Abstract
The amino acid sequences of ferredoxins I and II from a blue-green alga, Nostoc strain MAC were determined. This alga is able to grow autotrophically in the light or heterotrophically in the dark. Analyses of tryptic peptides of Cm-proteins by conventional methods including solid-phase Edman degradation gave the complete amino acid sequences. Both molecules consisted of 98 amino acid residues and 34 amino acid differences including two deletions were found between the two. Comparing these sequences with those of ferredoxins from Chlorogloeopsis fritschii and Synechocystis 6714, which are also capable of growing under both conditions, showed that Nostoc strain MAC ferredoxin II had unique amino acids around the [2Fe-2S] cluster. This finding provides a structural basis for explaining the different chemical and functional properties of Nostoc strain MAC ferredoxin II reported in a previous paper (Hutson et al. (1978) Biochem. J. 172, 465-477).
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