage leading to release of nitrous oxide is energetically feasible. An energy profile for the entire catalytic cycle of such a direct coupling mechanism is presented, and it is shown that the suggested mechanism agrees with data on FDP variants. Finally, an energy profile for the entire process starting with the fully reduced enzyme turning over four NO equivalents is constructed. This energy profile suggests explanations to experimentally observed states, such as the dihydroxyl form of the fully oxidized diferric state, and the difference with respect to returning to the original oxidized state after NO reduction between the flavinated and the deflavinated form of the enzyme.

Photosynthetic regulation in response to strontium stress in moss Racomitrium japonicum L.

Strontium (Sr2+) pollution and its biological effects are of great concern including photosynthetic regulation, which is fundamental to environmental responses, especially for bryophytes during their terrestrial adaptation. Alternative electron flows mediated by flavodiiron proteins (FLVs) and cyclic electron flow (CEF) in photosystem I (PSI) are crucial to abiotic stresses moss responses; however, little is known about the moss photosynthesis regulation under nuclide treatment. We measured chlorophyll fluorescence parameters in PSI, photosystem II (PSII) and the P700 redox state, oxidative stress in the moss Racomitrium japonicum under low (5mg/L), moderate (50mg/L) and high (500mg/L) Sr2+ stress level. Moderate and high Sr2+ stress triggered H2O2 and malondialdehyde (MDA) generation, and catalase (CAT) activity increases, which are involved in reactive oxygen species regulation. The significant PSII photochemistry (Fv/Fm), Chla/chlb, Y(I)/Y(II), Y(NA), Y(ND) and ETRI-ETRII decreases at moderate and high Sr2+, and the Y(I), Y(II) decreases at high Sr2+ revealed the photo-inhibition and photo-damage in PSI and PSII by moderate and high Sr2+ stress. The nonphotochemical quenching (NPQ) increased significantly at moderate and high Sr2+ stress, reflecting a heat-dissipation-related photo-protective mechanism in antenna system and reaction centers. Moreover, rapid re-oxidation of P700 indicated that FLV-dependent flows significantly regulated PSI redox state under moderate and high Sr2+ stress. and CEF upregulation was found at low Sr2+. Finally, photosynthetic acclimation to Sr2+ stress in R. japonicum was linked to FLVs and CEF adjustments.

Flv3A facilitates O2 photoreduction and affects H2 photoproduction independently of Flv1A in diazotrophic Anabaena filaments.

The model heterocyst-forming filamentous cyanobacterium Anabaena sp. PCC 7120 (Anabaena) is a typical example of a multicellular organism capable of simultaneously performing oxygenic photosynthesis in vegetative cells and O2 -sensitive N2 -fixation inside heterocysts. The flavodiiron proteins have been shown to participate in photoprotection of photosynthesis by driving excess electrons to O2 (a Mehler-like reaction). Here, we performed a phenotypic and biophysical characterization of Anabaena mutants impaired in vegetative-specific Flv1A and Flv3A in order to address their physiological relevance in the bioenergetic processes occurring in diazotrophic Anabaena under variable CO2 conditions. We demonstrate that both Flv1A and Flv3A are required for proper induction of the Mehler-like reaction upon a sudden increase in light intensity, which is likely important for the activation of carbon-concentrating mechanisms and CO2 fixation. Under ambient CO2 diazotrophic conditions, Flv3A is responsible for moderate O2 photoreduction, independently of Flv1A, but only in the presence of Flv2 and Flv4. Strikingly, the lack of Flv3A resulted in strong downregulation of the heterocyst-specific uptake hydrogenase, which led to enhanced H2 photoproduction under both oxic and micro-oxic conditions. These results reveal a novel regulatory network between the Mehler-like reaction and the diazotrophic metabolism, which is of great interest for future biotechnological applications.

The Dynamic Changes of Alternative Electron Flows upon Transition from Low to High Light in the Fern Cyrtomium fortune and the Gymnosperm Nageia nagi

In photosynthetic organisms except angiosperms, an alternative electron sink that is mediated by flavodiiron proteins (FLVs) plays the major role in preventing PSI photoinhibition while cyclic electron flow (CEF) is also essential for normal growth under fluctuating light. However, the dynamic changes of FLVs and CEF has not yet been well clarified. In this study, we measured the P700 signal, chlorophyll fluorescence, and electrochromic shift spectra in the fern Cyrtomium fortune and the gymnosperm Nageia nagi. We found that both species could not build up a sufficient proton gradient (∆pH) within the first 30 s after light abruptly increased. During this period, FLVs-dependent alternative electron flow was functional to avoid PSI over-reduction. This functional time of FLVs was much longer than previously thought. By comparison, CEF was highly activated within the first 10 s after transition from low to high light, which favored energy balancing rather than the regulation of a PSI redox state. When FLVs were inactivated during steady-state photosynthesis, CEF was re-activated to favor photoprotection and to sustain photosynthesis. These results provide new insight into how FLVs and CEF interact to regulate photosynthesis in non-angiosperms.

