Origin of the Two Bands in the B800 Ring and Their Involvement in the Energy Transfer Network of <i>Allochromatium vinosum</i>

Bacterial photosynthesis features robust and adaptable energy-harvesting processes in which light-harvesting proteins play a crucial role. The peripheral light-harvesting complex of the purple bacterium <i>Allochromatium vinosum</i> is particularly distinct, featuring a double peak structure in its B800 absorption band. Two hypothesesnot necessarily mutually exclusiveconcerning the origin of this splitting have been proposed; either two distinct B800 bacteriochlorophyll site energies are involved, or an excitonic dimerization of bacteriochlorophylls within the B800 ring takes place. Through the use of two-dimensional electronic spectroscopy, we present unambiguous evidence that excitonic interaction shapes the split band. We further identify and characterize all of the energy transfer pathways within this complex by using a global kinetic fitting procedure. Our approach demonstrates how the combination of two-dimensional spectral resolution and self-consistent fitting allows for extraction of information on light-harvesting processes, which would otherwise be inaccessible due to signal congestion