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  • Title: Enzymatic ring opening of an iron corrole by plant-type heme oxygenases: unexpected substrate and protein selectivities.
    Author: Gisk B, Brégier F, Krüger RA, Bröring M, Frankenberg-Dinkel N.
    Journal: Biochemistry; 2010 Nov 30; 49(47):10042-4. PubMed ID: 20979354.
    Abstract:
    Heme oxygenases are widely distributed enzymes involved in the oxidative cleavage of the heme macrocycle that yields the open-chain tetrapyrrole biliverdin IX, CO, and iron. For the first time, two regioisomeric iron corroles [α-CH- and γ-CH-Fe(cor)] have been utilized as artificial substrate and cofactor analogues to mammalian, plant, cyanobacterial, and bacterial heme oxygenases. The non-natural enzymatic cleavage of γ-CH-Fe(cor), catalyzed by plant-type heme oxygenases from Arabidopsis thaliana and Synechocystis sp., happens selectively at the unexpected bipyrrolic position and yields a biomimetic biliverdin-like product. The reaction is selective for this corrole regioisomer and for plant-type heme oxygenases and is the first report of an enzymatic corrole ring opening.
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