Abstract
A newly purified Photosystem (PS) I particle is described, with still active iron-sulfur acceptors: A, B and X. Apart from the apoprotein of P700, 3 other main polypeptides of this particle are located at 20, 17 and 10 kDa, and two minor ones are detectable at 16.5 and 8 kDa. Both in vivo 35S labeling and carboxymethylation with iodo[ 14C]acetate show that most of the cysteine residues are located in the 8-kDa band. The amino acid composition of this band reveals important common features with small iron-sulfur proteins of the ferredoxin type.
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