JBC, Vol. 251, Issue 1, 129-136, Jan, 1976
Primary structure of a high potential iron-sulfur protein from the purple non-sulfur photosynthetic bacterium Rhodopseudomonas gelatinosa
S. M. Tedro, T. E. Meyer and M. D. Kamen
The third amino acid sequence of a high potential iron-sulfur protein, that
of the non-sulfur purple photosynthetic bacterium Rhodopseudomonas
gelatinosa, has been determined. It consists of a single polypeptide chain
of 74 amino acid residues, which is slightly smaller than the high
potential iron-sulfur proteins from the sulfur purple bacteria Chromatium
vinosum (85 residues) and Thiocapsa pfennigii (81 residues). The sequence
of the gelatinosa protein is similar to the C. vinosum and T. pfennigii
proteins with 38% and 37% identically matching residues, although six gaps
are proposed for the comparison (the C. vinosum and T. pfennigii proteins
have 44% identically matching residues out of 73 positions compared with
only one 4-residue gap). Only 17 redisues, including the 4 cystein residues
essential for binding the four-iron-sulfur chromophore, are invariant in
the three known sequences. A discussion of the role of conserved residues
in maintenance of the three-dimensional structure and in electron transport
is presented.
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