Water-Dependent Reactions of Diiron(II) Carboxylate Complexes.

The article discusses the water-dependent reactions of diiron(II) carboxylate complexes. Carboxylate-bridged diiron(II) cores, housed in four-helix bundles, occur frequently at the active sites of dioxygen-dependent non-heme diiron enzymes. The R2 subunit of ribonucleotide reductase, toluene monooxygenase, and the hydroxylase component of soluble methane monooxygenase are important members of this metalloprotein family. Much effort has been devoted to reproducing the structures and functions of the active sites in these enzymes by synthetic model complexes. So, the article describes the isolation and characterization of novel iron(II) complexes with varying numbers of ligated water molecules, indicating the existence of water-dependent structures involving the carboxylate-bridged diiron(II) core.