Abstract

Phycobilisomes (PBSs) are photosynthetic antenna megacomplexes comprising pigment-binding proteins (cores and rods) joined with linker proteins. A rod-type PBS that does not have a core is connected to photosystem I (PSI) by a CpcL linker protein, which stabilizes a red-form of the phycocyanobilin (red-PCB) in the rod. However, quantitative information on the energy transfer from red-type PBS to PSI has not been determined. Herein, the isolated supercomplex of the rod-type PBS and the PSI tetramer from Anabaena sp. PCC 7120 were probed by time-resolved spectroscopy at 77 K and by decay-associated spectral analysis to show that red-PCB mediates the fast and efficient (time constant = 90 ps, efficiency = 95%) transfer of excitation energy from PCB to chlorophyll a (Chl a). According to the Förster energy transfer mechanism, this high efficiency corresponds to a 4 nm distance between red-PCB and Chl a, suggesting that β-84 PCB in the rod acts as red-PCB.

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