Non-heme iron dioxygenase models

Since in catechol dioxygenases there are two tyrosinates coordinated to iron in the active site [94,95],the above complex may be regarded as a mimic for the enzyme center. Iron(III) is not necessarily reduced by coordinated catecholate, and the high-spin iron(III) can 

Weller and Weser s iron(III)-NTA complex shows catechol cleavage activity [96], converting 3,5-DTBC to 3,5-di-t-butyl-5-carboxymethyl- 

2-furanone (15). Salts of [Fe(NTA)(2,3-DTBC)], which have been isolated with a stoichiometry indicating that catecholate is coordinated to iron(III) as a bidentate ligand [97], are converted to the cleavage product upon reaction with O. Interestingly, the related 

Fe-N bond in [Fe(NTA) (2,3-DTBC) ]. This bond cleavage leads to unidentate catecholate coordination, which allows for reaction with 

Recently, a series of iron(III) complexes [Fe(D(3,5-DTBC)], where L is the tripodal ligand nitrilotriacetate (NTA) or its derivatives 41, 42 and 43, 44, 45, 46 have been synthesized and the systems shown to act as functional mimics for catechol 1,2-dioxygenase [98-100]. The ligands used permit adjustment of the Lewis acidity of the ferric 

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