Enzymatic Ring Opening of an Iron Corrole by Plant-Type Heme Oxygenases: Unexpected Substrate and Protein Selectivities

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 co...

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Bibliographic Details
Published in:Biochemistry (Easton) 2010-11, Vol.49 (47), p.10042-10044
Main Authors: Gisk, Björn, Brégier, Frédérique, Krüger, Robin A, Bröring, Martin, Frankenberg-Dinkel, Nicole
Format: Article
Language:English
Subjects:
Arabidopsis Proteins - metabolism
Heme - analogs & derivatives
Heme - metabolism
Heme Oxygenase (Decyclizing) - antagonists & inhibitors
Heme Oxygenase (Decyclizing) - metabolism
Metalloporphyrins - metabolism
Plants - enzymology
Substrate Specificity
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Summary: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.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi1014369