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Hydrogen peroxide (H₂O₂) is produced, via superoxide and superoxide dismutase, by electron transport in chloroplasts and mitochondria, plasma membrane NADPH oxidases, peroxisomal oxidases, type III peroxidases and other apoplastic oxidases. Intracellular transport is facilitated by aquaporins and H₂O₂ is removed by catalase, peroxiredoxin, glutathione peroxidase-like enzymes and ascorbate peroxidase, all of which have cell compartment-specific isoforms. Apoplastic H₂O₂ influences cell expansion, development and defence by its involvement in type III peroxidase-mediated polymer cross-linking, lignification and, possibly, cell expansion via H₂O₂-derived hydroxyl radicals. Excess H₂O₂ triggers chloroplast and peroxisome autophagy and programmed cell death. The role of H₂O₂ in signalling, for example during acclimation to stress and pathogen defence, has received much attention, but the signal transduction mechanisms are poorly defined. H₂O₂ oxidizes specific cysteine residues of target proteins to the sulfenic acid form and, similar to other organisms, this modification could initiate thiol-based redox relays and modify target enzymes, receptor kinases and transcription factors. Quantification of the sources and sinks of H₂O₂ is being improved by the spatial and temporal resolution of genetically encoded H₂O₂ sensors, such as HyPer and roGFP2-Orp1. These H₂O₂ sensors, combined with the detection of specific proteins modified by H₂O₂, will allow a deeper understanding of its signalling roles.

The stationary life of plants has led to the evolution of a complex gridded antioxidant defence system constituting numerous enzymatic components, playing a crucial role in overcoming various stress conditions. Mainly, these plant enzymes are superoxide dismutase (SOD), catalase (CAT), peroxidase (POX), glutathione peroxidase (GPX), glutathione reductase (GR), glutathione S-transferases (GST), ascorbate peroxidase (APX), monodehydroascorbate reductase (MDHAR), and dehydroascorbate reductase (DHAR), which work as part of the antioxidant defence system. These enzymes together form a complex set of mechanisms to minimise, buffer, and scavenge the reactive oxygen species (ROS) efficiently. The present review is aimed at articulating the current understanding of each of these enzymatic components, with special attention on the role of each enzyme in response to the various environmental, especially abiotic stresses, their molecular characterisation, and reaction mechanisms. The role of the enzymatic defence system for plant health and development, their significance, and cross-talk mechanisms are discussed in detail. Additionally, the application of antioxidant enzymes in developing stress-tolerant transgenic plants are also discussed.

Reactive oxygen species (ROS) originate as a natural byproduct in standard metabolism of oxygen activities. The principal sites of ROS generation in the cell are apoplast, mitochondria, chloroplasts, and peroxisomes. These ROS can induce cellular injuries by proteins oxidation, lipid peroxidation, and DNA damage, which finally may result in plant cellular death. Under regular circumstances, there is a steadiness between generation and elimination of ROS, but this balance is hampered by different biotic and abiotic stress factors such as exposure to heavy metals, high and low-light conditions, pathogens, insects and temperature extremes, resulting in a high generation of ROS which should be counteracted by the antioxidant machinery in cells. The antioxidant system of defense is composed by two groups: (i) Enzymatic antioxidants such as superoxide dismutase (SOD), catalase (CAT), ascorbate peroxidase (APX), general peroxidases (PRX) (e.g. guaiacol peroxidase GPX), glutathione reductase (GR), monodehydroascorbate reductase (MDHAR), and dehydroascorbate reductase (DHAR); (ii) Non-enzymatic antioxidants such as ascorbic acid (AA), reduced glutathione (GSH), α-tocopherol, carotenoids, plastoquinone/ubiquinone and flavonoids. These two groups of metabolites and enzymes work together with the main aim of ROS scavenging, but also in determining plant signaling, immune response, and plant growth and development. Finally, the molecular genetics of ROS genes and related metabolic pathways are briefly outlined, including gene isoforms, cellular localization, detection methods used and interactions amongst them. This information is crucial in better understanding and designing procedures for plants´stress tolerance; leading to a better management of agricultural plants under challenging and changing climatic conditions and food security.

Ascorbate peroxidase (APX; EC 1.11.1.11) activity and transcript levels of CrAPX1 , CrAPX2 , and CrAPX4 of Chlamydomonas reinhardtii increased under 1,400 μE·m −2 ·s −1 condition (HL). CrAPX4 expression was the most significant. So, CrAPX4 was downregulated using amiRNA technology to examine the role of APX for HL acclimation. The CrAPX4 knockdown amiRNA lines showed low APX activity and CrAPX4 transcript level without a change in CrAPX1 and CrAPX2 transcript levels, and monodehydroascorbate reductase (MDAR), dehydroascorbate reductase (DHAR), and glutathione reductase (GR) activities and transcript levels. Upon exposure to HL, CrAPX4 knockdown amiRNA lines appeared a modification in the expression of genes encoding the enzymes in the ascorbate–glutathione cycle, including an increase in transcript level of CrVTC2, a key enzyme for ascorbate (AsA) biosynthesis but a decrease in MDAR and DHAR transcription and activity after 1 h, followed by increases in reactive oxygen species production and lipid peroxidation after 6 h and exhibited cell death after 9 h. Besides, AsA content and AsA/DHA (dehydroascorbate) ratio decreased in CrAPX4 knockdown amiRNA lines after prolonged HL treatment. Thus, CrAPX4 induction together with its association with the modulation of MDAR and DHAR expression for AsA regeneration is critical for Chlamydomonas to cope with photo-oxidative stress.

