Excitation-energy transfer in photosystem I (PSI) is changed by a cation formation of a special pair chlorophyll P700 in the PSI core; however, it remains unclear how light-harvesting pigment-protein complexes are involved in the P700-related energy-transfer mechanisms. Here, we report effects of the redox changes of P700 on excitation-energy dynamics in diatom PSI-fucoxanthin chlorophyll a/c-binding protein (PSI-FCPI) and PSI core complexes by means of time-resolved fluorescence (TRF) spectroscopy. For the TRF measurements, the PSI-FCPI and PSI were adapted under P700 neutral and cation conditions using chemical reagents. Upon the P700(+) formation, fluorescence decay-associated (FDA) spectra constructed from the TRF spectra exhibit a larger fluorescence decay amplitude relative to a fluorescence rise magnitude within 100 ps in each of the PSI-FCPI and PSI. The decay components are shifted to lower wavelengths in each of the P700-cation PSI-FCPI and PSI than in the P700-neutral PSIs. The rapid fluorescence decays upon the P700(+) formation are clearly verified by mean lifetimes reconstructed from the FDA spectra. Because the P700-cation PSI does not cause charge-separation reactions, the relatively strong decay components and rapid fluorescence decays observed are likely attributed to excitation-energy quenching. These observations suggest that chlorophylls in PSI and around/within FCPI are involved in the energy-quenching events by the redox changes of P700.