Functional redundancy between flavodiiron proteins and NDH-1 in Synechocystis sp. PCC 6803

Functional redundancy between flavodiiron proteins and NDH-1 in Synechocystis sp. PCC 6803

Nitrous Oxide Emissions from Nitrite Are Highly Dependent on Nitrate Reductase in the Microalga Chlamydomonas reinhardtii.

Nitrous oxide (N2O) is a powerful greenhouse gas and an ozone-depleting compound whose synthesis and release have traditionally been ascribed to bacteria and fungi. Although plants and microalgae have been proposed as N2O producers in recent decades, the proteins involved in this process have been only recently unveiled. In the green microalga Chlamydomonas reinhardtii, flavodiiron proteins (FLVs) and cytochrome P450 (CYP55) are two nitric oxide (NO) reductases responsible for N2O synthesis in the chloroplast and mitochondria, respectively. However, the molecular mechanisms feeding these NO reductases are unknown. In this work, we use cavity ring-down spectroscopy to monitor N2O and CO2 in cultures of nitrite reductase mutants, which cannot grow on nitrate or nitrite and exhibit enhanced N2O emissions. We show that these mutants constitute a very useful tool to study the rates and kinetics of N2O release under different conditions and the metabolism of this greenhouse gas. Our results indicate that N2O production, which was higher in the light than in the dark, requires nitrate reductase as the major provider of NO as substrate. Finally, we show that the presence of nitrate reductase impacts CO2 emissions in both light and dark conditions, and we discuss the role of NO in the balance between CO2 fixation and release.

Photosynthetic regulation in fluctuating light under combined stresses of high temperature and dehydration in three contrasting mosses

Photosynthesis regulation is fundamental for the response to environmental dynamics, especially for bryophytes during their adaptation to terrestrial life. Alternative electron flow mediated by flavodiiron proteins (FLV) and cyclic electron flow (CEF) around photosystem I (PSI) play seminal roles in the response to abiotic stresses in mosses; nevertheless, their correlation and relative contribution to photoprotection of mosses exposed to combined stresses remain unclear. In the present study, the photosynthetic performance and recovery capacity of three moss species from different growth habitats were examined during heat and dehydration with fluctuating light. Our results showed that dehydration at 22 °C for 24 h caused little photodamage, and most of the parameters recovered to their original values after rehydration. In contrast, dehydration at 38 °C caused drastic injuries, especially to PSII, which was mainly caused by the inactivation of non-photochemical quenching (NPQ). Dehydration also induced a high accumulation of O2- and H2O2. A consistently higher CEF as well as a positive correlation between CEF and FLV was observed in resistant R. japonicum, implying CEF played a more important protective role for R. japonicum. In H. plumaeforme and P. cuspidatum, the positive relationship under mild stress switched to negative when stress became severe. Therefore, FLV pathway was sensitive to environmental fluctuations and maybe less efficient than CEF thus, readily to be lost during land colonization and evolution in angiosperms. Our work provides insights into the coordination of various pathways to fine-tune photosynthetic protection and can be used as a basis for species screening and development of breeding strategies for degraded ecosystem restoration with pioneering mosses.

A natural fusion of flavodiiron, rubredoxin, and rubredoxin oxidoreductase domains is a self-sufficient water-forming oxidase of Trichomonas vaginalis

Microaerophilic pathogens such as Giardia lamblia, Entamoeba histolytica, and Trichomonas vaginalis have robust oxygen consumption systems to detoxify oxygen and maintain intracellular redox balance. This oxygen consumption results from H2O-forming NADH oxidase (NOX) activity of two distinct flavin-containing systems: H2O-forming NOXes and multicomponent flavodiiron proteins (FDPs). Neither system is membrane bound, and both recycle NADH into oxidized NAD+ while simultaneously removing O2 from the local environment. However, little is known about the specific contributions of these systems in T. vaginalis. In this study, we use bioinformatics and biochemical analyses to show that T. vaginalis lacks a NOX–like enzyme and instead harbors three paralogous genes (FDPF1–3), each encoding a natural fusion product between the N-terminal FDP, central rubredoxin (Rb), and C-terminal NADH:Rb oxidoreductase domains. Unlike a “stand-alone” FDP that lacks Rb and oxidoreductase domains, this natural fusion protein with fully populated flavin redox centers directly accepts reducing equivalents of NADH to catalyze the four-electron reduction of oxygen to water within a single polypeptide with an extremely high turnover. Furthermore, using single-particle cryo-EM, we present structural insights into the spatial organization of the FDP core within this multidomain fusion protein. Together, these results contribute to our understanding of systems that allow protozoan parasites to maintain optimal redox balance and survive transient exposure to oxic conditions.

Alternative photosynthesis pathways drive the algal CO2-concentrating mechanism.

