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Protein redox regulation in the thylakoid lumen: the importance of disulfide bonds for violaxanthin de-epoxidase.
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- Additional Information
- Source:
Publisher: John Wiley & Sons Ltd Country of Publication: England NLM ID: 0155157 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-3468 (Electronic) Linking ISSN: 00145793 NLM ISO Abbreviation: FEBS Lett Subsets: MEDLINE
- Publication Information:
Publication: Jan. 2016- : West Sussex : John Wiley & Sons Ltd.
Original Publication: Amsterdam, North-Holland on behalf of the Federation of European Biochemical Societies.
- Subject Terms:
- Abstract:
When exposed to saturating light conditions photosynthetic eukaryotes activate the xanthophyll cycle where the carotenoid violaxanthin is converted into zeaxanthin by the enzyme violaxanthin de-epoxidase (VDE). VDE protein sequence includes 13 cysteine residues, 12 of which are strongly conserved in both land plants and algae. Site directed mutagenesis of Arabidopsis thaliana VDE showed that all these 12 conserved cysteines have a major role in protein function and their mutation leads to a strong reduction of activity. VDE is also shown to be active in its completely oxidized form presenting six disulfide bonds. Redox titration showed that VDE activity is sensitive to variation in redox potential, suggesting the possibility that dithiol/disulfide exchange reactions may represent a mechanism for VDE regulation.
(Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)
- Contributed Indexing:
Keywords: Carotenoid; Cysteine; Photosynthesis; Photosynthetic pigments; Xanthophyll cycle; Zeaxanthin
- Accession Number:
0 (Disulfides)
EC 1.- (Oxidoreductases)
EC 1.- (violaxanthin de-epoxidase)
- Publication Date:
Date Created: 20150310 Date Completed: 20150520 Latest Revision: 20220310
- Publication Date:
20250114
- Accession Number:
10.1016/j.febslet.2015.02.033
- Accession Number:
25747136
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