X-ray structure analysis shows that the monomer of trimeric photosystem I (PS I) of Synechococcus sp. consists of a catalytic domain and a smaller domain that connects the monomers. The 4Fe-4S clusters F(X), F(A) and F(B), 28 alpha-helices and 45 chlorophyll a molecules were located. The two large subunits of PS I are represented by nine alpha-helices each; they are related by a local 2-fold rotation axis passing through F(X). Electron densities close to this axis are interpreted as carriers of the electron transfer chain.
|Number of pages||6|
|Publication status||Published - 28 Jan 1993|