American Chemical Society
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Model Studies for Heme Oxygenase-Catalyzed Porphyrin Meso Hydroxylation

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journal contribution
posted on 2007-03-29, 00:00 authored by Yaoqiu Zhu, Richard B. Silverman
Nonenzymatic model studies based on a porphyrin analogue (2,4-diacetyldeuteroporphyrin) that avoid the steric effect complications of the heme oxygenase active site were carried out to determine the polarity of the ferric hydroperoxide attacking species. Mass spectral and deuterium-labeling experiments indicate that the porphyrin meso positions that are at higher π-electron densities in ferric 2,4-diacetyldeuteroporphyrin are selectively attacked. This supports an electrophilic aromatic substitution mechanism for the heme oxygenase-catalyzed porphyrin meso hydroxylation.