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The Fenna-Matthews-Olson (FMO) protein-pigment complex acts as a molecularwire between the outer antenna system and the reaction center (RC); it is animportant model system to study the excitonic energy transfer. Recentcrystallographic studies report the existence of an additional (eighth)bacteriochlorophyll a (BChl a). To understand the functionality of this eighthBChl, we simulated the two-dimensional electronic spectra of both the 7-site(apo form) and the 8-site (holo form) variant of the FMO complex from greensulfur bacteria, Prosthecochloris aestuarii. By comparing the differencebetween the spectrum, it was found that the eighth BChl can affect twodifferent excitonic energy transfer pathways, these being: (1) directly involvein the first pathway 6 $\rightarrow$ 3 $\rightarrow$ 1 of the apo form model bypassing the excitonic energy to exciton 6; and (2) increase the excitonic wavefunction overlap between excitons 4 and 5 in the second pathway (7$\rightarrow$ 4,5 $\rightarrow$ 2 $\rightarrow$ 1) and thus increase thepossible downward sampling routes across the BChls.

Probing the Role of the Eighth Bacteriochlorophyll in holo-FMO Complex by Simulated Two-Dimensional Electronic Spectroscopy