The Journal of Physical Chemistry Letters · 2018 · 20 citations · 32 references
Life SciencesBiochemistryBiophysicsBiophysical ChemistryPhotosynthesisSpectroscopyPhotochemical KineticsPhotosynthesis BiochemistryPhotosynthesis In MicroorganismsPhotosynthetic Energy ConversionPhotosynthetic Energy TransferPhotosynthetic PigmentsEnergy TransferPhotochemical Energy TransferPhotosynthetic BacteriaPhotosynthetic Reaction CentersPhotosynthetic Reaction KineticsTemperature Dependence Of Electron TransferTemperature Dependence Of Energy TransferThermal Activation
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 (ΔE = 630 cm–1) of 3-fold thermal energy (3kBT). 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 ΔE was found to be linear over a broad range of ΔE, 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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Brent P. Krueger, Gregory D. Scholes, Graham R. Fleming · The Journal of Physical Chemistry B · 1998 · 692 citations
Crystal Structure of the RC-LH1 Core Complex from <i>Rhodopseudomonas palustris</i>
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Structure of the LH1–RC complex from Thermochromatium tepidum at 3.0 Å
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Structure of photosynthetic LH1–RC supercomplex at 1.9 Å resolution
Long‐Jiang Yu, Michihiro Suga, Zheng‐Yu Wang‐Otomo et al. · Nature · 2018 · 174 citations · Full text