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Excitation energy-transfer processes in pigment-protein complexes in photosynthetic organisms are often changed under different pH conditions. However, it is unclear how the pH changes affect excitation energy relaxations in photosystem I (PSI) cores. In this study, we examined the pH sensitivity of energy dynamics in the PSI tetramer, dimer, and monomer isolated from a cyanobacterium, Anabaena sp. PCC 7120, by means of time-resolved fluorescence spectroscopy. Each PSI was adapted to pH 5.0, 6.5, and 8.0. Fluorescence decay-associated (
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