Purification and amino acid sequence of a fern (Gleichenia japonica) ferredoxin.

A chloroplast-type ferredoxin was purified from a fern, Gleichenia japonica, and its amino acid sequence was determined. The conventional method for soft leaves proved to be unsuitable for the extraction of ferredoxin from G. japonica, but a good yield was obtained by blending the leaves in cold acetone. The analysis of 8 tryptic peptides of Cm-ferredoxin gave the complete amino acid sequence. The molecule consisted of a single polypeptide chain of 95 amino acid sequence. The molecule consisted of a single polypeptide chain of 95 amino acid residues and lacked tryptophan. Relatively high contents of phenylalanine and arginine were noted, some of which had unique locations in comparison with other ferredoxins. G. japonica ferredoxin did not show a close sequence homology with the ferredoxins from horsetails, which, like ferns, belong to Pteridophyta, or with those from plants of different taxonomical groups. The fern ferredoxins were suggested to form a unique group in the chloroplast-type ferredoxins.