TY - JOUR
T1 - Regulation of excitation energy transfer in diatom PSII dimer
T2 - How does it change the destination of excitation energy?
AU - Yokono, Makio
AU - Nagao, Ryo
AU - Tomo, Tatsuya
AU - Akimoto, Seiji
N1 - Funding Information:
This work was partly supported by Grants-in-aid for Scientific Research from the Ministry of Education of Japan ( 24370025 and 26220801 to T.T.).
Publisher Copyright:
© 2015 Elsevier B.V.
PY - 2015/7/25
Y1 - 2015/7/25
N2 - Abstract Energy transfer dynamics in dimeric photosystem II (PSII) complexes isolated from four diatoms, Chaetoceros gracilis, Cyclotella meneghiniana, Thalassiosira pseudonana, and Phaeodactylum tricornutum, are examined. Time-resolved fluorescence measurements were conducted in the range of 0-80 ns. Delayed fluorescence spectra showed a clear difference between PSII monomer and PSII dimer isolated from the four diatoms. The difference can be interpreted as reflecting suppressed energy transfer between PSII monomers in the PSII dimer for efficient energy trapping at the reaction center. The observation was especially prominent in C. gracilis and T. pseudonana. The pathways seem to be suppressed under a low pH condition in isolated PSII complexes from C. gracilis, and excitation energy may be quenched with fucoxanthin chlorophyll a/c-binding protein (FCP) that was closely associated with PSII in C. gracilis. The energy transfer between PSII monomers in the PSII dimer may play a role in excitation energy regulation in diatoms.
AB - Abstract Energy transfer dynamics in dimeric photosystem II (PSII) complexes isolated from four diatoms, Chaetoceros gracilis, Cyclotella meneghiniana, Thalassiosira pseudonana, and Phaeodactylum tricornutum, are examined. Time-resolved fluorescence measurements were conducted in the range of 0-80 ns. Delayed fluorescence spectra showed a clear difference between PSII monomer and PSII dimer isolated from the four diatoms. The difference can be interpreted as reflecting suppressed energy transfer between PSII monomers in the PSII dimer for efficient energy trapping at the reaction center. The observation was especially prominent in C. gracilis and T. pseudonana. The pathways seem to be suppressed under a low pH condition in isolated PSII complexes from C. gracilis, and excitation energy may be quenched with fucoxanthin chlorophyll a/c-binding protein (FCP) that was closely associated with PSII in C. gracilis. The energy transfer between PSII monomers in the PSII dimer may play a role in excitation energy regulation in diatoms.
KW - Abbreviations PSI photosystem I
KW - Chl chlorophyll
KW - FCP fucoxanthin chlorophyll a/c-binding protein
KW - FDAS fluorescence decay-associated spectrum
KW - PSII photosystem II
KW - RC reaction center
KW - TRFS time-resolved fluorescence spectra
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U2 - 10.1016/j.bbabio.2015.07.006
DO - 10.1016/j.bbabio.2015.07.006
M3 - Article
AN - SCOPUS:84937835629
VL - 1847
SP - 1274
EP - 1282
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
SN - 0005-2728
IS - 10
M1 - 47503
ER -