Plants are exposed to various environmental stresses in their lifespan that threaten their survival. Reactive oxygen species (ROS), the byproducts of aerobic metabolism, are essential signalling molecules in regulating multiple plant developmental processes as well as in reinforcing plant tolerance to biotic and abiotic stimuli. However, intensified environmental challenges such as salinity, drought, UV irradiation, and heavy metals usually interfere with natural ROS metabolism and homeostasis, thus aggravating ROS generation excessively and ultimately resulting in oxidative stress. Cellular damage is confined to the degradation of biomolecular structures, including carbohydrates, proteins, lipids, pigments, and DNA. The nature of the double-edged function of ROS as a secondary messenger or harmful oxidant has been attributed to the degree of existing balance between cellular ROS production and ROS removal machinery. The activities of enzyme-based antioxidants, catalase (CAT, EC 1.11.1.6), monodehydroascorbate reductase (MDHAR, E.C.1.6.5.4), dehydroascorbate reductase (DHAR, EC 1.8.5.1), superoxide dismutase (SOD, EC 1.15.1.1), ascorbate peroxidase (APX, EC 1.11.1.11), glutathione reductase (GR, EC 1.6.4.2), and guaiacol peroxidase (GPX, EC 1.11.1.7); and non-enzyme based antioxidant molecules, ascorbate (AA), glutathione (GSH), carotenoids, α-tocopherol, prolines, flavonoids, and phenolics, are indeed parts of the defensive strategies developed by plants to scavenge excess ROS and to maintain cellular redox homeostasis during oxidative stress. This review briefly summarises current knowledge on enzymatic and non-enzymatic antioxidant machinery in plants. Moreover, additional information about the beneficial impact of the microbiome on countering abiotic/biotic stresses in association with roots and plant tissues has also been provided.

Reactive oxygen species (ROS) generation is a usual phenomenon in a plant both under a normal and stressed condition. However, under unfavorable or adverse conditions, ROS production exceeds the capacity of the antioxidant defense system. Both non-enzymatic and enzymatic components of the antioxidant defense system either detoxify or scavenge ROS and mitigate their deleterious effects. The Ascorbate-Glutathione (AsA-GSH) pathway, also known as Asada–Halliwell pathway comprises of AsA, GSH, and four enzymes viz. ascorbate peroxidase, monodehydroascorbate reductase, dehydroascorbate reductase, and glutathione reductase, play a vital role in detoxifying ROS. Apart from ROS detoxification, they also interact with other defense systems in plants and protect the plants from various abiotic stress-induced damages. Several plant studies revealed that the upregulation or overexpression of AsA-GSH pathway enzymes and the enhancement of the AsA and GSH levels conferred plants better tolerance to abiotic stresses by reducing the ROS. In this review, we summarize the recent progress of the research on AsA-GSH pathway in terms of oxidative stress tolerance in plants. We also focus on the defense mechanisms as well as molecular interactions.

Key message Overexpression of the heat-responsive ascorbate peroxidase gene NoAPX2430 improves thermotolerance and growth of Nannochloropsis oceanica , offering potential strategies for enhanced resilience in plant cells. Microalgae are promising for industrial lipid production but face challenges from high-temperature (HT) stress. This study focused on improving thermotolerance in Nannochloropsis oceanica by studying and modifying the heat-responsive ascorbate peroxidase gene, NoAPX2430 . Functional and localization analyses confirmed NoAPX2430 as an active enzyme in the chloroplast stroma. Knockdown of NoAPX2430 resulted in reduced growth, photosynthetic efficiency, and reactive oxygen species (ROS) scavenging under HT (35 °C). In contrast, overexpression of NoAPX2430 significantly improved photosynthetic performance, lowered ROS levels, and boosted growth rates. Additionally, lipid and triacylglycerol contents increased significantly under combined nitrogen depletion and HT, with polyunsaturated fatty acids rising by up to 194.4%. These results highlight NoAPX2430 ’s critical role in enhancing thermotolerance and lipid biosynthesis. This provides a foundation for genetic and environmental strategies to boost microalgal resilience and productivity for sustainable biofuel and nutraceutical development.

