Molecular and Functional Characterization of Monodehydro-ascorbate and Dehydroascorbate Reductases

Сано, С.

doi:10.1007/978-3-319-74057-7_5

Cited by 8 publications

(12 citation statements)

References 155 publications

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“…The apparent K M of the novel DHAR was slightly higher than that of the classical DHARs, namely 2.00 mM for DHA and 12.71 mM for GSH. This suggests a lower level of activity, as reported for other chloroplast enzymes with a side DHAR activity [14]. In these proteins, the DHAR activity seems to be related to the presence of reactive cysteine residues in the active site [40], which are also present in the classical DHAR sequences [41].…”

Section: Discussionmentioning

confidence: 61%

“…This has been already reported as a common plant response to stress [26]. Additionally, in chloroplasts, the oxidized ASC can be alternatively reduced by ferredoxin-, glutathione-, and NAD(P)H-dependent pathways [14].…”

Section: Discussionmentioning

confidence: 75%

“…Similarly, the SDS-PAGE analysis revealed a major band having a molecular weight of roughly 26 kDa. For classical DHARs, apparent K M for DHA ranges from 0.07 to 0.50 mM, whereas from 0.04 to 10 mM for GSH [14]. The apparent K M of the novel DHAR was slightly higher than that of the classical DHARs, namely 2.00 mM for DHA and 12.71 mM for GSH.…”

Section: Discussionmentioning

confidence: 86%

“…This underlines that this enzyme plays a critical role in the ASC-GSH recycling reaction in higher plants [13]. DHAR activity has been identified in cytosol, chloroplasts, mitochondria, and peroxisomes [14], the latter three organelles being the compartments where the electron transport chains and photochemical reactions take place and reactive oxygen species (ROS) are generated the most [15]. So far, three different genes coding for DHAR have been found in Arabidopsis; they were localized in cytosol (DHAR2), peroxisomes (DHAR1), and in chloroplasts (DHAR3) [16].…”

Section: Introductionmentioning

confidence: 75%

“…Those proteins have not been reported to possess DHA reducing activity yet. However, other proteins, such as trypsin-like proteins, thioredoxin reductases, glutaredoxins, protein disulfide isomerases, discolorins, and the 3-α-hydroxysteroid dehydrogenase were shown to possess also DHAR activity [14,42,43], meaning that those proteins can reduce DHA as a result of a "side" activity. Nonetheless, it cannot be excluded that the SBPase and the RNA-binding protein may be part of a protein complex that possesses DHA reducing activity or function as auxiliary proteins, together with the proteins which showed a higher molecular weight in the SDS-PAGE (Figure 4, Panel C).…”

Section: Discussionmentioning

confidence: 99%

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A Novel and Potentially Multifaceted Dehydroascorbate Reductase Increasing the Antioxidant Systems is Induced by Beauvericin in Tomato

et al. 2020

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Dehydroascorbate reductases (DHARs) are important enzymes that reconvert the dehydroascorbic acid (DHA) into ascorbic acid (ASC). They are involved in the plant response to oxidative stress, such as that induced by the mycotoxin beauvericin (BEA). Tomato plants were treated with 50 µM of BEA; the main antioxidant compounds and enzymes were evaluated. DHARs were analyzed in the presence of different electron donors by native and denaturing electrophoresis as well as by western blot and mass spectrometry to identify a novel induced protein with DHAR activity. Kinetic parameters for dehydroascorbate (DHA) and glutathione (GSH) were also determined. The novel DHAR was induced after BEA treatment. It was GSH-dependent and possessed lower affinity to DHA and GSH than the classical DHARs. Interestingly, the mass spectrometry analysis of the main band appearing on sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) revealed a chloroplast sedoheptulose 1,7-bisphosphatase, a key enzyme of the Calvin cycle, and a chloroplast mRNA-binding protein, suggesting that the DHA reducing capacity could be a side activity or the novel DHAR could be part of a protein complex. These results shed new light on the ascorbate-glutathione regulation network under oxidative stress and may represent a new way to increase the plant antioxidant defense system, plant nutraceutical value, and the health benefits of plant consumption.

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Section: Discussionmentioning

confidence: 61%

Section: Discussionmentioning

confidence: 75%

Section: Discussionmentioning

confidence: 86%

Section: Introductionmentioning

confidence: 75%

Section: Discussionmentioning

confidence: 99%

See 3 more Smart Citations

A Novel and Potentially Multifaceted Dehydroascorbate Reductase Increasing the Antioxidant Systems is Induced by Beauvericin in Tomato

et al. 2020

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Unraveling the Dynamics of Antioxidant Defense in Plants Under Drought Conditions

Kumar

2024

Plant Secondary Metabolites and Abiotic Stress

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Cytological alterations and oxidative stress induced by Cerium and Neodymium in lentil seedlings and onion bulbs

Gjata

Tommasi²,

Leonardis³

et al. 2022

Front. Environ. Sci.

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Rare earth elements (REEs) are a group of 15 elements, the lanthanides and Yttrium and Scandium, with similar chemical and physical properties. Their use for many advanced technological applications remarkably increased in the last decades, and it was associated with an intensive extraction of such elements from their ores. Consequently, increasing amounts of either REE-containing by-products, deriving from the extraction process, and REE-containing wastes, deriving from the disposal of REE-containing devices, are reaching the environmental systems both at the local and global levels, as never in the past. Few data in the literature concern the effect (beneficial or toxic) induced by REEs application in terrestrial plant species and at different physiological stages. A set of experiments with exposure to two REEs was performed on some plants to evaluate this. Data of investigations focused on the exposure of lentil (Lens culinaris Medik.) seedlings and onion (Allium cepa L.) bulbs to cerium chloride (CeCl3) and neodymium chloride (NdCl3) at different concentrations for 72 h. Results showed alteration of the growth rate and the levels of some parameters considered as biomarkers of stress (reactive oxygen species and antioxidant systems). An increase in some mitotic aberrations was also observed in the root tissues of both species. The results indicate that the sensitivity of lentil in this bioassay is higher for lower concentrations compared to onion. Also, lower concentrations of these REEs had a positive effect on the growth rate of lentils underlining the complex interaction occurring between REEs and different plant organisms.

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Molecular and Functional Characterization of Monodehydro-ascorbate and Dehydroascorbate Reductases

Cited by 8 publications

References 155 publications

A Novel and Potentially Multifaceted Dehydroascorbate Reductase Increasing the Antioxidant Systems is Induced by Beauvericin in Tomato

A Novel and Potentially Multifaceted Dehydroascorbate Reductase Increasing the Antioxidant Systems is Induced by Beauvericin in Tomato

Unraveling the Dynamics of Antioxidant Defense in Plants Under Drought Conditions

Cytological alterations and oxidative stress induced by Cerium and Neodymium in lentil seedlings and onion bulbs

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