Spectroscopic and Magnetic Studies of Metalloprotein Active Sites

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A coupled binuclear non-heme iron active site exists in a variety of proteins which perform different biological functions. hemerythrin (Hr) binds O2, methane monooxygenase activates it for hydroxylation, reducted ribonucleotide reductase reacts with O2 to generate a catalytically active tyrosyl radical, and reduced purple acid phosphatase is oxidatively inactivated in the presence of phosphate. These protein sites (and analogous model complexes) can be obtained in three oxidation states. Dr. Solomon's spectral studies on these sites and their substrate and small molecule bound forms emphasize bsorption, circular dichrosims, and magnetic circular dichroism (MCD) to probe the excited states, and variable- temperature, variable-field MCD to probe ground state sublevel splittings. This data enables a determination of the geometry of each iron, and the exchange coupling which is associated with bridging ligation. The goal of this research is to define active site geometric and electronic structural diffeences which correlate with variation in biological reactivity.