Amino acid sequence of [2Fe-2S] ferredoxin from Clostridium pasteurianum.

The complete amino acid sequence of the [2Fe-2S] ferredoxin from the saccharolytic anaerobe Clostridium pasteurianum has been determined by automated Edman degradation of the whole protein and of peptides obtained by tryptic and by staphylococcal protease digestion. The polypeptide chain consists of 102 amino acids, including 5 cysteine residues in positions 11, 14, 24, 56, and 60. The sequence has been analyzed for hydrophilicity and for secondary structure predictions. In its native state the protein is a dimer, each subunit containing one [2Fe-2S] cluster, and it has a molecular weight of 23,174, including the four iron and inorganic sulfur atoms. The extinction coefficient of the native protein is 19,400 M-1 cm-1 at 463 nm. The positions of the cysteine residues, four of which are most probably the ligands of the [2Fe-2S] cluster, on the polypeptide chain of this protein are very different from those found in other [2Fe-2S] proteins, and in other ferredoxins in general. In addition, whole sequence comparisons of the [2Fe-2S] ferredoxin from C. pasteurianum with a number of other ferredoxins did not reveal any significant homologies. The likely occurrence of several phylogenetically unrelated ferredoxin families is discussed in the light of these observations.

Amino acid sequence of the [4Fe-4S] ferredoxin isolated from Desulfovibrio desulfuricans Norway.

The complete amino acid sequence of the [4Fe-4S] ferredoxin from Desulfovibrio desulfuricans Norway was determined by repetitive Edman degradation of the whole protein and peptides derived from tryptic digestion. The protein has 59 residues. Four of the six cysteine residues are involved in the binding of the [4Fe-4S] cluster in the same arrangement as in clostridial ferredoxins. This sequence is compared to various Desulfovibrio ferredoxin sequences and to the sequence and three-dimensional structure of Peptococcus aerogenes ferredoxin. Evidence of gene duplication is indicated. The requirement of some sequence features in the ferredoxin for an interaction process with its electron transfer partner, cytochrome c3, is postulated in the discussion.