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Convenient Preparation and Energy Transfer Kinetic Process Verification by Ultrafast Time-resolved Fluorescence Spectra for Natural Cryptophyte Phycocyanin 645.

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Title: Convenient Preparation and Energy Transfer Kinetic Process Verification by Ultrafast Time-resolved Fluorescence Spectra for Natural Cryptophyte Phycocyanin 645.
Authors: Pu, Yang1 (AUTHOR), Liu, Chuanxu1 (AUTHOR), Lan, Xiangyu1 (AUTHOR), Xiao, Chao2 (AUTHOR), Xie, Mingyuan3 (AUTHOR) xiemy5@mail.sysu.edu.cn, Li, Wenjun4 (AUTHOR) wjli@yic.ac.cn, Chen, Min5 (AUTHOR) chenmclm@163.com
Source: Journal of Fluorescence. Mar2026, Vol. 36 Issue 3, p2535-2546. 12p.
Subjects: Energy transfer, Time-resolved spectroscopy, Protein fractionation, Photosynthesis, Fluorescence spectroscopy, Phycocyanin, Chromatographic analysis
Abstract: As a remarkable model protein for studying excitation energy transfer (EET), Cryptophyte phycocyanin 645 (Cr-PC645) is not only important in the frontier research field on photosynthesis but also, like other kinds of phycocyanin, valuable in food and cosmetic industries as a kind of natural blue pigment protein. Here, we report a convenient preparation method for the purification of Cr-PC645 from cryptophytic algae, Chroomonas placoidea, mainly using hydrophobic interaction chromatography, and a study of EET characterization based on it. The final recovery of Cr-PC645 is 58.49% and the highest purity of final samples reaches 7.27 (A645/A280) in the obtained products. In addition to high purity, the properties of unchanged intact optical activity of purified Cr-PC645 are proved by comprehensively analyzing absorption, fluorescence, circular dichroism, and ultrafast time-resolved spectra. Furthermore, three time components of 6, 59, and 1021 ps are confirmed by 77 K time-resolved fluorescence spectroscopy experiments, which can be assigned to the time of energy transfer process between specific phycocyanobilins (PCBs), suggesting that the excitation energy is transferred from PCB-158 to PCB-82 in the same β subunit and localized the PCB-82 chromophores between different β subunits, then transferred to the downstream acceptors. In view of all these results, this optimized method is efficient and will be conducive to multi-field applications in the future. [ABSTRACT FROM AUTHOR]
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Database: Engineering Source
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Abstract:As a remarkable model protein for studying excitation energy transfer (EET), Cryptophyte phycocyanin 645 (Cr-PC645) is not only important in the frontier research field on photosynthesis but also, like other kinds of phycocyanin, valuable in food and cosmetic industries as a kind of natural blue pigment protein. Here, we report a convenient preparation method for the purification of Cr-PC645 from cryptophytic algae, Chroomonas placoidea, mainly using hydrophobic interaction chromatography, and a study of EET characterization based on it. The final recovery of Cr-PC645 is 58.49% and the highest purity of final samples reaches 7.27 (A645/A280) in the obtained products. In addition to high purity, the properties of unchanged intact optical activity of purified Cr-PC645 are proved by comprehensively analyzing absorption, fluorescence, circular dichroism, and ultrafast time-resolved spectra. Furthermore, three time components of 6, 59, and 1021 ps are confirmed by 77 K time-resolved fluorescence spectroscopy experiments, which can be assigned to the time of energy transfer process between specific phycocyanobilins (PCBs), suggesting that the excitation energy is transferred from PCB-158 to PCB-82 in the same β subunit and localized the PCB-82 chromophores between different β subunits, then transferred to the downstream acceptors. In view of all these results, this optimized method is efficient and will be conducive to multi-field applications in the future. [ABSTRACT FROM AUTHOR]
ISSN:10530509
DOI:10.1007/s10895-025-04663-7