Photosynthetic bacteria do not release oxygen during photosynthesis but can convert solar energy into chemical energy with remarkably high efficiency. They also utilize near-infrared light—wavelengths unused by plants—and thrive in diverse environments, including freshwater, seawater, and hot springs.
Among these organisms, the marine purple nonsulfur bacterium Rhodovulum sulfidophilum is a model species notable for its strong tolerance to oxygen. However, the molecular mechanism by which its light-harvesting and energy-converting LH1-RC complex maintains highly efficient photosynthesis under oxic conditions remains unclear.
Researchers at University of Tsukuba used cryo-electron microscopy to visualize the structure of the protein complex responsible for photosynthesis in Rhodovulum sulfidophilum. Their analysis uncovered a previously unrecognized membrane protein and revealed structural features that could explain how this organism achieves efficient energy conversion despite the presence of oxygen.
In their study published in Communications Biology, the researchers determined the structure of the LH1-RC complex at an exceptionally high resolution of 1.8 Å using cryo-EM. Their analysis identified a previously unknown membrane protein called protein-3h, which is located within the LH1 opening. They further discovered a non-heme Fe ion positioned near the triheme cytochrome subunit, which is coordinated by a histidine residue and water molecules rather than by heme. This configuration indicates that the Fe ion might act as an intermediary site for electron transfer.
These findings provide deeper insight into the photosynthetic complex in R. sulfidophilum and could contribute to future applications, such as genetically engineered phototrophic systems and environmentally relevant technologies, including the bioremediation of hydrogen sulfide-containing wastewater.
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