Please use this identifier to cite or link to this item:
|Title:||Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase|
|Authors:||Casadei, Cecilia M.|
Metcalfe, Clive L.
Murphy, Emma J.
Concilio, Maria Grazia
Teixeira, Susana C. M.
Schrader, Tobias E.
Fielding, Alistair J.
Blakeley, Matthew P.
Raven, Emma L.
Moody, Peter C. E.
|Publisher:||American Association for the Advancement of Science|
|Citation:||Science, 2014, 345 (6193), pp. 193-197|
|Abstract:||Heme enzymes activate oxygen through formation of transient iron-oxo (ferryl) intermediates of the heme iron. A long-standing question has been the nature of the iron-oxygen bond and, in particular, the protonation state. We present neutron structures of the ferric derivative of cytochrome c peroxidase and its ferryl intermediate; these allow direct visualization of protonation states. We demonstrate that the ferryl heme is an Fe(IV)=O species and is not protonated. Comparison of the structures shows that the distal histidine becomes protonated on formation of the ferryl intermediate, which has implications for the understanding of O-O bond cleavage in heme enzymes. The structures highlight the advantages of neutron cryo-crystallography in probing reaction mechanisms and visualizing protonation states in enzyme intermediates.|
|Rights:||Copyright © 2014, American Association for the Advancement of Science. Deposited with reference to the publisher’s open access archiving policy.|
|Description:||This is the author’s version of the work. It is posted here by permission of the AAAS for personal use, not for redistribution. The definitive version was published in Science Magazine on 345(6193), DOI: 10.1126/science.1254398|
|Appears in Collections:||Published Articles, Dept. of Chemistry|
Files in This Item:
|Casadei et al open access pdf file.pdf||Post-review (final submitted)||66.69 MB||Adobe PDF||View/Open|
Items in LRA are protected by copyright, with all rights reserved, unless otherwise indicated.