Functional organization of photosystem II antenna complexes
| Autor: | Laura M. Roy, Roberta Croce, Pengqi Xu |
|---|---|
| Přispěvatelé: | Biophysics Photosynthesis/Energy, LaserLaB - Energy |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
Chlorophyll
0301 basic medicine Photosynthetic reaction centre Light Photosystem II Pigment binding Arabidopsis Light-Harvesting Protein Complexes Biophysics Photosynthesis Photochemistry CP29 Biochemistry Light-harvesting complex Chloroplast Proteins 03 medical and health sciences SDG 7 - Affordable and Clean Energy PSII supercomplexes Arabidopsis Proteins Chemistry Spectrum Analysis Photosystem II Protein Complex Pigments Biological Cell Biology Carotenoids 030104 developmental biology Membrane Energy Transfer Ribonucleoproteins Membrane protein In vivo mutation analysis Mutation sense organs Light-harvesting complexes Chlorophyll Binding Proteins Antenna (radio) |
| Zdroj: | Biochimica et Biophysica Acta-Bioenergetics, 1858(10), 815-822. Elsevier Xu, P, Roy, L M & Croce, R 2017, ' Functional organization of photosystem II antenna complexes : CP29 under the spotlight ', Biochimica et Biophysica Acta-Bioenergetics, vol. 1858, no. 10, pp. 815-822 . https://doi.org/10.1016/j.bbabio.2017.07.003 |
| ISSN: | 0005-2728 |
| Popis: | In the first step of the photosynthetic process, light is absorbed by the pigments associated with the antenna proteins, known as light-harvesting complexes (Lhcs), which in vivo are functionally organized as hetero-oligomers. The architecture of the pigments, chlorophylls, and carotenoids bound to each LHC is responsible for the efficient excitation energy transfer resulting in photochemistry. So far, the only LHC studied in depth was LHCII, the most abundant membrane protein of plants, while less information was available for the other antennae. In particular, despite the availability of the structure of CP29 obtained at near atomic resolution in 2011 (Pan et al., 2011), the mismatch in pigment content and spectroscopic properties between CP29 in solution and in the crystal has hampered the possibility to use the structure to interpret the experimental data. In this work, we purified CP29 and its larger assembly (CP29-LHCII-CP24) from the membrane in very mild conditions using a His-tag, and we have studied their pigment binding and spectroscopic properties. In addition, we have performed mutation analysis in vivo to obtain mutants of CP29 lacking individual chlorophylls. The peculiar properties of this antenna support its role in directing the energy flow from the external antennae to the reaction center. |
| Databáze: | OpenAIRE |
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