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Efficient purification and excitation energy transfer characterization of phycoerythrin 545 from Rhodomonas sp.

文献类型：期刊论文

作者Pu, Yang4; Dong, Shuo3; Wang, Jiayu1,2; Li, Min4; Dong, Kai4; Li, Wenjun5; Tang, Zhihong3
刊名PROTEIN EXPRESSION AND PURIFICATION
出版日期2025-03-01
卷号227页码:8
关键词Cryptomonad Phycoerythrin 545 Purification Hydrophobic interaction chromatography Ultrafast absorption spectroscopy
ISSN号1046-5928
DOI10.1016/j.pep.2024.106634
通讯作者Li, Wenjun(wjli@yic.ac.cn) ; Tang, Zhihong(tangzhh@ytu.edu.cn)
英文摘要Cryptomonad phycoerythrin 545 (PE545) is an important type of phycobiliprotein in basic research and technological innovations. Herein, we report a minimalistic hydrophobic chromatography method for its purification. High purity was achieved, with a purity ratio (A545/A280) of 13.66 and a recovery ratio of 78.63 %. Following SDS-PAGE, Coomassie Brilliant Blue staining revealed three bands at 9 kDa, 10 kDa, and 20 kDa, corresponding to alpha 1, alpha 2 and beta subunits. Multiple spectral characteristics were analyzed to ensure that optical activity was consistent with that of the natural protein. Absorption and fluorescence spectroscopies of purified PE545 displayed a strong absorption peak at 545 nm, a shoulder peak at 564 nm, and a fluorescence emission peak at 587 nm, which confirmed unchanged energy transfer properties. Furthermore, the structural and functional integrity, especially the existence of strongly coupled central chromophore pairs with excitation delocalization, was verified by circular dichroism and ultrafast absorption spectroscopy. From the studies of ultrafast absorption spectroscopy of excitation energy transfer (EET) of PE545, four decay components with lifetimes at 0.5 ps, 2.2 ps, 63 ps, and 3000 ps were obtained. In addition, the dynamics of these components confirmed the EET pathways from the central PEB chromophore pairs to the peripheral pigments and localized in the lowest state. Our work will be of considerable value for both fundamental research and applications of PE545.
WOS关键词LIGHT-HARVESTING PROTEINS ; TRANSIENT ABSORPTION ; DYNAMICS ; STATE
WOS研究方向Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
语种英语
WOS记录号WOS:001372982900001
资助机构National Key Research and Development Program of China ; Natural Science Foundation of Shandong Province ; The 2023 science and technology cooperation between Jilin Province and the Chinese Academy of Sciences for special projects in high technology industrialization ; Yantai City school and land integration development project ; Graduate Innovation Foundation of Yantai University, GIFYTU
源URL[http://ir.yic.ac.cn/handle/133337/38163]  
专题海岸带生物学与生物资源利用重点实验室
烟台海岸带研究所_海岸带生物学与生物资源利用所重点实验室
通讯作者Li, Wenjun; Tang, Zhihong
作者单位1.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
2.Chinese Acad Sci, Lab Soft Matter Phys, Inst Phys, Beijing 100190, Peoples R China
3.Yantai Univ, Coll Life Sci, Yantai 264005, Peoples R China
4.Ludong Univ, Sch Agr, Yantai 264025, Peoples R China
5.Chinese Acad Sci, Yantai Inst Coastal Zone Res, Yantai 264003, Peoples R China
推荐引用方式
GB/T 7714		 Pu, Yang,Dong, Shuo,Wang, Jiayu,et al. Efficient purification and excitation energy transfer characterization of phycoerythrin 545 from Rhodomonas sp.[J]. PROTEIN EXPRESSION AND PURIFICATION,2025,227:8.
APA Pu, Yang.,Dong, Shuo.,Wang, Jiayu.,Li, Min.,Dong, Kai.,...&Tang, Zhihong.(2025).Efficient purification and excitation energy transfer characterization of phycoerythrin 545 from Rhodomonas sp..PROTEIN EXPRESSION AND PURIFICATION,227,8.
MLA Pu, Yang,et al."Efficient purification and excitation energy transfer characterization of phycoerythrin 545 from Rhodomonas sp.".PROTEIN EXPRESSION AND PURIFICATION 227(2025):8.

入库方式： OAI收割

来源：烟台海岸带研究所

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