Background Celery is a widely cultivated vegetable abundant in ascorbate (AsA), a natural plant antioxidant capable of scavenging free radicals generated by abiotic stress in plants. Ascorbate peroxidase (APX) is a plant antioxidant enzyme that is important in the synthesis of AsA and scavenging of excess hydrogen peroxide. However, the characteristics and functions of APX in celery remain unclear to date. Results In this study, a gene encoding APX was cloned from celery and named AgAPX1 . The transcription level of the AgAPX1 gene was significantly upregulated under drought stress. AgAPX1 was expressed in Escherichia coli BL21 (DE3) and purified. The predicted molecular mass of rAgAPX1 was 33.16 kDa, which was verified by SDS-PAGE assay. The optimum pH and temperature for rAgAPX1 were 7.0 and 55 °C, respectively. Transgenic Arabidopsis hosting the AgAPX1 gene showed elevated AsA content, antioxidant capacity and drought resistance. Less decrease in net photosynthetic rate, chlorophyll content, and relative water content contributed to the high survival rate of transgenic Arabidopsis lines after drought. Conclusions The characteristics of APX in celery were different from that in other species. The enhanced drought resistance of overexpressing AgAPX1 in Arabidopsis may be achieved by increasing the accumulation of AsA, enhancing the activities of various antioxidant enzymes, and promoting stomatal closure. Our work provides new evidence to understand APX and its response mechanisms to drought stress in celery.

Lignin biosynthesis is evolutionarily conserved among higher plants and features a critical 3-hydroxylation reaction involving phenolic esters. However, increasing evidence questions the involvement of a single pathway to lignin formation in vascular plants. Here we describe an enzyme catalyzing the direct 3-hydroxylation of 4-coumarate to caffeate in lignin biosynthesis as a bifunctional peroxidase that oxidizes both ascorbate and 4-coumarate at comparable rates. A combination of biochemical and genetic evidence in the model plants Brachypodium distachyon and Arabidopsis thaliana supports a role for this coumarate 3-hydroxylase (C3H) in the early steps of lignin biosynthesis. The subsequent efficient O -methylation of caffeate to ferulate in grasses is substantiated by in vivo biochemical assays. Our results identify C3H as the only non-membrane bound hydroxylase in the lignin pathway and revise the currently accepted models of lignin biosynthesis, suggesting new gene targets to improve forage and bioenergy crops. Lignin biosynthesis in higher plants relies upon a 3-hydroxylation reaction that can occur via shikimate esters of 4-coumarate. Here, Barros et al. define an alternative biosynthetic pathway via cytosolic ascorbate peroxidase that can catalyze direct 3-hydroxylation of 4-coumarate.

Arbuscular mycorrhizal fungi (AMF) form symbiotic relationships with the roots of nearly all land-dwelling plants, increasing growth and productivity, especially during abiotic stress. AMF improves plant development by improving nutrient acquisition, such as phosphorus, water, and mineral uptake. AMF improves plant tolerance and resilience to abiotic stressors such as drought, salt, and heavy metal toxicity. These benefits come from the arbuscular mycorrhizal interface, which lets fungal and plant partners exchange nutrients, signalling molecules, and protective chemical compounds. Plants’ antioxidant defence systems, osmotic adjustment, and hormone regulation are also affected by AMF infestation. These responses promote plant performance, photosynthetic efficiency, and biomass production in abiotic stress conditions. As a result of its positive effects on soil structure, nutrient cycling, and carbon sequestration, AMF contributes to the maintenance of resilient ecosystems. The effects of AMFs on plant growth and ecological stability are species- and environment-specific. AMF’s growth-regulating, productivity-enhancing role in abiotic stress alleviation under abiotic stress is reviewed. More research is needed to understand the molecular mechanisms that drive AMF-plant interactions and their responses to abiotic stresses. AMF triggers plants’ morphological, physiological, and molecular responses to abiotic stress. Water and nutrient acquisition, plant development, and abiotic stress tolerance are improved by arbuscular mycorrhizal symbiosis. In plants, AMF colonization modulates antioxidant defense mechanisms, osmotic adjustment, and hormonal regulation. These responses promote plant performance, photosynthetic efficiency, and biomass production in abiotic stress circumstances. AMF-mediated effects are also enhanced by essential oils (EOs), superoxide dismutase (SOD), peroxidase (POD), ascorbate peroxidase (APX), hydrogen peroxide (H2O2), malondialdehyde (MDA), and phosphorus (P). Understanding how AMF increases plant adaptation and reduces abiotic stress will help sustain agriculture, ecosystem management, and climate change mitigation. Arbuscular mycorrhizal fungi (AMF) have gained prominence in agriculture due to their multifaceted roles in promoting plant health and productivity. This review delves into how AMF influences plant growth and nutrient absorption, especially under challenging environmental conditions. We further explore the extent to which AMF bolsters plant resilience and growth during stress.