ArticlePhotosynthesis research2015
Violaxanthin de-epoxidase disulphides and their role in activity and thermal stability.
Article in Photosynthesis research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 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
- Antioxidants Differentially Regulate Non-Photochemical Quenching.Plant, cell & environment · 2026Article
- Structure and regulation of violaxanthin de-epoxidase, a key enzyme in the photoprotection of photosynthesis.Plant physiology · 2026Review
- Mechanisms underpinning natural variation in non-photochemical quenching kinetics.Biochemical Society transactions · 2025Review
- Nitric Oxide and Melatonin Cross Talk on Photosynthetic Machinery.Molecules (Basel, Switzerland) · 2025Review
- Current Knowledge on Mechanisms Preventing Photosynthesis Redox Imbalance in Plants.Antioxidants (Basel, Switzerland) · 2021Review
- Lipid Dependence of Xanthophyll Cycling in Higher Plants and Algae.Frontiers in plant science · 2020Review
- Photosynthetic Accumulation of Lutein inMarine drugs · 2018Article
- Exploring the Valuable Carotenoids for the Large-Scale Production by Marine Microorganisms.Marine drugs · 2018Review
- Direct isolation of a functional violaxanthin cycle domain from thylakoid membranes of higher plants.Planta · 2017Article
- Molecular studies on structural changes and oligomerisation of violaxanthin de-epoxidase associated with the pH-dependent activation.Photosynthesis research · 2016Article
- Carotenoids from Haloarchaea and Their Potential in Biotechnology.Marine drugs · 2015Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Violaxanthin de-epoxidase (VDE) catalyses the conversion of violaxanthin to zeaxanthin at the lumen side of the thylakoids during exposure to intense light. VDE consists of a cysteine-rich N-terminal domain, a lipocalin-like domain and a negatively charged C-terminal domain. That the cysteines are important for the activity of VDE is well known, but in what way is less understood. In this study, wild-type spinach VDE was expressed in E. coli as inclusion bodies, refolded and purified to give a highly active and homogenous preparation. The metal content (Fe, Cu, Ni, Mn, Co and Zn) was lower than 1 mol% excluding a metal-binding function of the cysteines. To investigate which of the 13 cysteines that could be important for the function of VDE, we constructed mutants where the cysteines were replaced by serines, one by one. For 12 out of 13 mutants the activity dropped by more than 99.9%. A quantification of free cysteines showed that only the most N-terminal of these cysteines was in reduced form in the native VDE. A disulphide pattern in VDE of C9-C27, C14-C21, C33-C50, C37-C46, C65-C72 and C118-C284 was obtained after digestion of VDE with thermolysin followed by mass spectroscopy analysis of reduced versus non-reduced samples. The residual activity found for the mutants showed a variation that was consistent with the results obtained from mass spectroscopy. Reduction of the disulphides resulted in loss of a rigid structure and a decrease in thermal stability of 15 °C.
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