Model studies for heme oxygenase-catalyzed porphyrin meso hydroxylation

Yaoqiu Zhu, Richard B. Silverman*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


Figure presented 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.

Original languageEnglish (US)
Pages (from-to)1195-1198
Number of pages4
JournalOrganic Letters
Issue number7
StatePublished - Mar 29 2007

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry


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