Structure-based validation of recombinant light-harvesting complex II

Light-harvesting complex II (LHCII) captures sunlight and dissipates excess energy to drive photosynthesis. To elucidate this mechanism, the individual optical properties of pigments in the LHCII protein must be identified. In vitro reconstitution with apoproteins synthesized by and pigment-lipid mi...

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Bibliographic Details
Published in:PNAS nexus 2024-09, Vol.3 (9), p.pgae405
Main Authors: Seki, Soichiro, Miyata, Tomoko, Norioka, Naoko, Tanaka, Hideaki, Kurisu, Genji, Namba, Keiichi, Fujii, Ritsuko
Format: Article
Language:English
Subjects:
Amino acids
Analysis
Carotenoids
Chlorophyll
Cryoelectron microscopy
Electronics industry
Escherichia coli
Health aspects
Methods
Optical properties
Photosynthesis
Synthesis
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Summary:Light-harvesting complex II (LHCII) captures sunlight and dissipates excess energy to drive photosynthesis. To elucidate this mechanism, the individual optical properties of pigments in the LHCII protein must be identified. In vitro reconstitution with apoproteins synthesized by and pigment-lipid mixtures from natural sources is an effective approach; however, the local environment surrounding each pigment within reconstituted LHCII (rLHCII) has only been indirectly estimated using spectroscopic and biochemical methods. Here, we used cryo-electron microscopy to determine the 3D structure of the rLHCII trimer and found that rLHCII exhibited a structure that was virtually identical to that of native LHCII, with a few exceptions: some C-terminal amino acids were not visible, likely due to aggregation of the His-tags; a carotenoid at the V1 site was not visible; and at site 614 showed mixed occupancy by both chlorophyll and molecules. Our observations confirmed the applicability of the in vitro reconstitution technique.
ISSN:2752-6542
2752-6542
DOI:10.1093/pnasnexus/pgae405