TY - JOUR
T1 - Low-Energy Chlorophylls in Fucoxanthin Chlorophyll a/ c-Binding Protein Conduct Excitation Energy Transfer to Photosystem i in Diatoms
AU - Nagao, Ryo
AU - Yokono, Makio
AU - Ueno, Yoshifumi
AU - Shen, Jian Ren
AU - Akimoto, Seiji
N1 - Funding Information:
This work was supported by the Grants-in-Aid for Scientific Research from Japan Society for the Promotion of Science KAKENHI JP17K07442 (to R.N.), JP17H06433 (to J.R.S.), and JP16H06553 (to S.A.).
Publisher Copyright:
© 2018 American Chemical Society.
PY - 2019/10/1
Y1 - 2019/10/1
N2 - Photosynthetic organisms handle solar energy precisely to achieve efficient photochemical reactions. Because there are a wide variety of light-harvesting antennas in oxyphototrophs, the excitation energy transfer mechanisms are thought to differ significantly. In this study, we compared excitation energy dynamics between photosystem I (PSI) cores and a complex between PSI and fucoxanthin chlorophyll (Chl) a/c-binding protein I (PSI-FCPI) isolated from a diatom, Chaetoceros gracilis, by means of picosecond time-resolved fluorescence analyses. Time-resolved spectra measured at 77 K clearly show that low-energy Chls in the FCPI transfer not only most of the excitation energy to the reaction center Chls in the PSI cores but also the remaining energy to carotenoids for quenching. Under room-temperature conditions, the energy in the low-energy Chls is rapidly equilibrated on Chls in the PSI cores by uphill energy transfer within a few tens of picoseconds. These findings provide solid evidence that the low-energy Chls in the FCPI contribute to the photochemical reactions in PSI.
AB - Photosynthetic organisms handle solar energy precisely to achieve efficient photochemical reactions. Because there are a wide variety of light-harvesting antennas in oxyphototrophs, the excitation energy transfer mechanisms are thought to differ significantly. In this study, we compared excitation energy dynamics between photosystem I (PSI) cores and a complex between PSI and fucoxanthin chlorophyll (Chl) a/c-binding protein I (PSI-FCPI) isolated from a diatom, Chaetoceros gracilis, by means of picosecond time-resolved fluorescence analyses. Time-resolved spectra measured at 77 K clearly show that low-energy Chls in the FCPI transfer not only most of the excitation energy to the reaction center Chls in the PSI cores but also the remaining energy to carotenoids for quenching. Under room-temperature conditions, the energy in the low-energy Chls is rapidly equilibrated on Chls in the PSI cores by uphill energy transfer within a few tens of picoseconds. These findings provide solid evidence that the low-energy Chls in the FCPI contribute to the photochemical reactions in PSI.
UR - http://www.scopus.com/inward/record.url?scp=85058836577&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85058836577&partnerID=8YFLogxK
U2 - 10.1021/acs.jpcb.8b09253
DO - 10.1021/acs.jpcb.8b09253
M3 - Article
C2 - 30511857
AN - SCOPUS:85058836577
SN - 1520-6106
VL - 123
SP - 66
EP - 70
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
IS - 1
ER -