The major light-harvesting chlorophyll a/b complex (LHCII) of the photosynthetic apparatus in green plants consists of a membrane protein and numerous noncovalently bound pigments that make up about one-third of the molecular mass of the pigment-protein complex. Due to this high pigment density, LHCII is potentially interesting as a light-harvesting component in synthetic constructs. However, for such applications its stability needs to be significantly improved. In this work, LHCII was dramatically stabilized by enclosing it within polymerizing colloidal silica. The entrapped LHCII stayed functional at 50 °C for up to 24 h instead of a few minutes in detergent solution and clearly showed energy transfer between complexes. Entrapment yield was enhanced by a polycationic peptide attached to the N terminus. Both the extent of stabilization and the yield of entrapment strongly increased with decreasing diameters of the silica particles.
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http://dx.doi.org/10.1021/la503858t | DOI Listing |
J Phys Chem Lett
December 2024
Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, 100190, China.
Light-harvesting complex II (LHCII), the most abundant membrane protein in photosystem II, plays dual roles, i.e., efficient light harvesting and energy transfer to the reaction center under low light conditions and dissipating excess energy as heat to prevent photodamage under high irradiation conditions.
View Article and Find Full Text PDFJ Chem Theory Comput
December 2024
The Graduate University for Advanced Studies (SOKENDAI), 38 Nishigo-Naka, Myodaiji, Okazaki, Aichi 444-8585, Japan.
The light-harvesting complex II (LHCII) in green plants exhibits highly efficient excitation energy transfer (EET). A comprehensive understanding of the EET mechanism in LHCII requires quantum chemical, molecular dynamics (MD), and statistical mechanics calculations that can adequately describe pigment molecules in heterogeneous environments. Herein, we develop MD simulation parameters that accurately reproduce the quantum mechanical/molecular mechanical energies of both the ground and excited states of all chlorophyll (Chl) molecules in membrane embedded LHCII.
View Article and Find Full Text PDFJ Phys Chem Lett
December 2024
Department of Chemistry, IIT Jodhpur, Jodhpur, Rajasthan 342037, India.
The plant thylakoid membrane hosting the light-harvesting complex (LHCII) is the site of oxygenic photosynthesis. Contrary to the earlier consensus of a protein-driven single lamellar phase of the thylakoid, despite containing 40% non-bilayer-forming lipids, recent experiments confirm the polymorphic state of the functional thylakoid. What, then, is the origin of this polymorphism and what factors control it? The current Letter addresses the question using a total of 617.
View Article and Find Full Text PDFJ Photochem Photobiol B
December 2024
Department of Biology, University of New Brunswick, Fredericton E3B5A3, NB, Canada. Electronic address:
Under ideal conditions, Chlamydomonas reinhardtii can photoacclimate to excess light through various short- and long-term mechanisms. However, how microalgae handle excess light stress once they exit exponential growth, and especially in stationary phase, is less understood. Our study explored C.
View Article and Find Full Text PDFSci Adv
December 2024
Department of Biology, Saint Louis University, St. Louis, MO, 63103, USA.
Photosystem II (PSII) splits water in oxygenic photosynthesis on Earth. The structure and function of the CSM-type PSII-LHCII (light-harvesting complex II) megacomplexes from the wild-type and PsbR-deletion mutant plants are studied through electron microscopy (EM), structural mass spectrometry, and ultrafast fluorescence spectroscopy [time-resolved fluorescence (TRF)]. The cryo-EM structure of a type I CSM megacomplex demonstrates that the three domains of PsbR bind to the stromal side of D1, D2, and CP43; associate with the single transmembrane helix of the redox active Cyt ; and stabilize the luminal extrinsic PsbP, respectively.
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