Primary structure of a high potential, four-iron-sulfur ferredoxin from the photosynthetic bacterium Rhodospirillum tenue.
The amino acid sequence of a high oxidation-reduction potential iron-sulfur protein (HiPIP) isolated from the purple photosynthetic bacterium Rhodospirillum tenue has been determined. This is the smallest of the HiPIP's, containing 63 residues, with only 3 residues apparently conserved in addition to the 4 cluster-binding cysteines. A minimum of four internal genetic gaps is postulated to align tenue high potential iron-sulfur protein with the previously known proteins. It is the most divergent of its class, with an average of only 25% identically matching residues in common with any of the other species.
D000595:Amino Acid Sequence; D002918:Chymotrypsin; D005288:Ferredoxins; D010446:Peptide Fragments / Q000032:analysis; D012246:Rhodospirillum / Q000032:analysis*; D013045:Species Specificity; D013820:Thermolysin; D014357:Trypsin
D005288:Ferredoxins; D010446:Peptide Fragments; D002918:Chymotrypsin; D014357:Trypsin; D013820:Thermolysin