Abstract
The fluorescence profile of Photosystem I/Photosystem II mixtures in different solvent systems shows that both non-hydrophobic and hydrophobic interactions govern their association and control energy transfer from Photosystem II to Photosystem I. The non-hydrophobic interactions lead to a highly efficient excitation energy transfer from Photosystem II to Photosystem I. In view of this, we propose that similar non-hydrophobic interactions, between the Photosystem II and Photosystem I peripheral proteins, also play a significant role in their association in thylakoids that control state transitions in cyanobacteria.
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