Abstract
Due to the availability of synthetic precedents, the Fe2(μ-O)2 diamond core has emerged as an attractive candidate for the core structures of the high-valent intermediates of nonheme diiron enzymes such as methane monooxygenase and ribonucleotide reductase. Such cores have spectroscopic signatures that distinguish them from other proposed structures, particularly the Fe=O moiety associated with high-valent states of heme enzymes. The Mössbauer, Raman, and EXAFS features of the Fe2(μ-O)2 diamond core can be used to ascertain whether the high-valent intermediates of methane monooxygenase and ribonucleotide reductase utilize such structures to access the iron(IV) oxidation state.
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