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Cryo-EM structures of light-harvesting 2 complexes from Rhodopseudomonas palustris reveal the molecular origin of absorption tuning

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Significance The light-harvesting (LH) complexes of phototrophic bacteria absorb solar energy for photosynthesis, and it is important to understand how the protein components influence the way bound pigments absorb light.… Click to show full abstract

Significance The light-harvesting (LH) complexes of phototrophic bacteria absorb solar energy for photosynthesis, and it is important to understand how the protein components influence the way bound pigments absorb light. We studied the LH2 complexes of Rhodopseudomonas palustris, which are encoded by a multigene family. Various combinations of LH2 genes were deleted, yielding strains that assemble only one of the four types of LH2. Following purification, the structures of four LH2 complexes were determined by cryogenic electron microscopy, revealing a basic nonameric ring structure comprising nine αβ-polypeptide pairs. An additional hitherto unknown polypeptide, γ, was found in each structure that binds six further bacteriochlorophylls. Comparison of these different structures shows how nature tunes their ability to absorb different wavelengths of light.

Keywords: cryo structures; complexes rhodopseudomonas; harvesting complexes; structures light; rhodopseudomonas palustris; light harvesting

Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Year Published: 2022

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