Journal of Energy Bioscience 2024, Vol.15, No.4, 255-266 http://bioscipublisher.com/index.php/jeb 258 Additionally, the structural and functional integrity of photosynthetic complexes can be compromised under stress conditions, affecting their ability to capture and convert light energy efficiently (Jordan et al., 2001). The adaptability of photosynthetic organisms to different ecological niches has led to structural changes in photosystems, which can influence their performance under varying environmental conditions (Amunts and Nelson, 2009). Understanding these stress responses and their impact on photosynthetic efficiency is crucial for optimizing photosynthetic systems for improved light energy conversion. By addressing these challenges and leveraging insights from natural photosynthetic systems, researchers can develop more efficient artificial photosynthetic systems for practical solar fuels production and other applications. Figure 1 Structures of PSI-LHCI-LHCII from plants and green algae (Adopted from Shang et al., 2023) Image caption: (a) Overall structure of ZmPSI-LHCI-LHCII (PDB code: 5ZJI). (b) Overall structure of CrPSI-LHCI-LHCII (PDB code: 7DZ7). (c) Modeled PpPSI-LHCI-LHCII based on the PpPSI-L structure (PDB code: 8HTU). The PSI-LHCI parts are displayed as a cartoon, with Lhcas, PsaO, and ZmPsaN shown in different colors and labeled. The other core subunits are shown in white. The LHCII trimers are displayed as a surface and distinguished by different colors. The Lhcb9 and Lhca proteins in the outer LHCI belt from PpPSI-L, which are not included in the modeled PpPSI-LHCI-LHCII, are shown as a ribbon. (d) Comparison of the membrane-spanning regions of the three PSI-LHCI-LHCII complexes. LHCIIs (CrLHCII-1) are displayed as a cartoon, and other parts are shown as a ribbon. ZmPSI-LHCI-LHCII, CrPSI-LHCI-LHCII, and modeled PpPSI-LHCI-LHCII are displayed in magenta, yellow, and cyan, respectively. Arrows indicate the deflection of LHCII relative to the membrane. The phosphorylated N-terminal regions of LHCIIs are highlighted in a red box. (e) Structural comparison of the first five residues from ZmLhcb2, CrLhcbM1, and PpLhcbM2. (f) Zoomed-in view of the binding sites of the N-terminal regions of CrLhcbM1 and CrLhcbM5 in CrPSI-LHCI-LHCII. The phosphorylated Thr residues are highlighted with spheres (Adapted from Shang et al., 2023)
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