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- W2005506718 abstract "We report ultrafast femtosecond transient absorption measurements of energy-transfer dynamics for the antenna protein phycoerythrin 545, PE545, isolated from a unicellular cryptophyte Rhodomonas CS24. The phycoerythrobilins are excited at both 485 and 530 nm, and the spectral response is probed between 400 and 700 nm. Room-temperature measurements are contrasted with measurements at 77 K. An evolution-associated difference spectra (EADS) analysis is combined with estimations of bilin spectral positions and energy-transfer rates to obtain a detailed kinetic model for PE545. It is found that sub pulse-width dynamics include relaxation between the exciton states of a chromophore dimer (β50/60) located in the core of the protein. Energy transfer from the lowest exciton state of the phycoerythrobilin (PEB) dimer to one of the periphery 15,16-dihydrobiliverdin (DBV) bilins is found to occur on a time scale of 250 fs at room temperature and 960 fs at 77 K. A host of energy-transfer dynamics involving the β158, β82, and α19 bilins occur on a time scale of 2 ps at room temperature and 3 ps at 77 K. A final energy transfer occurs between the red-most DBV bilins with a time scale estimated to be ∼30 ps. The role of the centrally located phycoerythrobilin dimer is seen as crucial−spectrally as it expands the cross-section of absorption of the protein; structurally as it sits in the middle of the protein acting as an intermediary trap; and kinetically, as the internal conversion and subsequent red-shift of the excitation is extremely fast." @default.
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- W2005506718 date "2005-06-29" @default.
- W2005506718 modified "2023-10-11" @default.
- W2005506718 title "Mediation of Ultrafast Light-Harvesting by a Central Dimer in Phycoerythrin 545 Studied by Transient Absorption and Global Analysis" @default.
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- W2005506718 doi "https://doi.org/10.1021/jp051173j" @default.
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