The amino acid sequence of ferredoxin from Brassica napus (rape)

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Abstract
The amino acid sequence of the ferredoxin of B. napus was determined by using a Beckman 890C sequencer in combination with the characterization of peptides obtained by tryptic and chymotryptic digestion of the protein; some peptides were subdigested with thermolysin. The molecule consists of a single polypeptide chain of 96 amino acid residues and has an unblocked N-terminus. The primary structure shows considerable similarity with other plant-type ferredoxins. [Ferredoxins are a class of iron-sulfur proteins that act as electron carriers in a number of different biochemical processes, including photosynthetic electron transport.].