ArticleThe journal of physical chemistry letters2019
Molecular Mechanisms of Nonphotochemical Quenching in the LHCSR3 Protein of Chlamydomonas reinhardtii.
Article in The journal of physical chemistry letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 26 citations in OpenAlex.
- The Orange Carotenoid Protein Triggers Cyanobacterial Photoprotection by Quenching Bilins via a Structural Switch of Its Carotenoid.Journal of the American Chemical Society · 2024Article
- Ultrafast energy quenching mechanism of LHCSR3-dependent photoprotection in Chlamydomonas.Nature communications · 2024Article
- How the pH Controls Photoprotection in the Light-Harvesting Complex of Mosses.Journal of the American Chemical Society · 2023Article
- Biochemical and molecular properties of LHCX1, the essential regulator of dynamic photoprotection in diatoms.Plant physiology · 2022Article
- The Role of Acidic Residues in the C Terminal Tail of the LHCSR3 Protein ofThe journal of physical chemistry letters · 2021Article
- Article
- Chlamydomonas reinhardtii LHCSR1 and LHCSR3 proteins involved in photoprotective non-photochemical quenching have different quenching efficiency and different carotenoid affinity.Scientific reports · 2020Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Photosynthetic organisms possess photoprotection mechanisms from excess light conditions. The fastest response consists in the pH-triggered activation of a dissipation channel of the energy absorbed by the chlorophylls into heat, called nonphotochemical quenching. In green algae, the pigment binding complex LHCSR3 acts both as a chlorophyll quencher and as a pH detector. In this work, we study the quenching of the LHCSR3 protein in vitro considering two different protein aggregation states and two pH conditions using a combination of picosecond time-resolved photoluminescence and femtosecond transient absorption in the visible and NIR spectral regions. We find that the mechanisms at the basis of LHCSR3 quenching activity are always active, even at pH 7.5 and low aggregation. However, quenching efficiency is strongly enhanced by pH and by aggregation conditions. In particular, we find that electron transfer from carotenoids to chlorophylls is enhanced at low pH, while quenching mediated by protein-protein interactions is increased by going to a high aggregation state. We also observe a weak pH-dependent energy transfer from the chlorophylls to the S
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