ArticleBiophysical journal2021
Membrane-dependent heterogeneity of LHCII characterized using single-molecule spectroscopy.
Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- LHCSR1 Functions as a Dimmer Switch for Light Harvesting.The journal of physical chemistry letters · 2026Article
- A design principle for tuning far-red absorption of chlorophyll a in light-harvesting complexes.Communications chemistry · 2026Article
- What are grana in chloroplasts of vascular plants good for?Annals of botany · 2026Review
- Ultrafast energy quenching mechanism of LHCSR3-dependent photoprotection in Chlamydomonas.Nature communications · 2024Article
- Energetic driving force for LHCII clustering in plant membranes.Science advances · 2023Article
- Cryo-EM structures of LHCII in photo-active and photo-protecting states reveal allosteric regulation of light harvesting and excess energy dissipation.Nature plants · 2023Article
- Energetic robustness to large scale structural fluctuations in a photosynthetic supercomplex.Nature communications · 2023Article
- Stimuli-Induced Subconformation Transformation of the PSI-LHCI Protein at Single-Molecule Resolution.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In green plants, light harvesting complex of Photosystem II (LHCII) absorbs and transports excitation energy toward the photosynthetic reaction centers and serves as a site for energy-dependent nonphotochemical quenching (qE), the photoprotective dissipation of energy as heat. LHCII is thought to activate dissipation through conformational changes that change the photophysical behaviors. Understanding this balance requires a characterization of how the conformations of LHCII, and thus its photophysics, are influenced by individual factors within the membrane environment. Here, we used ensemble and single-molecule fluorescence to characterize the excited-state lifetimes and switching kinetics of LHCII embedded in nanodisc- and liposome-based model membranes of various sizes and lipid compositions. As the membrane area decreased, the quenched population and the rate of conformational dynamics both increased because of interactions with other proteins, the aqueous solution, and/or disordered lipids. Although the conformational states and dynamics were similar in both thylakoid and asolectin lipids, photodegradation increased with thylakoid lipids, likely because of their charge and pressure properties. Collectively, these findings demonstrate the ability of membrane environments to tune the conformations and photophysics of LHCII.
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