English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Photosynthesis, the process by which energy from sunlight drives cellularmetabolism, relies on a unique organization of light-harvesting and reactioncenter complexes. Recently, the organization of light-harvesting LH2 complexesand dimeric reaction center-light harvesting I-PufX (RC-LH1-PufX) corecomplexes in membranes of purple non-sulfur bacteria was revealed by atomicforce microscopy (AFM)1. Here, we report that the structure of LH2 and itsorganization within the membrane can be largely rationalized by a simplephysical model that relies primarily on exciton transfer optimization. Theprocess through which the light-harvesting complexes transfer excitation energyhas been recognized to incorporate both coherent and incoherent processesmediated by the surrounding protein environment. Using the Haken-Strobl model,we show that the organization of the complexes in the membrane can be almostentirely explained by simple electrostatic considerations and that quantumeffects act primarily to enforce robustness with respect to spatial disorderbetween complexes. The implications of such an arrangement are discussed in thecontext of biomimetic photosynthetic analogs capable of transferring energyefficiently across tens to hundreds of nanometers

Organization of the Bacterial Light-Harvesting Apparatus Rationalized by Exciton Transport Optimization