Abstract
Monomolecular layers at the air-water interface were formed directly with isolated largest light-harvesting pigment-protein complex of Photosystem II (LHC II) or out of egg yolk lecithin (EYL) liposomes containing incorporated LHC II. Pure protein monolayers showed a mean area of 1400 A ̊ 2 per molecule at the air-water interface. Monolayers were deposited onto glass slides by means of Langmuir-Blodgett (LB) technique. Chlorophyll fluorescence of LHC II-LB and EYL-LHC II-LB films proved energetic coupling of chlorophyll a and b, thus indicating native conformation of LHC II within the monolayers. Scanning force microscopy (SFM) revealed ring-like structures formed in monocomponent protein layers as well as in mixed protein-lipid films. These results suggest that a structural arrangement of LHC II is favoured in a lipid environment but that the protein has itself a strong tendency for structural complex rearrangement in our system.
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