Abstract
The amino-acid sequence of ferredoxin III from the sulfate-reducing bacterium Desulfovibrio africanus was determined by a combination of various conventional methods. It is composed of 61 amino acids, including seven cysteine residues. One of the cysteine-containing segments shows exactly the same distribution as clostridial ferredoxins for binding a (4Fe-4S) cluster, but the other shows a unique distribution, with a cysteine and a proline residue replaced by aspartic and glutamic acid, respectively. This cysteine distribution could possibly accommodate a three-iron center. The ferredoxin III sequence is compared to other Desulfovibrio ferredoxins and to other bacterial ferredoxins thought to contain three iron centers and devoid of a cysteine residue. Structural features common to all are discussed which may be necessary to bind three-iron centers.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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