Abstract
Photosystem I (PSI) converts the energy of light into chemical energy. The terminal electron transfer cofactors in PS I are three iron-sulfur clusters named FX, FA and FB. The PsaC subunit of PS I harbors binding sites of the [4Fe-4S] clusters FA and FB. We modeled them by preparing two peptides (maquettes), sixteen amino acids each, using Fmoc solid state peptide synthesis. These model peptides incorporate the consensus iron-sulfur binding motif along with amino acids from the immediate environment of the respective iron-sulfur cluster. The [4Fe-4S] clusters were successfully incorporated into these model peptides, as shown by their optical absorbance, EPR and Mossbauer spectra. The oxidation- reduction potential of the iron-sulfur clusters in the model peptides is close to that of FA and FB in PsaC at room temperature and is considerably lower than that observed for other [4Fe-4S] model systems described earlier.
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