Abstract
Iron-sulfur (Fe–S) clusters are considered one of the most ancient and versatile inorganic cofactors present in the three domains of life. Fe–S clusters can act as redox sensors or catalysts and are found to be used by a large number of functional and structurally diverse proteins. Here, we cover current knowledge of the SUF multiprotein machinery that synthesizes and inserts Fe–S clusters into proteins. Specific focus is put on the ABC ATPase SufC, which contributes to building Fe–S clusters, and appeared early on during evolution.
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