ArticleThe Journal of biological chemistry
A new, unquenched intermediate of LHCII.
Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Carotenoids in the Context of the Mediterranean Dietary Pattern: From Food Matrix and Bioavailability to Biomarkers and Human Health.Antioxidants (Basel, Switzerland) · 2026Review
- Quick conversions and de novo synthesis within the entire α- and β-carotenoid branches during non-steady-state light transients.Photosynthesis research · 2026Article
- Nonphotochemical quenching in plants: Mechanisms and mysteries.The Plant cell · 2025Review
- In vivo detection of spectral reflectance changes associated with regulated heat dissipation mechanisms complements fluorescence quantum efficiency in early stress diagnosis.The New phytologist · 2025Article
- A perspective on the major light-harvesting complex dynamics under the effect of pH, salts, and the photoprotective PsbS protein.Photosynthesis research · 2023Review
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
When plants are exposed to high-light conditions, the potentially harmful excess energy is dissipated as heat, a process called non-photochemical quenching. Efficient energy dissipation can also be induced in the major light-harvesting complex of photosystem II (LHCII) in vitro, by altering the structure and interactions of several bound cofactors. In both cases, the extent of quenching has been correlated with conformational changes (twisting) affecting two bound carotenoids, neoxanthin, and one of the two luteins (in site L1). This lutein is directly involved in the quenching process, whereas neoxanthin senses the overall change in state without playing a direct role in energy dissipation. Here we describe the isolation of an intermediate state of LHCII, using the detergent n-dodecyl-α-D-maltoside, which exhibits the twisting of neoxanthin (along with changes in chlorophyll-protein interactions), in the absence of the L1 change or corresponding quenching. We demonstrate that neoxanthin is actually a reporter of the LHCII environment-probably reflecting a large-scale conformational change in the protein-whereas the appearance of excitation energy quenching is concomitant with the configuration change of the L1 carotenoid only, reflecting changes on a smaller scale. This unquenched LHCII intermediate, described here for the first time, provides for a deeper understanding of the molecular mechanism of quenching.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.