Abstract
AbstractThis article reviews 7Fe ferredoxins (Fds), [FeS] proteins that contain [3Fe–4S]+/0and [4Fe–4S]2+/+clusters. The 7Fe Fds from 19 prokaryotes are described in terms of biological function, and categorized with respect to cysteine ligand motifs, length of amino‐acid sequence, and metal ion content. Biochemical, mutagenesis, electrochemical, spectroscopic, and crystallographic data are summarized for well‐studied examples of distinct subclasses, including 7Fe Fds fromAzotobacter vinelandii,Desulfovibrio africanus,Bacillus schlegelii, andSulfolobus acidocaldarius. 7Fe Fds have been used to study cysteine ligand motifs, the interconversion of [3Fe–4S] and [4Fe–4S] clusters, proton transfer to [3Fe–4S]0clusters, and the protein control of [FeS] cluster reduction potential.
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