Abstract
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.
Original language | English |
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Pages (from-to) | 326-331 |
Number of pages | 6 |
Journal | Nature |
Volume | 361 |
Issue number | 6410 |
Publication status | Published - 28 Jan 1993 |