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A role for electron transfer in heme catabolism? Structure and redox behavior of an intermediate, (pyridine)2Fe(octaethyloxophlorin).
Autorzy
Rok wydania
1996
Czasopismo
Journal of the American Chemical Society
Numer woluminu
118
Strony
2760-2761
DOI
10.1021/ja953410+
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
Oxidative heme catabolism, either by heme oxygenase1orby the coupled oxidation procedure,2results in the removal ofa methine group from the iron porphyrin with the eventualrelease of carbon monoxide, iron, and biliverdin. Threemolecules of dioxygen are involved in the overall reaction. Itis widely believed that the process involves initial mesohydroxylation of the heme to form an iron oxophlorin (or ironmeso-hydroxyporphyrin) as an intermediate. A number ofhypothetical mechanistic schemes have been drawn to accountfor this process.1,2While many of these propose directcoordination of dioxygen to iron, few have been concerned withthe effects of other axial ligands, and none have given anyconsideration to the significance of outer-sphere electron transferreactions. Here we report the structural characterization of theiron complex, (pyridine)2Fe(octaethyloxophlorin), (py)2Fe-(OEPO),1,3a likely intermediate in coupled oxidation,2andits redox behavior which includes the discovery of a facile, one-electron oxidation.
Słowa kluczowe
Bioinorganic chemistry, Iron, Oxidation, Pyridines, Redox reactions
Adres publiczny
https://doi.org/10.1021/ja953410+
Strona internetowa wydawcy
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