7 research outputs found

    The structure of a red-shifted photosystem I reveals a red site in the core antenna

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    Cyanobacterial photosystem I has a highly conserved core antenna consisting of eleven subunits and more than 90 chlorophylls. Here via CryoEM and spectroscopy, the authors determine the location of a red-shifted low-energy chlorophyll that allows harvesting of longer wavelengths of light

    Nanodiscs as a novel approach to resolve inter-protein energy transfer within the photosynthetic membrane of purple bacteria

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    International audiencePhotosynthetic purple bacteria capture sunlight and convert it to chemical energy with almost 100% quantum efficiency: almost every photon absorbed leads to charge separation. Such high efficiency is achieved through a series of ultrafast inter-protein energy transfer events within an antenna network of light-harvesting proteins located in the photosynthetic membrane. Understanding how the organization of proteins within the membrane leads to efficient energy transfer is imperative to designing efficient artificial solar harvesting techniques. Determining inter-protein energy transfer between light-harvesting complex 2 (LH2) proteins, the most common light-harvesting protein in vivo, has proven challenging due to the heterogeneous organization of proteins within the membrane environment. In this work, we introduce model membrane nanodiscs as a novel technique to reconstruct the complex membrane environment in a controlled manner. By forming nanodiscs large enough to incorporate two variants of LH2, we can directly resolve inter-protein energy transfer. By controlling nanodisc size, we can change the inter-protein distance and resolve the effect of membrane organization on energy transfer rate. Using a combination of ultrafast transient absorption spectroscopy, cryogenic electron microscopy, and quantum chemical calculations, we find that LH2 complexes prefer to associate closely in the membrane (25 â„«), with an energy transfer rate of 5.7 ps. The results suggest that these tightly-packed LH2s are important for long-distance energy transfer, as the 25 â„« distance is similar to the most common inter-protein distance in vivo. Overall, our work introduces nanodiscs as a platform to study complex energy transfer events and the effect of membrane organization on critical biological processes

    Elucidating interprotein energy transfer dynamics within the antenna network from purple bacteria

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    International audienceIn photosynthesis, absorbed light energy transfers through a network of antenna proteins with near-unity quantum efficiency to reach the reaction center, which initiates the downstream biochemical reactions. While the energy transfer dynamics within individual antenna proteins have been extensively studied over the past decades, the dynamics between the proteins are poorly understood due to the heterogeneous organization of the network. Previously reported timescales averaged over such heterogeneity, obscuring individual interprotein energy transfer steps. Here, we isolated and interrogated interprotein energy transfer by embedding two variants of the primary antenna protein from purple bacteria, light-harvesting complex 2 (LH2), together into a near-native membrane disc, known as a nanodisc. We integrated ultrafast transient absorption spectroscopy, quantum dynamics simulations, and cryogenic electron microscopy to determine interprotein energy transfer timescales. By varying the diameter of the nanodiscs, we replicated a range of distances between the proteins. The closest distance possible between neighboring LH2, which is the most common in native membranes, is 25 Å and resulted in a timescale of 5.7 ps. Larger distances of 28 to 31 Å resulted in timescales of 10 to 14 ps. Corresponding simulations showed that the fast energy transfer steps between closely spaced LH2 increase transport distances by ∼15%. Overall, our results introduce a framework for well-controlled studies of interprotein energy transfer dynamics and suggest that protein pairs serve as the primary pathway for the efficient transport of solar energy
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