Contribution of low-temperature single-molecule techniques to structural issues of pigment-protein complexes from photosynthetic purple bacteria.
Contribution of low-temperature single-molecule techniques to structural issues of pigment-protein complexes from photosynthetic purple bacteria.
复制标题
低温单分子技术对光合紫色细菌色素-蛋白质复合物结构问题的贡献。
DOI:
10.1098/rsif.2017.0680
复制
发表时间:
2018
期刊:
影响因子:
--
通讯作者:
Löhner A
中科院分区:
文献类型:
--
作者:
Löhner A
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.