The amino acid sequence of a ferredoxin from parsley (Petroserinum sativum) was determined by various conventional methods. Five tryptic peptides of carboxymethylated(Cm)-ferrodoxin were sequenced by a combination of automatic solid-phase and manual Edman degradations. The amino(N)-terminal sequences of Cm-ferrodoxin and its carboxy(C)-terminal half produced by tryptic cleavage specifically at the sole arginine residue of the molecule overlapped the five tryptic peptides. The molecule consists of 96 amino acid residues, including 5 cysteines, and lacks tryptophan. Parsley ferredoxin shows the greatest homology to wheat ferredoxin among other green plant ferredoxins.
The complete amino acid sequence of parsley (Petroserinum sativum) ferrodoxin. Publishing Authors By Initials