Abstract
P700, the primary donor of photosystem 1 is thought to consist of a ‘special pair’ of chlorophylls, similar to the primary donor in the well-characterized reaction center (RC) of purple bacteria. A pair of chlorophylls near the lumenal side, oriented parallel to each other and with their plane perpendicular to the membrane, has been identified in the X-ray structural model and attributed to P700 (1). These structural results are in good agreement with spectroscopic data on P700. However, the actual resolution did not yet allow determining the sites of interaction between the protein and the cofactors and especially which residues provide the 5th, axial ligand to the Mg2+ of the two Chl a molecules. Visible and FTIR difference spectroscopy are suitable tools to study pigment-protein interactions especially when combined with site-directed mutagenesis (2).
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