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Novel features of LH1‐RC from Thermochromatium tepidum revealed from its atomic resolution structure

Yu, Long‐Jiang, Suga, Michihiro, Wang‐Otomo, Zheng‐Yu, Shen, Jian‐Ren
TheFEBS journal 2018 v.285 no.23 pp. 4359-4366
Thermochromatium tepidum, calcium, electron transfer, energy transfer, ions, photosynthetic bacteria, quinones, spectral analysis, thermal stability
Light‐harvesting‐1 (LH1)‐reaction center (RC) super‐complex is a membrane protein–pigment complex existing in purple photosynthetic bacteria, where LH1 absorbs light energy and transfers them rapidly and efficiently to RC to initiate the charge separation and electron transfer reactions. The structure of LH1‐RC has been reported at relatively low resolutions from several different species of bacteria previously, but was solved at an atomic resolution recently from a thermophilic photosynthetic bacterium Thermochromatium tepidum. This high‐resolution structure revealed the detailed organization of the super‐complex including a number of unique features that are important for its functioning, such as a more intact RC structure, transporting routes for quinones to replace the bound QB as well as for the in‐and‐out of the closed LH1 ring, detailed coordinating environment of the Ca²⁺ ions in LH1 important for the remarkable red shift of the absorption spectrum, as well as for the enhanced thermostability. These results thus greatly advance our understanding on the mechanisms of energy transfer, quinone exchange, the red shift in the LH1‐Qy transition and the enhanced thermal stability, in this super‐complex.