Stimuli‐Induced Subconformation Transformation of the PSI‐LHCI Protein at Single‐Molecule Resolution
Abstract Photosynthesis is a very important process for the current biosphere which can maintain such a subtle and stable circulatory ecosystem on earth through the transformation of energy and substance. Even though been widely studied in various aspects, the physiological activities, such as intri...
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| Format: | Article |
| Language: | English |
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Wiley
2023-07-01
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| Series: | Advanced Science |
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| Online Access: | https://doi.org/10.1002/advs.202205945 |
| _version_ | 1827907068207562752 |
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| author | Zhiheng Yang Jie Wang Bing Yin Wenzhe Liu Dongbao Yin Jianren Shen Wenda Wang Lidong Li Xuefeng Guo |
| author_facet | Zhiheng Yang Jie Wang Bing Yin Wenzhe Liu Dongbao Yin Jianren Shen Wenda Wang Lidong Li Xuefeng Guo |
| author_sort | Zhiheng Yang |
| collection | DOAJ |
| description | Abstract Photosynthesis is a very important process for the current biosphere which can maintain such a subtle and stable circulatory ecosystem on earth through the transformation of energy and substance. Even though been widely studied in various aspects, the physiological activities, such as intrinsic structural vibration and self‐regulation process to stress of photosynthetic proteins, are still not in‐depth resolved in real‐time. Herein, utilizing silicon nanowire biosensors with ultrasensitive temporal and spatial resolution, real‐time responses of a single photosystem I‐light harvesting complex I (PSI‐LHCI) supercomplex of Pisum sativum to various conditions, including gradient variations in temperature, illumination, and electric field, are recorded. Under different temperatures, there is a bi‐state switch process associated with the intrinsic thermal vibration behavior. When the variations of illumination and the bias voltage are applied, two additional shoulder states, probably derived from the self‐conformational adjustment, are observed. Based on real‐time monitoring of the dynamic processes of the PSI‐LHCI supercomplex under various conditions, it is successively testified to promising nanotechnology for protein profiling and biological functional integration in photosynthesis studies. |
| first_indexed | 2024-03-13T01:04:47Z |
| format | Article |
| id | doaj.art-56330847d7924d0288351315f6817c05 |
| institution | Directory Open Access Journal |
| issn | 2198-3844 |
| language | English |
| last_indexed | 2024-03-13T01:04:47Z |
| publishDate | 2023-07-01 |
| publisher | Wiley |
| record_format | Article |
| series | Advanced Science |
| spelling | doaj.art-56330847d7924d0288351315f6817c052023-07-06T07:39:03ZengWileyAdvanced Science2198-38442023-07-011019n/an/a10.1002/advs.202205945Stimuli‐Induced Subconformation Transformation of the PSI‐LHCI Protein at Single‐Molecule ResolutionZhiheng Yang0Jie Wang1Bing Yin2Wenzhe Liu3Dongbao Yin4Jianren Shen5Wenda Wang6Lidong Li7Xuefeng Guo8State Key Laboratory for Advanced Metals and Materials School of Materials Science and Engineering University of Science and Technology Beijing Beijing 100083 P. R. ChinaPhotosynthesis Research Center Key Laboratory of Photobiology Institute of Botany Chinese Academy of Sciences Beijing 100093 P. R. ChinaBeijing National Laboratory for Molecular Sciences National Biomedical Imaging Center College of Chemistry and Molecular Engineering Peking University 292 Chengfu Road, Haidian District Beijing 100871 P. R. ChinaBeijing National Laboratory for Molecular Sciences National Biomedical Imaging Center College of Chemistry and Molecular Engineering Peking University 292 Chengfu Road, Haidian District Beijing 100871 P. R. ChinaBeijing National Laboratory for Molecular Sciences National Biomedical Imaging Center College of Chemistry and Molecular Engineering Peking University 292 Chengfu Road, Haidian District Beijing 100871 P. R. ChinaPhotosynthesis Research Center Key Laboratory of Photobiology Institute of Botany Chinese Academy of Sciences Beijing 100093 P. R. ChinaPhotosynthesis Research Center Key Laboratory of Photobiology Institute of Botany Chinese Academy of Sciences Beijing 100093 P. R. ChinaState Key Laboratory for Advanced Metals and Materials School of Materials Science and Engineering University of Science and Technology Beijing Beijing 100083 P. R. ChinaBeijing National Laboratory for Molecular Sciences National Biomedical Imaging Center College of Chemistry and Molecular Engineering Peking University 292 Chengfu Road, Haidian District Beijing 100871 P. R. ChinaAbstract Photosynthesis is a very important process for the current biosphere which can maintain such a subtle and stable circulatory ecosystem on earth through the transformation of energy and substance. Even though been widely studied in various aspects, the physiological activities, such as intrinsic structural vibration and self‐regulation process to stress of photosynthetic proteins, are still not in‐depth resolved in real‐time. Herein, utilizing silicon nanowire biosensors with ultrasensitive temporal and spatial resolution, real‐time responses of a single photosystem I‐light harvesting complex I (PSI‐LHCI) supercomplex of Pisum sativum to various conditions, including gradient variations in temperature, illumination, and electric field, are recorded. Under different temperatures, there is a bi‐state switch process associated with the intrinsic thermal vibration behavior. When the variations of illumination and the bias voltage are applied, two additional shoulder states, probably derived from the self‐conformational adjustment, are observed. Based on real‐time monitoring of the dynamic processes of the PSI‐LHCI supercomplex under various conditions, it is successively testified to promising nanotechnology for protein profiling and biological functional integration in photosynthesis studies.https://doi.org/10.1002/advs.202205945electric fieldphotosynthesisphotosystem I‐light harvesting complex I proteinsilicon nanowire biosensorssingle‐molecule level |
| spellingShingle | Zhiheng Yang Jie Wang Bing Yin Wenzhe Liu Dongbao Yin Jianren Shen Wenda Wang Lidong Li Xuefeng Guo Stimuli‐Induced Subconformation Transformation of the PSI‐LHCI Protein at Single‐Molecule Resolution Advanced Science electric field photosynthesis photosystem I‐light harvesting complex I protein silicon nanowire biosensors single‐molecule level |
| title | Stimuli‐Induced Subconformation Transformation of the PSI‐LHCI Protein at Single‐Molecule Resolution |
| title_full | Stimuli‐Induced Subconformation Transformation of the PSI‐LHCI Protein at Single‐Molecule Resolution |
| title_fullStr | Stimuli‐Induced Subconformation Transformation of the PSI‐LHCI Protein at Single‐Molecule Resolution |
| title_full_unstemmed | Stimuli‐Induced Subconformation Transformation of the PSI‐LHCI Protein at Single‐Molecule Resolution |
| title_short | Stimuli‐Induced Subconformation Transformation of the PSI‐LHCI Protein at Single‐Molecule Resolution |
| title_sort | stimuli induced subconformation transformation of the psi lhci protein at single molecule resolution |
| topic | electric field photosynthesis photosystem I‐light harvesting complex I protein silicon nanowire biosensors single‐molecule level |
| url | https://doi.org/10.1002/advs.202205945 |
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