Heme dioxygenases structure

Contents I. A. Cohen Metal-Metal Interactions in Metalloporphy-rins, Metalloproteins and Metalloenzymes. - L QueJr. Non-Heme Iron Dioxygenases. Structure and Mechanism. - H. Umezawa,... 

The heme dioxygenase enzymes involved in tryptophan oxidation catalyse the first and rate-limiting step in the kynurenine pathway—the 02-dependent oxidation of 1-tryptophan to AT -formylkynurenine. In the past 10 years, there have been substantial new developments, including new structural information, bacterial expression systems for a number of dioxygenases, contributions from computational chemistry, and emerging... 

A representative sampling of non-heme iron proteins is presented in Fig. 3. Evident from this atlas is the diversity of structural folds exhibited by non-heme iron proteins it may be safely concluded that there is no unique structural motif associated with non-heme iron proteins in general, or even for specific types of non-heme iron centers. Protein folds may be generally classified into several categories (i.e., all a, parallel a/)3, or antiparallel /8) on the basis of the types and interactions of secondary structures (a helix and sheet) present (Richardson, 1981). Non-heme iron proteins are found in all three classes (all a myohemerythrin, ribonucleotide reductase, and photosynthetic reaction center parallel a/)8 iron superoxide dismutase, lactoferrin, and aconitase antiparallel )3 protocatechuate dioxygenase, rubredoxins, and ferredoxins). This structural diversity is another reflection of the wide variety of functional roles exhibited by non-heme iron centers. 

Cobaltn-Schiff base complexes, e.g. Co(salen),567 Co(acacen)568 and cobalt(II) porphyrins,569 e.g. Co(TPP), are effective catalysts for the selective oxygenation of 3-substituted indoles to keto amides (equation 249), a reaction which can be considered as a model for the heme-containing enzyme tryptophan-2,3-dioxygenase (equation 21).66 This reaction has been shown to proceed via a ternary complex, Co-02-indole, with probable structure (175), which is converted into indolenyl hydroperoxide (176). Decomposition of (176) to the keto amide (174) readily occurs in the presence of Co(TPP), presumably via formation of a dioxetane intermediate (177).569,56 Catalytic oxygenolysis of flavonols readily occurs in the presence of Co(salen) and involves a loss of one mole of CO (equation 251).570... 

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