The photosynthetic process has the unique ability to capture energy from sunlight and accumulate that energy in sugars and starch. This thesis deals with the light driven part of photosynthesis. The aim has been to investigate how the light-absorbing protein complexes Photosystem I (PS I) and Photosystem II (PS II), react upon illumination of light with lower energy (far-red light; 700-850 nm) than the absorption peak at respective primary donor, P700 and P680.  The results were unexpected. At 295 K, we showed that both PS I and PS II were able to perform photochemistry with light up to 130 nm above its respective primary donor absorption maxima. As such, it was found that the primary donors’ action spectra extended approximately 80 nm further out into the red-region of the spectrum than previously reported.  The ability to perform photochemistry with far-red light was conserved at cryogenic temperatures (< 77 K) in both photosystems. By performing EPR measurements on various photosystem preparations, under different illumination conditions the origin of the effect was localized to their respective reaction center. It is also likely that underlying mechanism is analogous for PS I and PS II, given the similarities in spatial coordination of the reaction center pigments. For PS II, the results obtained allowed us to suggest a model involving a previously unknown electron transfer pathway. This model is based upon the conclusion that the primary cation from primary charge separation induced by far-red light resides primarily on ChlD1 in P680. This is in contrast to the cation being located on PD1, as has been suggested as for visible light illumination. The property to drive photochemistry with far-red wavelengths implies a hither to unknown absorption band, probably originating from the pigments that compose P700 and P680. The results presented here might clarify how the pigments inside P680 are coupled and also how the complex charge separation processes within the first picoseconds that initiate photosynthetic reactions occur.

京都大学 / 新制・課程博士 / 博士(生命科学) / 甲第24982号 / 生博第511号 / 新制||生||68(附属図書館) / 京都大学大学院生命科学研究科統合生命科学専攻 / (主査)教授 河内 孝之, 教授 荒木 崇, 教授 中野 雄司 / 学位規則第4条第1項該当 / Doctor of Philosophy in Life Sciences / Kyoto University / DFAM