부산대학교 도서관

Marine diatoms contribute to oxygenic photosynthesis and carbon fixation and handle large changes under variable light intensity on a regular basis. The unique light-harvesting apparatus of diatoms are the fucoxanthin-chlorophyll a / c -binding proteins (FCPs). Here, we show the enhancement of chlorophyll a / c (Chl a / c ), fucoxanthin (Fx), and diadinoxanthin (Dd) marker bands in the Raman spectra of the centric diatom T. pseudonana , which allows distinction of the pigment content in the cells grown under low- (LL) and high-light (HL) intensity at room temperature. Reversible LL-HL dependent conformations of Chl c , characteristic of two conformations of the porphyrin macrocycle, and the presence of five- and six-coordinated Chl a / c with weak axial ligands are observed in the Raman data. Under HL the energy transfer from Chl c to Chl a is reduced and that from the red-shifted Fxs is minimal. Therefore, Chl c and the blue-shifted Fxs are the only contributors to the energy transfer pathways under HL and the blue- to red-shifted Fxs energy transfer pathway characteristic of the LL is inactive. The results indicate that T. pseudonana can redirect its function from light harvesting to energy-quenching state, and reversibly to light-harvesting upon subsequent illumination to LL by reproducing the red-shifted Fxs and decrease the number of Dds. The LL to HL reversible transitions are accompanied by structural modifications of Chl a / c and the lack of the red-shifted Fxs.
Competing Interests: There are no conflicts to declare.
(This journal is © The Royal Society of Chemistry.)