| Numéro |
J. Phys. Colloques
Volume 47, Numéro C8, Décembre 1986
EXAFS and Near Edge Structure IV
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|---|---|---|
| Page(s) | C8-1137 - C8-1142 | |
| DOI | https://doi.org/10.1051/jphyscol:19868221 | |
J. Phys. Colloques 47 (1986) C8-1137-C8-1142
DOI: 10.1051/jphyscol:19868221
STRUCTURAL CHARACTERIZATION OF HIGH VALENT INTERMEDIATES IN HORSERADISH PEROXIDASE
J. E. PENNER-HAHN1, K. SMITH EBLE2, J.H. DAWSON2 et K.O. HODGSON31 Department of Chemistry, The University of Michigan, Ann Arbor, MI 48109-1055, U.S.A.
2 Department of Chemistry, The University of South Carolina, Columbia, SC 29208, U.S.A.
3 Department of Chemistry, Stanford University, Stanford, CA 94305, U.S.A.
Abstract
Extended X-ray absorption fine structure and X-ray absorption near edge structure spectroscopies have been utilized to determine the structural environment of the heme iron sites in horseradish peroxidase compounds I and II. For comparison, analogous studies have been undertaken on putative ferryl, Fe (IV) =0, porphyrin model compounds and on crystallographically characterized Cr (IV) =0 and Cr (V) =N porphyrins. The present work demonstrates unambiguously that a short, ca. 1.64 Å, Fe-O bond length is present both in HRP Compounds I and II and in their synthetic analogues. Edge spectra show the oxidation state of these high-valent species to be Fe (IV) or greater. These structures are consistent only with an oxoferryl (Fe=O) complex as the active oxygen species of horseradish peroxidase. The structural details and their implications for heme protein mediated oxygen activation are discussed.