Molecular reorganization induced by Ca2+ of plant photosystem I reconstituted into phosphatidylglycerol liposomes.

The interaction of divalent cations with biomembranes is important for a number of biological processes. In this study, the regulatory effect of Ca2+ on the interaction between plant spinach photosystem I (PSI) particles and negatively charged lipid phosphatidylglycerol (PG) was investigated by circular dichroism (CD) spectroscopy. It was found that in the absence of CaCl2, PG causes an increase in alpha-helix and a decrease in disordered conformations of protein secondary structures of PSI, the beta-sheet and turns being almost unaffected. Meanwhile, the same effect also enhances the excitonic interactions relating to Chl a and Chl b from the PSI core complex and external antenna light-harvesting complex (LHCI). By contrast, in the presence of CaCl2, PG hardly interferes with the structure of the proteins' skeleton of PSI, but it can depress the excitonic interactions for Chl b of LHCI and for PSI core complex Chl a at (-) 433.5 nm of the CD signal which is accompanied by a blue shift of its peak. It is most likely that the neutralization of the phosphate groups in the PSI-PG complex and the negative surface charges of PSI, and partial dehydration in the vicinity of the ester CO region of the PG polar head group by the Ca-ions modify the interaction between PSI and PG, thereby inducing molecular reorganization of protein and pigments within both the external antenna LHCI and PSI core complex in proteoliposomes.