Contribution of low-temperature single-molecule techniques to structural issues of pigment–protein complexes from photosynthetic purple bacteria
| Autor: | Richard J. Cogdell, Jürgen Köhler, Alexander Löhner |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Materials science Light-Harvesting Protein Complexes Biomedical Engineering Biophysics Degrees of freedom (statistics) Bioengineering 010402 general chemistry 01 natural sciences Biochemistry Purple bacteria Spectral line Biomaterials 03 medical and health sciences Bacterial Proteins Molecule Photosynthesis Spectroscopy Review Articles Physics::Biological Physics biology Observable Pigments Biological Chromophore biology.organism_classification Photobleaching 0104 chemical sciences Rhodopseudomonas 030104 developmental biology Chemical physics Biotechnology |
| Zdroj: | Journal of The Royal Society Interface. 15:20170680 |
| ISSN: | 1742-5662 1742-5689 |
| DOI: | 10.1098/rsif.2017.0680 |
| Popis: | As the electronic energies of the chromophores in a pigment–protein complex are imposed by the geometrical structure of the protein, this allows the spectral information obtained to be compared with predictions derived from structural models. Thereby, the single-molecule approach is particularly suited for the elucidation of specific, distinctive spectral features that are key for a particular model structure, and that would not be observable in ensemble-averaged spectra due to the heterogeneity of the biological objects. In this concise review, we illustrate with the example of the light-harvesting complexes from photosynthetic purple bacteria how results from low-temperature single-molecule spectroscopy can be used to discriminate between different structural models. Thereby the low-temperature approach provides two advantages: (i) owing to the negligible photobleaching, very long observation times become possible, and more importantly, (ii) at cryogenic temperatures, vibrational degrees of freedom are frozen out, leading to sharper spectral features and in turn to better resolved spectra. |
| Databáze: | OpenAIRE |
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