Abstract
The aminoa cid sequence of ferredoxin I from a blue-green alga, Aphanizomenon flos-aquae, was determined. Tryptic and staphylococcal protease peptides were prepared and their sequences were analyzed. The ferredoxin was composed of 97 amino acid residues with a molecular weight of 10 384, excluding two iron and two sulfur atoms in the [2Fe-2S] cluster, and lacked methionine and tryptophan. The numbers of amino acid differences among blue-green algal ferredoxins indicated that A. flos-aquae ferredoxin has considerable similarity to other filamentous algal ferredoxins.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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