A Selective Stepwise Heme Oxygenase Model System: An Iron(IV)-Oxo Porphyrin π‑Cation Radical Leads to a Verdoheme-Type Compound via an Isoporphyrin Intermediate

The selective oxidation of the α-position of two heme-FeIII tetraarylporphryinate complexes occurs when water(hydroxide) attacks their oxidized Cmpd I-type equivalents, high-valent FeIVO π-cation radical species ((P+•)FeIVO). Stepwise intermediate formation occurs, as detected by UV–vis spectrosco...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2013-11, Vol.135 (44), p.16248-16251
Main Authors: Garcia-Bosch, Isaac, Sharma, Savita K, Karlin, Kenneth D
Format: Article
Language:English
Subjects:
Cations - chemistry
Cations - metabolism
Free Radicals - chemistry
Free Radicals - metabolism
Heme - analogs & derivatives
Heme - chemistry
Heme - metabolism
Heme Oxygenase (Decyclizing) - chemistry
Heme Oxygenase (Decyclizing) - metabolism
Iron - chemistry
Iron - metabolism
Metalloporphyrins - chemistry
Metalloporphyrins - metabolism
Molecular Structure
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Summary:The selective oxidation of the α-position of two heme-FeIII tetraarylporphryinate complexes occurs when water(hydroxide) attacks their oxidized Cmpd I-type equivalents, high-valent FeIVO π-cation radical species ((P+•)FeIVO). Stepwise intermediate formation occurs, as detected by UV–vis spectroscopic monitoring or mass spectrometric interrogation, being iron(III) isoporphyrins, iron(III) benzoyl-biliverdins, and the final verdoheme-like products. Heme oxygenase (HO) enzymes could proceed through heterolytic cleavage of an iron(III)-hydroperoxo intermediate to form a transient Cmpd I-type species.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja405739m