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Updated: Nov 19, 2025

Purification of Active Photosystem I-Light Harvesting Complex I from Plant Tissues
Published on: February 3, 2023
Structures of Rhodopseudomonas palustris RC-LH1 complexes with open or closed quinone channels
David J K Swainsbury1, Pu Qian2,3, Philip J Jackson2,4
1Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, UK. d.swainsbury@sheffield.ac.uk c.n.hunter@sheffield.ac.uk.
Abstract:
The reaction-center light-harvesting complex 1 (RC-LH1) is the core photosynthetic component in purple phototrophic bacteria. We present two cryo-electron microscopy structures of RC-LH1 complexes from Rhodopseudomonas palustris A 2.65-Å resolution structure of the RC-LH114-W complex consists of an open 14-subunit LH1 ring surrounding the RC interrupted by protein-W, whereas the complex without protein-W at 2.80-Å resolution comprises an RC completely encircled by a closed, 16-subunit LH1 ring. Comparison of these structures provides insights into quinone dynamics within RC-LH1 complexes, including a previously unidentified conformational change upon quinone binding at the RC QB site, and the locations of accessory quinone binding sites that aid their delivery to the RC. The structurally unique protein-W prevents LH1 ring closure, creating a channel for accelerated quinone/quinol exchange.
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