MODELS OF THE REDUCED FORMS OF POLYIRON-OXO PROTEINS : AN ASYMMETRIC, TRIPLY CARBOXYLATE BRIDGED DIIRON(II) COMPLEX AND ITS REACTION WITH DIOXYGEN

A diiron(II) model compound having features relevant to the active sites of the reduced forms of the polyiron-oxo proteins hemerythrin (Hr), ribonucleotide reductase (RR), and methane monooxygenase (MMO) has been prepared and characterized by elemental analysis, X-ray crystallography, magnetic susceptibility measurements, and Mossbauer, UV-vis, IR, 1 H NMR, and RPT spectroscopy