期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1777, 期 4, 页码 351-361出版社
ELSEVIER
DOI: 10.1016/j.bbabio.2008.01.011
关键词
Chaetoceros gracilis; diatom; fucoxanthin-chlorophyll-binding protein; photosystem I; time-resolved fluorescence spectra
Diatoms occupy a key position as a primary producer in the global aquatic ecosystem. We developed methods to isolate highly intact thylakoid membranes and the photosystent I (PS I) complex from a marine centric diatom, Chaetoceros gracilis. The PS I reaction center (RC) was purified as a super complex with light-harvesting fucoxanthin-chlorophyll (Chl)-binding proteins (FCP). The super complex contained 224 Chl a, 22 Chl e, and 55 facoxanthin molecules per RC. The apparent molecular mass of the purified FCP-PS I super complex (similar to 1000 kDa) indicated that the super complex was composed of a monomer of the PS I RC complex and about 25 copies of FCP. The complex contained menaquinone-4 as the secondary electron acceptor A(1) instead of phylloquinone. Time-resolved fluorescence emission spectra at 77 K indicated that fast (16 ps) energy transfer from a Chl a band at 685 nm on FCP to Chls on the PS I RC complex occurs. The ratio of fucoxanthin to Chl a on the PS I-bound FCP was lower than that of weakly bound FCP, suggesting that PS I-bound FCP specifically functions as the mediator of energy transfer between weakly bound FCPs and the PS I RC. (C) 2008 Elsevier B.V. All rights reserved.
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