Maksimov, EG; Li WJ(李文军)
; Protasova, EA; Friedrich, T; Ge, B; Qin, S; Sluchanko, NN发表期刊Biochemical and Biophysical Research Communications
ISSN0006-291X
2019
卷号516期号:3页码:699-704
关键词Orange Carotenoid ProteinPhycobilisomePhycobiliproteinsFluorescencePhotoprotectionNon-photochemical Quenching
研究领域Biochemistry & Molecular Biology; Biophysics
DOI10.1016/j.bbrc.2019.06.098
通讯作者Maksimov, Eugene G.(emaksimoff@yandex.ru); Qin, Song(sqin@yic.ac.cn)
作者部门海岸带生物学与生物资源保护实验室
英文摘要To regulate the effectiveness of photosynthesis and photoprotection cyanobacteria utilize a system
consisting of only few components. Photoactivation of the orange carotenoid protein (OCP) enables its
interaction with a specific, yet controversial site in the core of the light-harvesting antenna, the phycobilisome
(PBS). The resulting delivery of a quenching carotenoid molecule to the antenna pigments
leads to thermal dissipation of the excitation energy absorbed by the latter, and, consequently, to
depression of the photosynthetic activity. The nature of the OCP-induced PBS fluorescence quenching
mechanism remains debatable, however, specific protein-protein interactions between PBS and photoactivated
OCP should provide a unique environment for interactions between the excitation energy
donor and acceptor. Here we questioned whether the F�orster theory of resonance energy transfer can
explain PBS quenching by OCP even at their very small spectral overlap and whether in model systems,
the absence of specific protein-protein interactions of OCP with a donor of energy can be compensated by
a better spectral overlap. Hybridization of algal R-phycoerythrin with cyanobacterial OCP by chemical
crosslinking results in a significant decrease of R-phycoerythrin fluorescence lifetime, irrespective of the
OCP photoactivation status. Supported by structural considerations, this indicates that FRET may be the
essence of cyanobacterial photoprotection mechanism.
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文章类型Article
资助机构Russian Foundation for Basic Research; Russian Ministry of Science; Program of the Ministry of Science and Higher Education of Russia; National Natural Science Foundation of China
收录类别SCI
语种英语
关键词[WOS]Photosystem-i; Phycobilisome; Fluorescence; Features
研究领域[WOS]Biochemistry & Molecular Biology; Biophysics
WOS记录号WOS:000477917500016
引用统计被引频次：4[WOS][WOS记录][WOS相关记录]
文献类型期刊论文
条目标识符http://ir.yic.ac.cnhttp://ir.yic.ac.cn/handle/133337/25249
专题海岸带生物学与生物资源利用重点实验室_海岸带生物学与生物资源保护实验室
通讯作者Maksimov, EG; Qin, S作者单位1.Lomonosov Moscow State Univ, Dept Biophys, Fac Biol, Moscow 119991, Russia
2.Russian Acad Sci, Fed Res Ctr Biotechnol, AN Bach Inst Biochem, Moscow 119071, Russia
3.Chinese Acad Sci, Yantai Inst Coastal Zone Res, Chunhui Rd 17, Laishan Dist, Yantai, Peoples R China
4.Tech Univ Berlin, Inst Chem PC 14, Str 17 Juni 135, D-10623 Berlin, Germany
5.China Univ Petr Huadong, Qingdao, Shandong, Peoples R China
推荐引用方式
GB/T 7714Maksimov, EG,Li WJ,Protasova, EA,et al. Hybrid coupling of R-phycoerythrin and the orange carotenoid protein supports the FRET-based mechanism of cyanobacterial photoprotection[J]. Biochemical and Biophysical Research Communications,2019,516(3):699-704.
APAMaksimov, EG.,Li WJ.,Protasova, EA.,Friedrich, T.,Ge, B.,...&Sluchanko, NN.(2019).Hybrid coupling of R-phycoerythrin and the orange carotenoid protein supports the FRET-based mechanism of cyanobacterial photoprotection.Biochemical and Biophysical Research Communications,516(3),699-704.
MLAMaksimov, EG,et al."Hybrid coupling of R-phycoerythrin and the orange carotenoid protein supports the FRET-based mechanism of cyanobacterial photoprotection".Biochemical and Biophysical Research Communications 516.3(2019):699-704.
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