Hemerythrin model compounds

A new class of metalloprotelns containing polynuclear, non-heme oxo-bridged iron complexes has emerged recently. Dinuclear centers are present in hemerythrin (Hr), ribonucleotide reductase (RR), purple acid phosphatases (PAP) and, possibly, methane monooxygenase (MMO) these centers as well as model compounds are reviewed in Chapter 8. 

A second relevant aspect here is the consideration of models for the various dimetal species that could be important in the reactions at the ferroxidase centers. The area of di-iron metallosites has received a great deal of attention from the early 1980s since the identification of such sites in hemerythrin and the production of the first coordination chemistry model compounds for these (Chapters 8.12 and 8.13). Subsequently several other systems with this motif have been studied and the ones of most relevance to the ferroxidase centers would appear to be those involved in oxygen activation rather than transport. ... 

The complex HB(pz)3Fe(p-CH3C00)2(p-0)Fe(pz)3BH, prepared in one step as a model for the binuclear iron center in hemerythrin, contains two CH3COO and one O bridge between the two Fe(III) atoms. The same holds true for the similarly synthesized diformato and dibenzoato analogs The oxygen bridge in these compounds... 

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