Global photosynthesis consumes ten times more CO2 than net anthropogenic emissions, and microalgae account for nearly half of this consumption1. The high efficiency of algal photosynthesis relies on amechanism concentrating CO2 (CCM) at the catalytic site of the carboxylating enzyme RuBisCO, which enhances CO2 fixation2. Although many cellular components involved in the transport and sequestration of inorganic carbon have been identified3,4, how microalgae supply energy to concentrate CO2 against a thermodynamic gradient remains unknown4-6. Here we show that in the green alga Chlamydomonas reinhardtii, the combined action of cyclic electron flow and O2 photoreduction-which depend on PGRL1 and flavodiiron proteins, respectively-generate a low luminal pH that is essential for CCM function. We suggest that luminal protons are used downstream of thylakoid bestrophin-like transporters, probably for the conversion of bicarbonate to CO2. We further establish that an electron flow from chloroplast to mitochondria contributes to energizing non-thylakoid inorganic carbon transporters, probably by supplying ATP. We propose an integrated view of the network supplying energy to the CCM, and describe how algal cells distribute energy from photosynthesis to power different CCM processes. These results suggest a route for the transfer of a functional algal CCM to plants to improve crop productivity.

Flavodiiron proteins enhance the rate of CO2 assimilation in Arabidopsis under fluctuating light intensity.

The proton concentration gradient (ΔpH) and membrane potential (Δψ) formed across the thylakoid membrane contribute to ATP synthesis in chloroplasts. Additionally, ΔpH downregulates photosynthetic electron transport via the acidification of the thylakoid lumen. K+ exchange antiporter 3 (KEA3) relaxes this downregulation by substituting ΔpH with Δψ in response to fluctuation of light intensity. In the Arabidopsis (Arabidopsis thaliana) line overexpressing KEA3 (KEA3ox), the rate of electron transport is elevated by accelerating the relaxation of ΔpH after a shift from high light (HL) to low light. However, the plant cannot control electron transport toward photosystem I (PSI), resulting in PSI photodamage. In this study, we crossed the KEA3ox line with the line (Flavodiiron [Flv]) expressing the Flv proteins of Physcomitrium patens. In the double transgenic line (Flv-KEA3ox), electrons overloading toward PSI were pumped out by Flv proteins. Consequently, photodamage of PSI was alleviated to the wild-type level. The rate of CO2 fixation was enhanced in Flv and Flv-KEA3ox lines during HL periods of fluctuating light, although CO2 fixation was unaffected in any transgenic lines in constant HL. Upregulation of CO2 fixation was accompanied by elevated stomatal conductance in fluctuating light. Consistent with the results of gas exchange experiments, the growth of Flv and Flv-KEA3ox plants was better than that of WT and KEA3ox plants under fluctuating light.

The flip side of reactive oxygen species in the tropical disease‐Amoebiasis

Entamoeba histolytica is the conductive agent of amoebiasis. Upon the parasite's infection, macrophages and neutrophils are activated by interferon γ, IL-13 and tumour necrosis factor. These immune cells then carry out the amoebicidal activity by releasing nitric oxide synthase and reactive oxygen species (ROS). This review talks about the protective and destructive role of ROS in Eh.E.histolytica has defence strategies against oxidative stress which is a result of excess ROS production. They possess antioxidants for their defence such as L-Cysteine, flavodiiron proteins, peroxiredoxin and trichostatin A, which contribute to the parasite's virulence. The ROS are harmful to the host cells as excess ROS production stimulates cell death by mechanisms like apoptosis and necroptosis. NADPH oxidase (NOX) is a key source of ROS in mammalian cells and causes apoptosis of host cells via the protein kinase transduction pathway. This review provides insights into why NOX inhibitors that could be a potent antiparasitic drug, is not effective for in vivo purposes. This paper also gives an insight into a solution that could be a potent source in generating new treatment and vaccines for amoebiasis by targeting parasite development.

Roles of alternative electron flows in response to excess light in Ginkgo biloba

Ginkgo biloba L., the only surviving species of Ginkgoopsida, is a famous relict gymnosperm, it may provide new insight into the evolution of photosynthetic mechanisms. Flavodiiron proteins (FDPs) are conserved in nonflowering plants, but the role of FDPs in gymnosperms has not yet been clarified. In particular, how gymnosperms integrate FDPs and cyclic electron transport (CET) to better adapt to excess light is poorly understood. To elucidate these questions, we measured the P700 signal, chlorophyll fluorescence and electrochromic shift signal under fluctuating and constant light in G. biloba. Within the first seconds after light increased, G. biloba could not build up a sufficient proton gradient (ΔpH). Concomitantly, photo-reduction of O2 mediated by FDPs contributed to the rapid oxidation of P700 and protected PSI under fluctuating light. Therefore, in G. biloba, FDPs mainly protect PSI under fluctuating light at acceptor side. Under constant high light, the oxidation of PSI and the induction of non-photochemical quenching were attributed to the increase in ΔpH formation, which was mainly caused by the increase in CET rather than linear electron transport. Therefore, under constant light, CET finely regulates the PSI redox state and non-photochemical quenching through ΔpH formation, protecting PSI and PSII against excess light. We conclude that, in G. biloba, FDPs are particularly important under fluctuating light while CET is essential under constant high light. The coordination of FDPs and CET fine-tune photosynthetic apparatus under excess light.