Heme cleavage with remarkable ease: Paramagnetic intermediates formed by aerobic oxidation of a meso-amino-substituted iron porphyrin

Heather Kalish, Hon Man Lee, Marilyn M. Olmstead, Lechosław Latos-Grazyński, Sankar Prasad Rath, Alan L. Balch

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19 Citations (Scopus)


Hemes must be oxidatively stable to carry out their functions as biological oxidants, but introduction of a single amino group at a meso position of octaethylheme renders it extremely sensitive to ring opening by dioxygen. Exposure of a red pyridine (py) solution of diamagnetic (py)2FeII(H2N-OEP) (1) (H2N-OEP is the dianion of meso-amino-octaethylporphyrin) to air results in the immediate formation of a green intermediate which is subsequently converted into a second species that has been crystallized and characterized by X-ray diffraction. This process is distinct from coupled oxidation, a model for biological heme cleavage, because it does not require a sacrificial reducing agent to initiate the process.

Original languageEnglish
Pages (from-to)4674-4675
Number of pages2
JournalJournal of the American Chemical Society
Issue number16
Publication statusPublished - 2003 Apr 23


All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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