期刊
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
卷 9, 期 12, 页码 3278-3284出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.8b01197
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资金
- Natural Science Foundation of China (NSFC) [21673288]
- JSPS KAKENHI [JP16H04174]
- JSPS Research Fellowship
The uphill excitation energy transfer (EET) from the core antenna (LH1) to the reaction center (RC) of purple photosynthetic bacteria was investigated at room temperature by comparing the native LH1-RC from Thermochromatium (Tch.) tepidum with the hybrid LH1-RC from a mutant strain of Rhodobacter (Rba.) sphaeroides. The latter protein with chimeric Tch-LH1 and Rba-RC exhibits a substantially larger RC-to-LH1 energy difference (Delta E = 630 cm(-1)) of 3-fold thermal energy (3k(B)T). The spectroscopic and kinetics results are discussed on the basis of the newly reported high-resolution structures of Tch. tepidum LH1-RC, which allow us to propose the existence of a passage formed by LH1 BChls that facilitates the LH1 -> RC EET. The semilogarithmic plot of the EET rate against Delta E was found to be linear over a broad range of Delta E, which consolidates the mechanism of thermal activation as promoted by the spectral overlap between the LH1 fluorescence and the special pair absorption of RC.
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