Structures of <i>Rhodopseudomonas palustris</i> RC-LH1 complexes with open or closed quinone channels
David J. K. Swainsbury, Qian Pu, Philip J. Jackson, Kaitlyn M. Faries, Dariusz M. Niedzwiedzki, Elizabeth C. Martin, David A. Farmer, Lorna Malone, Rebecca F. Thompson, Neil A. Ranson, Daniel P. Canniffe, Mark J. Dickman, Dewey Holten, Christine Kirmaier, Andrew Hitchcock, C. Neil Hunter
Abstract
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.
Topics & Concepts
Rhodopseudomonas palustrisQuinonePhotosynthetic reaction centreRhodopseudomonasChemistryStereochemistryBiologyPhotosynthesisBiochemistryBacteriaGeneticsPhotosynthetic Processes and MechanismsPorphyrin and Phthalocyanine ChemistryMetalloenzymes and iron-sulfur proteins