Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme

The nature of the ferryl intermediate generated in reactions catalysed by heme-containing enzymes is uncertain, due to the ambiguity of X-ray crystallography data. Here, the authors apply neutron diffraction, kinetics and other spectroscopy to directly observe a protonated ferryl intermediate in a h...

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Main Authors: Hanna Kwon, Jaswir Basran, Cecilia M. Casadei, Alistair J. Fielding, Tobias E. Schrader, Andreas Ostermann, Juliette M. Devos, Pierre Aller, Matthew P. Blakeley, Peter C. E. Moody, Emma L. Raven
Format: Article
Language:English
Published: Nature Publishing Group 2016-11-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms13445
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spelling doaj-ba0cf1877308498b991c38c8062c04312021-05-11T10:56:03ZengNature Publishing GroupNature Communications2041-17232016-11-01711610.1038/ncomms13445Direct visualization of a Fe(IV)–OH intermediate in a heme enzymeHanna Kwon0Jaswir Basran1Cecilia M. Casadei2Alistair J. Fielding3Tobias E. Schrader4Andreas Ostermann5Juliette M. Devos6Pierre Aller7Matthew P. Blakeley8Peter C. E. Moody9Emma L. Raven10Department of Molecular and Cell Biology and Leicester Institute of Structural and Chemical Biology, University of LeicesterDepartment of Molecular and Cell Biology and Leicester Institute of Structural and Chemical Biology, University of LeicesterDepartment of Molecular and Cell Biology and Leicester Institute of Structural and Chemical Biology, University of LeicesterThe Photon Science Institute and School of Chemistry, The University of ManchesterJülich Centre for Neutron Science (JCNS) at Heinz Maier-Leibnitz Zentrum (MLZ), Forschungszentrum Jülich GmbHHeinz Maier-Leibnitz Zentrum (MLZ), Technische Universität MünchenInstitut Laue-LangevinDiamond Light Source Ltd, Diamond House, Harwell Science and Innovation CampusInstitut Laue-LangevinDepartment of Molecular and Cell Biology and Leicester Institute of Structural and Chemical Biology, University of LeicesterDepartment of Chemistry and Leicester Institute of Structural and Chemical Biology, University of LeicesterThe nature of the ferryl intermediate generated in reactions catalysed by heme-containing enzymes is uncertain, due to the ambiguity of X-ray crystallography data. Here, the authors apply neutron diffraction, kinetics and other spectroscopy to directly observe a protonated ferryl intermediate in a heme peroxidase.https://doi.org/10.1038/ncomms13445
collection DOAJ
language English
format Article
sources DOAJ
author Hanna Kwon
Jaswir Basran
Cecilia M. Casadei
Alistair J. Fielding
Tobias E. Schrader
Andreas Ostermann
Juliette M. Devos
Pierre Aller
Matthew P. Blakeley
Peter C. E. Moody
Emma L. Raven
spellingShingle Hanna Kwon
Jaswir Basran
Cecilia M. Casadei
Alistair J. Fielding
Tobias E. Schrader
Andreas Ostermann
Juliette M. Devos
Pierre Aller
Matthew P. Blakeley
Peter C. E. Moody
Emma L. Raven
Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme
Nature Communications
author_facet Hanna Kwon
Jaswir Basran
Cecilia M. Casadei
Alistair J. Fielding
Tobias E. Schrader
Andreas Ostermann
Juliette M. Devos
Pierre Aller
Matthew P. Blakeley
Peter C. E. Moody
Emma L. Raven
author_sort Hanna Kwon
title Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme
title_short Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme
title_full Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme
title_fullStr Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme
title_full_unstemmed Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme
title_sort direct visualization of a fe(iv)–oh intermediate in a heme enzyme
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2016-11-01
description The nature of the ferryl intermediate generated in reactions catalysed by heme-containing enzymes is uncertain, due to the ambiguity of X-ray crystallography data. Here, the authors apply neutron diffraction, kinetics and other spectroscopy to directly observe a protonated ferryl intermediate in a heme peroxidase.
url https://doi.org/10.1038/ncomms13445
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