Publication date: 8th October 2020
The light-harvesting two complex (LH2) of the purple photosynthetic bacterium Rhodobacter (Rba.) sphaeroides is a highly efficient, light-harvesting antenna that allows growth under a wide-range of light intensities. In order to expand the spectral range of this antenna complex, we first used a series of competition assays to measure the capacity of the non-native pigments 3-acetyl chlorophyll (Chl) a, Chl d, Chl f or bacteriochlorophyll (BChl) b to replace native BChl a in the B800 binding site of LH2. We then adjusted the B800 site and systematically assessed the binding of non-native pigments. We find that Arg-10 of the LH2 β polypeptide plays a crucial role in binding specificity, by providing a hydrogen-bond to the 3-acetyl group of native and non-native pigments. Reconstituted LH2 complexes harbouring the series of (B)Chls were examined by transient absorption and steady-state fluorescence spectroscopies. Although slowed 10-fold to ~6 ps, energy transfer from to Chl a to B850 BChls remained highly efficient. We measured faster energy-transfer rates for Chl d (3.5 ps-1) and Chl f (2.7 ps-1), which have red-shifted absorption maxima compared to Chl a. BChl b, red-shifted from the native BChl a, gave extremely rapid (≤0.1 ps-1) transfer. These results show that modified LH2 complexes, combined with engineered (bacterio)chlorophyll biosynthesis pathways in vivo, have potential for retaining high efficiency while acquiring increased spectral range.
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