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Energy transfer dynamics in B-phycoerythrin from the red alga Porphyridium purpureum
Institution:1. Yantai Institute of Coastal Zone Research, Chinese Academy of Sciences, 17 Chunhui Road, Laishan District, Yantai 264003, China;2. School of physics, State Key Laboratory of Optoelectronic Materials and Technologies, Sun Yat-sen University, Guangzhou 510275, China;3. School of Agriculture, Ludong University, Yantai 264025, China;4. College of Life Science, Yantai University, 30 Qingquan Street, Yantai 264005, China;5. School of Information Technology, Beijing Institute of Technology, Zhuhai, Zhuhai, 519088, China;1. Post-Graduate Department of Biosciences, UGC-Centre of Advanced Study, Satellite Campus, Vadtal Road, Sardar Patel University, Bakrol, Anand 388315, Gujarat, India;2. School of Sciences, P. P. Savani University, Dhamdod, Kosamba 394125, Gujarat, India;3. Department of Biotechnology, Shree A. N. Patel PG Institute, Anand 388001, Gujarat, India;1. Molecular Photoscience Research Center, Kobe University, Kobe 657-8501, Japan;2. Graduate School of Science, Kobe University, Kobe 657-8501, Japan;3. CREST, Japan Science and Technology Agency (JST), Kobe 657-8501, Japan;4. Graduate School of Human and Environmental Studies, Kyoto University, Kyoto 606-8501, Japan;5. Division of Material Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan;6. Faculty of Science, Tokyo University of Science, Tokyo 162-8601 Japan;7. PRESTO, Japan Science and Technology Agency (JST), Saitama 332-0012, Japan
Abstract:The B-phycoerythrin hexamer (αβ)6γ of Porphyridium purpureum was isolated and purified. The absorption, circular dichroism, fluorescence and ultrafast time-resolved spectra were obtained. The results showed a double absorption peak at 545 nm and 565 nm and a shoulder peak at 498 nm, and fluorescence emission maxima at 580 nm and 620 nm were observed. The circular dichroism spectra in the near-ultraviolet region were obtained and resolved for the first time, which showed that the two peaks at 260 nm and 305 nm were considered to be correlated to phenylalanine (Phe) and tryptophan (Trp) in a conservative hydrophobic microenvironment, respectively. The circular dichroism spectra in the visible region showed that PEB139α/PEB158β and PEB82α/PEB82β existed as two exciton-coupled bilin pairs. Energy transfer within the exciton-coupled pairs was by exciton splitting, while between the exciton-coupled pairs was by Förster resonance. From the studies of the energy transfer dynamics by ultrafast time-resolved fluorescence spectroscopy, it was confirmed that the energy transfer of the B-PE hexamer had three time components of 8 ps, 60 ps, and 1200 ps. In addition, the internal energy transfer pathways of B-phycoerythrin hexamer were identified by deconvoluting the fluorescence decay curve at different detection wavelengths.
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