ArticleThe Journal of biological chemistry2010
Mutation analysis of violaxanthin de-epoxidase identifies substrate-binding sites and residues involved in catalysis.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 67 citations in OpenAlex.
- A Natural qE- and qZ-Deficient Alga Retains Functional Plant-Like and Chlorophycean Violaxanthin De-Epoxidases.bioRxiv : the preprint server for biology · 2026Article
- High-throughput Raman-activated cell sorting of microalgal genome-wide edited library revealed a regulatory pathway for carotenoid synthesis.Nature communications · 2026Article
- Structure and regulation of violaxanthin de-epoxidase, a key enzyme in the photoprotection of photosynthesis.Plant physiology · 2026Review
- The xanthophyll cycle balances photoprotection and photosynthetic efficiency in the seawater alga Nannochloropsis oceanica.Plant physiology · 2025Article
- Chloroplastic ascorbate modifies plant metabolism and may act as a metabolite signal regardless of oxidative stress.Plant physiology · 2024Article
- The ascorbate-glutathione cycle coming of age.Journal of experimental botany · 2024Review
- Chloroplast phosphate transporter CrPHT4-7 regulates phosphate homeostasis and photosynthesis in Chlamydomonas.Plant physiology · 2024Article
- The Functions of Chloroplastic Ascorbate in Vascular Plants and Algae.International journal of molecular sciences · 2023Review
- Effect of Salinity and Silicon Doses on Onion Post-Harvest Quality and Shelf Life.Plants (Basel, Switzerland) · 2022Article
- Metabolic engineering in food crops to enhance ascorbic acid production: crop biofortification perspectives for human health.Physiology and molecular biology of plants : an international journal of functional plant biology · 2022Review
- Chloroplast pH Homeostasis for the Regulation of Photosynthesis.Frontiers in plant science · 2022Review
- Characterization and functional validation of β-carotene hydroxylaseHorticulture research · 2022Article
- Lack of plastid-encoded Ycf10, a homolog of the nuclear-encoded DLDG1 and the cyanobacterial PxcA, enhances the induction of non-photochemical quenching in tobacco.Plant direct · 2021Article
- Article
- A blueprint for gene function analysis through Base Editing in the model plant Physcomitrium (Physcomitrella) patens.The New phytologist · 2021Article
- Essential components of the xanthophyll cycle differ in high and low toxin Karenia brevis.Harmful algae · 2021Article
- The Multiple Roles of Ascorbate in the Abiotic Stress Response of Plants: Antioxidant, Cofactor, and Regulator.Frontiers in plant science · 2021Review
- Evolutionary divergence of photoprotection in the green algal lineage: a plant-like violaxanthin de-epoxidase enzyme activates the xanthophyll cycle in the green alga Chlorella vulgaris modulating photoprotection.The New phytologist · 2020Article
- Triploid Citrus Genotypes Have a Better Tolerance to Natural Chilling Conditions of Photosynthetic Capacities and Specific Leaf Volatile Organic Compounds.Frontiers in plant science · 2020Article
- Ascorbate Deficiency Does Not Limit Nonphotochemical Quenching inPlant physiology · 2020Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plants are able to deal with variable environmental conditions; when exposed to strong illumination, they safely dissipate excess energy as heat and increase their capacity for scavenging reacting oxygen species. Both these protection mechanisms involve activation of the xanthophyll cycle, in which the carotenoid violaxanthin is converted to zeaxanthin by violaxanthin de-epoxidase, using ascorbate as the source of reducing power. In this work, following determination of the three-dimensional structure of the violaxanthin de-epoxidase catalytic domain, we identified the putative binding sites for violaxanthin and ascorbate by in silico docking. Amino acid residues lying in close contact with the two substrates were analyzed for their involvement in the catalytic mechanism. Experimental results supported the proposed substrate-binding sites and point to two residues, Asp-177 and Tyr-198, which are suggested to participate in the catalytic mechanism, based on complete loss of activity in mutant proteins. The role of other residues and the mechanistic similarity to aspartic proteases and epoxide hydrolases are discussed.
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