Summary
Electron microscopy has contributed greatly to the structural biology of Photosystem II (PS II) in higher plants and green algae from the level of its in vivo organization, within the thylakoid membrane, through to the determination of the structure of light-harvesting complex II (LHCII) at 3.4 Å. Freeze-fracture and freeze-etch techniques provided the first visualization of PS II and its antenna systems in vivo. Subsequently a range of PS II and PS II-antenna, super- and mega-complexes were purified from thylakoid membranes using mild detergent solubilization and these were structurally characterized by single particle analysis. In particular these studies showed the structural linkage between the PS II core and a range of bound macromolecular light-harvesting antennae, as well as the overall shape of the extrinsic oxygen-evolving complex. Electron crystallography extended the resolution range, revealing the positioning of PS II subunits and the transmembrane helix organization of both PS II and antenna proteins. This technique also identified many of the chlorin cofactors in the reaction center proteins of D1 and D2, and also in the inner antenna, CP47, and outer antenna of LHCII. Future work will involve obtaining more highly resolved structures of supercomplexes and megacomplexes, using electron cryo-microscopy and including structural information emerging from X-ray and electron crystallography, with the view to gaining a near atomic resolution model of higher plant/green algal PS II as it exists in the native thylakoid membrane.
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Hankamer, B., Barber, J., Nield, J. (2005). Structural Analysis of the Photosystem II Core/Antenna Holocomplex by Electron Microscopy. In: Wydrzynski, T.J., Satoh, K., Freeman, J.A. (eds) Photosystem II. Advances in Photosynthesis and Respiration, vol 22. Springer, Dordrecht. https://doi.org/10.1007/1-4020-4254-X_19
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