Non-redox roles for iron-sulfur clusters in enzymes.

In recent years a number of enzymes have been discovered which, contrary to prior expectations, contain FeS clusters but do not participate in redox reactions. In all cases but one, where the FeS cluster in these enzymes has been identified, it is a [4Fe-4S] cluster. In mammalian aconitase a single Fe atom of the [4Fe-4S] cluster participates in catalysis of hydration-dehydration reactions by direct ligation to the substrates. A number of hydrolyases containing FeS clusters have now been identified. In Bacillus subtilis glutamine phosphoribosyl-pyrophosphate amidotransferase the [4Fe-4S] cluster is essential for the active structure of the enzyme, but probably does not participate directly in catalysis. Rather, the cluster may serve as part of a mechanism of oxidative inactivation of the enzyme in vivo, which is followed by its intracellular degradation. The role played by a [4Fe-4S] cluster in Escherichia coli endonuclease III is at present completely unknown. Thus, a number of novel roles for FeS clusters in enzymology and protein structure have been discovered, and more novel findings must be anticipated.