Delocalization over the heme and the axial ligands of one of the two oxidizing equivalents stored above the ferric state in the peroxidase and catalase Compound-I intermediates: Indirect participation of the proximal axial ligand of iron in the oxidation reactions catalyzed by heme-based peroxidases and catalases?

Raymond Weiss*, Dominique Mandon, Thomas Wolter, Alfred X. Trautwein, Markus Müther, Eckhard Bill, Avram Gold, Karupiah Jayaraj, James Terner

*Corresponding author for this work
60 Citations (Scopus)

Abstract

A comparison of the exchange interactions arising in the peroxidase and catalase Compound I intermediates and their iron(IV)-oxo porphyrin π-cation radical models, both of which are two oxidizing equivalents above the ferric state, suggests that in the models the oxidizing equivalent is localized on the porphyrin ring, while in the proteins it is partly delocalized onto the proximal ligand. Thus, the proximal axial ligand of iron participates indirectly in the oxidation reactions catalyzed by the enzymes. Possible roles of the axial ligand in the catalytic mechanism of these heme-based enzymes are discussed.

Original languageEnglish
JournalJournal of Biological Inorganic Chemistry
Volume1
Issue number4
Pages (from-to)377-383
Number of pages7
ISSN0949-8257
DOIs
Publication statusPublished - 01.08.1996

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