Phosphatidylcholine-induced reactivation of photosystem II membranes pretreated with Triton X-100

Triton X-100-induced inactivation and phosphatidylcholine-induced reactivation of photosystem II (PSII) membranes were investigated using oxygen electrode, variable fluorescence and spectroscopic techniques including absorption and circular dichroism spectroscopy. Incubation of the PSII membrane with Triton X-100 reduced the oxygen-evolving rate, modified the variable chlorophyll fluorescence kinetics, changed the protein secondary structures, altered the chlorophyll binding state to proteins and decreased the excitonic interaction of chlorophyll molecules. Phosphatidylcholine addition did not change the protein secondary structures, but could partially reactivate the reduced oxygen-evolving rate, and partly reversed the variable fluorescence parameters, the chlorophyll binding state and the excitonic interaction of the chlorophyll molecules. The results indicate that the phosphatidylcholine environment can optimize the tertiary structures of PSII.