Origin of Energy Dissipation in the Oligomeric Fucoxanthin-Chlorophyll a/c Binding Proteins.

Fucoxanthin-chlorophyll proteins (FCPs) are a family of photosynthetic light-harvesting complex (LHC) proteins found in diatoms. They efficiently capture photons and regulate their functions, ensuring diatom survival in highly fluctuating light. FCPs are present in different oligomeric states , but functional differences among these FCP oligomers are not yet fully understood. Here we characterized two types of antenna complexes (FCP-B/C dimers and FCP-A tetramers) that coexist in the marine centric diatom using both time-resolved fluorescence and transient absorption spectroscopy. We found that the FCP-B/C complex did not show fluorescence quenching, whereas FCP-A was severely quenched, via an ultrafast excitation energy transfer (EET) pathway from Chl a Q to the fucoxanthin S/ICT state. These results highlight the functional differences between FCP dimers and tetramers and indicate that the EET pathway from Chl a to carotenoids is an energy dissipation mechanism conserved in a variety of photosynthetic organisms.