Photosynthesis is a crucial process that allows plants to convert carbon dioxide into organic compounds using solar energy. Light-harvesting complex II (LHCII) is a complex of pigment molecules bound to proteins. It switches between two main functions—dissipating harmful excess light energy as heat under high light intensity through nonphotochemical quenching, and transferring absorbed light to the reaction center with almost a unit efficiency under low light.
Bioengineering studies have shown that accelerating the transition between these two functions can increase photosynthetic efficiency—for example, soybean yields have been reported to increase by up to 33%. However, the atomic-level dynamic structural changes in LHCII that activate such allosteric regulation had not been previously elucidated.
The paper,"Cryo-EM Structures of LHCII in Photo-active and Photo-protecting States Reveal Allosteric Regulation of Light-Harvesting and Excess Energy-Dissipation," was published inAs part of their work, they reported a series of six cryo-EM structures, including the energy transfer state with LHCII in solution and the energy quenching state with laterally confined LHCII in membrane nanodiscs under both neutral and acidic conditions.
Comparison of these different structures shows that LHCII undergoes a conformational change upon acidification. This change allosterically alters the inter-pigment distance of the fluorescence quenching locus Lutein1 –Chlorophyll612 only when LHCII is confined in membrane nanodiscs, leading to the quenching of excited Chl612 by Lut1.
Through MSDFT calculations of cryo-EM structures and the known crystal structure in quenched states, together with transient fluorescence experiments, a significant quantum switching mechanism of LHCII has been revealed with Lut1–Chl612 distance as the key factor.
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