Abstract
There is much current interest in non-heme diiron carboxylate proteins. Included are the hydroxylase enzyme of methane monooxygenase (MMO), hemerythrin, ribonucleotide reductase, and purple acid phosphatase, all of which contain a dinuclear iron center at their active site. We ultimately desire an understanding of how these units are tuned in each protein to exhibit diverse functions ranging from the reversible binding of dioxygen in hemerythrin to activation of dioxygen for converting methane to methanol in MMO. In pursuit of this objective, we are investigating the proteins of the MMO system and exploring the fundamental chemistry of the hydroxylase diiron center. In the present article we review some of our recent progress in this area.
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