ArticleScientific reports2016
Structural understanding of the recycling of oxidized ascorbate by dehydroascorbate reductase (OsDHAR) from Oryza sativa L. japonica.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 66 citations in OpenAlex.
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- PbrWRKY62-PbrADC1 module involves in superficial scald development of Pyrus bretschneideri Rehd.fruit via regulating putrescine biosynthesis.Molecular horticulture · 2024Article
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- Over-Expression of Dehydroascorbate Reductase Improves Salt Tolerance, Environmental Adaptability and Productivity inAntioxidants (Basel, Switzerland) · 2022Article
- Reactive Oxygen Species, Antioxidant Responses and Implications from a Microbial Modulation Perspective.Biology · 2022Review
- Acetaminophen Induces an Antioxidative Response in Lettuce Plants.Plants (Basel, Switzerland) · 2021Article
- Recent Developments in Enzymatic Antioxidant Defence Mechanism in Plants with Special Reference to Abiotic Stress.Biology · 2021Review
- Proteomic Responses to Drought Vary Widely Among Eight Diverse Genotypes of Rice (International journal of molecular sciences · 2020Article
- Expression of HeterologousFrontiers in plant science · 2020Article
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- Regulation of Ascorbate-Glutathione Pathway in Mitigating Oxidative Damage in Plants under Abiotic Stress.Antioxidants (Basel, Switzerland) · 2019Review
- Ascorbic acid metabolism and functions: A comparison of plants and mammals.Free radical biology & medicine · 2018Review
- Arabidopsis thaliana dehydroascorbate reductase 2: Conformational flexibility during catalysis.Scientific reports · 2017Article
- Structure and catalytic mechanism of monodehydroascorbate reductase, MDHAR, from Oryza sativa L. japonica.Scientific reports · 2016Article
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dehydroascorbate reductase (DHAR) is a key enzyme involved in the recycling of ascorbate, which catalyses the glutathione (GSH)-dependent reduction of oxidized ascorbate (dehydroascorbate, DHA). As a result, DHAR regenerates a pool of reduced ascorbate and detoxifies reactive oxygen species (ROS). In previous experiments involving transgenic rice, we observed that overexpression of DHAR enhanced grain yield and biomass. Since the structure of DHAR is not available, the enzymatic mechanism is not well-understood and remains poorly characterized. To elucidate the molecular basis of DHAR catalysis, we determined the crystal structures of DHAR from Oryza sativa L. japonica (OsDHAR) in the native, ascorbate-bound, and GSH-bound forms and refined their resolutions to 1.9, 1.7, and 1.7 Å, respectively. These complex structures provide the first information regarding the location of the ascorbate and GSH binding sites and their interacting residues. The location of the ascorbate-binding site overlaps with the GSH-binding site, suggesting a ping-pong kinetic mechanism for electron transfer at the common Cys20 active site. Our structural information and mutagenesis data provide useful insights into the reaction mechanism of OsDHAR against ROS-induced oxidative stress in rice.
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