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Title: Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme
Authors: Kwon, Hanna
Basran, Jaswir
Casadei, Cecilia M.
Fielding, A. J.
Schrader, T. E.
Ostermann, A.
Devos, J. M.
Aller, P.
Blakeley, M. P.
Moody, Peter C. E.
Raven, Emma L.
First Published: 29-Nov-2016
Publisher: Nature Publishing Group
Citation: Nature Communications, 2016 7:13445
Abstract: Catalytic heme enzymes carry out a wide range of oxidations in biology. They have in common a mechanism that requires formation of highly oxidized ferryl intermediates. It is these ferryl intermediates that provide the catalytic engine to drive the biological activity. Unravelling the nature of the ferryl species is of fundamental and widespread importance. The essential question is whether the ferryl is best described as a Fe(IV)=O or a Fe(IV)–OH species, but previous spectroscopic and X-ray crystallographic studies have not been able to unambiguously differentiate between the two species. Here we use a different approach. We report a neutron crystal structure of the ferryl intermediate in Compound II of a heme peroxidase; the structure allows the protonation states of the ferryl heme to be directly observed. This, together with pre-steady state kinetic analyses, electron paramagnetic resonance spectroscopy and single crystal X-ray fluorescence, identifies a Fe(IV)–OH species as the reactive intermediate. The structure establishes a precedent for the formation of Fe(IV)–OH in a peroxidase.
DOI Link: 10.1038/ncomms13445
eISSN: 2041-1723
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit
Description: The authors declare that the data supporting the findings of this study are available within the article and its Supplementary Information. Atomic coordinates and diffraction data have been deposited in the Protein Data Bank (accession codes 5JPR and 5JQR).
Appears in Collections:Published Articles, Dept. of Chemistry

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