Anti-Stokes fluorescence excitation reveals conformational mobility of the C-phycocyanin chromophores
The structural organization of natural pigment-protein complexes provides a specific environment for the chromophore groups. Yet, proteins are inherently dynamic and conformationally mobile. In this work, we demonstrate the heterogeneity of chromophores of C-phycocyanin (C-PC) from Arthrospira plate...
| Main Authors: | , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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AIP Publishing LLC and ACA
2022-09-01
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| Series: | Structural Dynamics |
| Online Access: | http://dx.doi.org/10.1063/4.0000164 |
| _version_ | 1828135525336219648 |
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| author | Georgy V. Tsoraev Elena A. Protasova Elizaveta A. Klimanova Yury L. Ryzhykau Alexander I. Kuklin Yury S. Semenov Baosheng Ge Wenjun Li Song Qin Thomas Friedrich Nikolai N. Sluchanko Eugene G. Maksimov |
| author_facet | Georgy V. Tsoraev Elena A. Protasova Elizaveta A. Klimanova Yury L. Ryzhykau Alexander I. Kuklin Yury S. Semenov Baosheng Ge Wenjun Li Song Qin Thomas Friedrich Nikolai N. Sluchanko Eugene G. Maksimov |
| author_sort | Georgy V. Tsoraev |
| collection | DOAJ |
| description | The structural organization of natural pigment-protein complexes provides a specific environment for the chromophore groups. Yet, proteins are inherently dynamic and conformationally mobile. In this work, we demonstrate the heterogeneity of chromophores of C-phycocyanin (C-PC) from Arthrospira platensis. Part of the population of trimeric C-PC is subject to spontaneous disturbances of protein–protein interactions resulting in increased conformational mobility of the chromophores. Upon fluorescence excitation in the visible range, the spectral signatures of these poorly populated states are masked by bulk chromophore states, but the former could be clearly discriminated when the fluorescence is excited by near-infrared quanta. Such selective excitation of conformationally mobile C-PC chromophores is due to the structure of their S1 level, which is characterized by a significantly broadened spectral line. We demonstrate that the anti-Stokes C-PC fluorescence is the result of single-photon absorption. By combining spectral and structural methods, we characterize four distinct states of C-PC chromophores emitting at 620, 650, 665, and 720 nm and assigned the fast component in the anti-Stokes fluorescence decay kinetics in the range of 690–750 nm to the chromophores with increased conformational mobility. Our data suggest that the spectral and temporal characteristics of the anti-Stokes fluorescence can be used to study protein dynamics and develop methods to visualize local environment parameters such as temperature. |
| first_indexed | 2024-04-11T17:48:02Z |
| format | Article |
| id | doaj.art-c6fb86fbc9064e07bac4c672910d7588 |
| institution | Directory Open Access Journal |
| issn | 2329-7778 |
| language | English |
| last_indexed | 2024-04-11T17:48:02Z |
| publishDate | 2022-09-01 |
| publisher | AIP Publishing LLC and ACA |
| record_format | Article |
| series | Structural Dynamics |
| spelling | doaj.art-c6fb86fbc9064e07bac4c672910d75882022-12-22T04:11:14ZengAIP Publishing LLC and ACAStructural Dynamics2329-77782022-09-0195054701054701-1110.1063/4.0000164Anti-Stokes fluorescence excitation reveals conformational mobility of the C-phycocyanin chromophoresGeorgy V. Tsoraev0Elena A. Protasova1Elizaveta A. Klimanova2Yury L. Ryzhykau3Alexander I. Kuklin4Yury S. Semenov5Baosheng Ge6Wenjun Li7Song Qin8Thomas Friedrich9Nikolai N. Sluchanko10Eugene G. Maksimov11 Faculty of Biology, Lomonosov Moscow State University, Moscow 119991, Russia Faculty of Biology, Lomonosov Moscow State University, Moscow 119991, Russia Faculty of Biology, Lomonosov Moscow State University, Moscow 119991, Russia Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia China University of Petroleum (Huadong), College of Chemical Engineering, Qingdao 266580, People's Republic of China Yantai Institute of Coastal Zone Research, Chinese Academy of Sciences, Yantai 264003, People's Republic of China China University of Petroleum (Huadong), College of Chemical Engineering, Qingdao 266580, People's Republic of China Technical University of Berlin, Institute of Chemistry PC 14, D-10623 Berlin, Germany A.N. Bach Institute of Biochemistry, Federal Research Center of Biotechnology of the Russian Academy of Sciences, Moscow 119071, Russia Faculty of Biology, Lomonosov Moscow State University, Moscow 119991, RussiaThe structural organization of natural pigment-protein complexes provides a specific environment for the chromophore groups. Yet, proteins are inherently dynamic and conformationally mobile. In this work, we demonstrate the heterogeneity of chromophores of C-phycocyanin (C-PC) from Arthrospira platensis. Part of the population of trimeric C-PC is subject to spontaneous disturbances of protein–protein interactions resulting in increased conformational mobility of the chromophores. Upon fluorescence excitation in the visible range, the spectral signatures of these poorly populated states are masked by bulk chromophore states, but the former could be clearly discriminated when the fluorescence is excited by near-infrared quanta. Such selective excitation of conformationally mobile C-PC chromophores is due to the structure of their S1 level, which is characterized by a significantly broadened spectral line. We demonstrate that the anti-Stokes C-PC fluorescence is the result of single-photon absorption. By combining spectral and structural methods, we characterize four distinct states of C-PC chromophores emitting at 620, 650, 665, and 720 nm and assigned the fast component in the anti-Stokes fluorescence decay kinetics in the range of 690–750 nm to the chromophores with increased conformational mobility. Our data suggest that the spectral and temporal characteristics of the anti-Stokes fluorescence can be used to study protein dynamics and develop methods to visualize local environment parameters such as temperature.http://dx.doi.org/10.1063/4.0000164 |
| spellingShingle | Georgy V. Tsoraev Elena A. Protasova Elizaveta A. Klimanova Yury L. Ryzhykau Alexander I. Kuklin Yury S. Semenov Baosheng Ge Wenjun Li Song Qin Thomas Friedrich Nikolai N. Sluchanko Eugene G. Maksimov Anti-Stokes fluorescence excitation reveals conformational mobility of the C-phycocyanin chromophores Structural Dynamics |
| title | Anti-Stokes fluorescence excitation reveals conformational mobility of the C-phycocyanin chromophores |
| title_full | Anti-Stokes fluorescence excitation reveals conformational mobility of the C-phycocyanin chromophores |
| title_fullStr | Anti-Stokes fluorescence excitation reveals conformational mobility of the C-phycocyanin chromophores |
| title_full_unstemmed | Anti-Stokes fluorescence excitation reveals conformational mobility of the C-phycocyanin chromophores |
| title_short | Anti-Stokes fluorescence excitation reveals conformational mobility of the C-phycocyanin chromophores |
| title_sort | anti stokes fluorescence excitation reveals conformational mobility of the c phycocyanin chromophores |
| url | http://dx.doi.org/10.1063/4.0000164 |
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