Harvesting far-red light
| Autor: | Luca Bersanini, Roberta Croce, Martijn Tros, Gaozhong Shen, Donald A. Bryant, Ming Yang Ho, Ivo H. M. van Stokkum |
|---|---|
| Přispěvatelé: | Biophysics Photosynthesis/Energy, LaserLaB - Energy |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0106 biological sciences
0301 basic medicine Photosynthetic reaction centre Chlorophyll Pigments Light Chlorophyll f Biophysics Photosynthesis Photosystem I 01 natural sciences Biochemistry 03 medical and health sciences chemistry.chemical_compound Excitation energy transfer SDG 7 - Affordable and Clean Energy Synechococcus biology Photosystem I Protein Complex Far-red Time-resolved fluorescence Cell Biology biology.organism_classification Light harvesting 030104 developmental biology chemistry Energy Transfer Photosynthetically active radiation 010606 plant biology & botany Protein Binding |
| Zdroj: | Tros, M, Bersanini, L, Shen, G, Ho, M Y, van Stokkum, I H M, Bryant, D A & Croce, R 2020, ' Harvesting far-red light : Functional integration of chlorophyll f into Photosystem I complexes of Synechococcus sp. PCC 7002 ', Biochimica et Biophysica Acta-Bioenergetics, vol. 1861, no. 8, 148206, pp. 1-9 . https://doi.org/10.1016/j.bbabio.2020.148206 Biochimica et Biophysica Acta-Bioenergetics, 1861(8):148206, 1-9. Elsevier |
| ISSN: | 0005-2728 |
| DOI: | 10.1016/j.bbabio.2020.148206 |
| Popis: | The heterologous expression of the far-red absorbing chlorophyll (Chl) f in organisms that do not synthesize this pigment has been suggested as a viable solution to expand the solar spectrum that drives oxygenic photosynthesis. In this study, we investigate the functional binding of Chl f to the Photosystem I (PSI) of the cyanobacterium Synechococcus 7002, which has been engineered to express the Chl f synthase gene. By optimizing growth light conditions, one-to-four Chl f pigments were found in the complexes. By using a range of spectroscopic techniques, isolated PSI trimeric complexes were investigated to determine how the insertion of Chl f affects excitation energy transfer and trapping efficiency. The results show that the Chls f are functionally connected to the reaction center of the PSI complex and their presence does not change the overall pigment organization of the complex. Chl f substitutes Chl a (but not the Chl a red forms) while maintaining efficient energy transfer within the PSI complex. At the same time, the introduction of Chl f extends the photosynthetically active radiation of the new hybrid PSI complexes up to 750 nm, which is advantageous in far-red light enriched environments. These conclusions provide insights to engineer the photosynthetic machinery of crops to include Chl f and therefore increase the light-harvesting capability of photosynthesis. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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