Abstract
The light-harvesting Chl a/b-protein complex of photosystem II (LHC II) is the major antenna complex which plays an important role in the funneling of excitation energy to the reaction centers, in the plant adaptation to different environmental conditions, the membrane stacking and regulation of the photophysical processes in the antenna. Electron crystallography of LHC II confirmed a structural model of three transmembrane helices and one amphipatic helix located on the membrane surface (1). It has recently been shown that isolated LHC II forms macroaggregates with long-range chiral order and structural flexibility (2) which resemble the chirally organized macrodomains detected in granal thylakoids (3, 4). Macroaggregates with different ultrastructure, lipid content an composition, and content of minor antenna complexes have been isolated using different detergent concentration (5).
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Taneva, S.G., Simidjiev, I., Garab, G., Muga, A. (1998). Thermal Stability and Conformational Properties of Lamellar Macroaggregates of LHC II. In: Garab, G. (eds) Photosynthesis: Mechanisms and Effects. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-3953-3_76
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DOI: https://doi.org/10.1007/978-94-011-3953-3_76
Publisher Name: Springer, Dordrecht
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