ArticlePhotosynthesis research2017
Pigment structure in the violaxanthin-chlorophyll-a-binding protein VCP.
Article in Photosynthesis research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 25 citations in OpenAlex.
- Exciton Delocalization Promotes Far-Red Absorption in a Tetrameric ChlorophyllJournal of the American Chemical Society · 2025Article
- Distribution, Biosynthesis, and Function of Carotenoids in Oxygenic Phototrophic Algae.Marine drugs · 2025Review
- Kinetics of the xanthophyll cycle and its role in photoprotective memory and response.Nature communications · 2023Article
- Enhancement of violaxanthin accumulation inFrontiers in microbiology · 2022Article
- Red-shifted light-harvesting system of freshwater eukaryotic alga Trachydiscus minutus (Eustigmatophyta, Stramenopila).Photosynthesis research · 2019Article
- Snapshot transient absorption spectroscopy: toward in vivo investigations of nonphotochemical quenching mechanisms.Photosynthesis research · 2019Article
- Pigment configuration in the light-harvesting protein of the xanthophyte alga Xanthonema debile.Photosynthesis research · 2018Article
- Optimum Production Conditions, Purification, Identification, and Antioxidant Activity of Violaxanthin from MicroalgaMarine drugs · 2018Article
- A new, unquenched intermediate of LHCII.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Resonance Raman spectroscopy was used to evaluate pigment-binding site properties in the violaxanthin-chlorophyll-a-binding protein (VCP) from Nannochloropsis oceanica. The pigments bound to this antenna protein are chlorophyll-a, violaxanthin, and vaucheriaxanthin. The molecular structures of bound Chl-a molecules are discussed with respect to those of the plant antenna proteins LHCII and CP29, the crystal structures of which are known. We show that three populations of carotenoid molecules are bound by VCP, each of which is in an all-trans configuration. We assign the lower-energy absorption transition of each of these as follows. One violaxanthin population absorbs at 485 nm, while the second population is red-shifted and absorbs at 503 nm. The vaucheriaxanthin population absorbs at 525 nm, a position red-shifted by 2138 cm
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Registered trials
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