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Literature summary for 1.14.14.18 extracted from

  • Gisk, B.; Bregier, F.; Krueger, R.A.; Broering, M.; Frankenberg-Dinkel, N.
    Enzymatic ring opening of an iron corrole by plant-type heme oxygenases: unexpected substrate and protein selectivities (2010), Biochemistry, 49, 10042-10044.
    View publication on PubMed
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Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
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Synechocystis sp.
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
gamma-CH-Fe(cor) + 3 AH2 + 3 O2 the regioisomeric iron corrole is an artificial, not-natural substrate, the enzymatic cleavage happens selectively at the unexpected bipyrrolic position and yields a biomimetic biliverdin-like product. The enzymatic corrole ring opening is selective for this corrole regioisomer and for plant-type heme oxygenase, mechanism, overview Arabidopsis thaliana ?
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gamma-CH-Fe(cor) + 3 AH2 + 3 O2 the regioisomeric iron corrole is an artificial, not-natural substrate, the enzymatic cleavage happens selectively at the unexpected bipyrrolic position and yields a biomimetic biliverdin-like product. The enzymatic corrole ring opening is selective for this corrole regioisomer and for plant-type heme oxygenase, mechanism, overview Synechocystis sp. ?
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 ?

General Information

General Information Comment Organism
physiological function 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 Arabidopsis thaliana
physiological function 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 Synechocystis sp.