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

The genomes of some purple photosynthetic bacteria contain a multigene puc family encoding a series of α- and β-polypeptides that together form a heterogeneous antenna of light-harvesting 2 (LH2) complexes. To unravel this complexity, we generated four sets of puc deletion mutants in Rhodopseudomonas palustris, each encoding a single type of pucBA gene pair and enabling the purification of complexes designated as PucA-LH2, PucB-LH2, PucD-LH2, and PucE-LH2. The structures of all four purified LH2 complexes were determined by cryogenic electron microscopy (cryo-EM) at resolutions ranging from 2.7 to 3.6 Å. Uniquely, each of these complexes contains a hitherto unknown polypeptide, γ, that forms an extended undulating ribbon that lies in the plane of the membrane and that encloses six of the nine LH2 αβ-subunits. The γ-subunit, which is located near to the cytoplasmic side of the complex, breaks the C9 symmetry of the LH2 complex and binds six extra bacteriochlorophylls (BChls) that enhance the 800-nm absorption of each complex. The structures show that all four complexes have two complete rings of BChls, conferring absorption bands centered at 800 and 850 nm on the PucA-LH2, PucB-LH2, and PucE-LH2 complexes, but, unusually, the PucD-LH2 antenna has only a single strong near-infared (NIR) absorption peak at 803 nm. Comparison of the cryo-EM structures of these LH2 complexes reveals altered patterns of hydrogen bonds between LH2 αβ-side chains and the bacteriochlorin rings, further emphasizing the major role that H bonds play in spectral tuning of bacterial antenna complexes

Rings, ellipses and horseshoes: how purple bacteria harvest solar energy

This Review summarises the current state of research on the structure and function of light-harvesting apparatus in purple photosynthetic bacteria. Particular emphasis is placed on the major open questions still outstanding in this field in addition to what is already known

The structure and function of bacterial light-harvesting complexes (Review)

The harvesting of solar radiation by purple photosynthetic bacteria is achieved by circular, integral membrane pigment-protein complexes. There are two main types of light-harvesting complex, termed LH2 and LH1, that function to absorb light energy and to transfer that energy rapidly and efficiently to the photochemical reaction centres where it is trapped. This mini-review describes our present understanding of the structure and function of the purple bacterial light-harvesting complexes

How purple photosynthetic bacteria harvest solar energy

This short review provides a concise summary of the current status of research aimed at understanding the structure and function of purple bacterial antenna complexes. These structural studies provide the framework for a detailed understanding of how these bacteria harvest solar energy to power their photosynthetic growt

The structure of purple bacterial antenna complexes: From single molecules to native membranes

The photosynthetic unit of purple photosynthetic bacteria typically contains two types of light-harvesting complexes, called LH1 and LH2. These antenna complexes are constructed on a modular principle. They are circular or elliptical oligomers of dimers of two low-molecular weight, hydrophobic apoproteins, called a and b, that bind bacteriochlorophylls and carotenoids non-covalently. The LH1 complex surrounds the reaction centre and, depending on the species, is either a monomer or a dimer. The LH2 complexes are arranged around the LH1-RC complexes. This plenary lecture will present the current status of structural studies on these pigment-protein complexes, based upon a combination of X-ray crystallography and single molecule spectroscopy. Then an overall view of how they are arranged in their native photosynthetic membranes will be presented