Title
EPR analysis of cyanide complexes of wild-type human neuroglobin and mutants in comparison to horse heart myoglobin
Author
Faculty/Department
Faculty of Sciences. Physics
Faculty of Pharmaceutical, Biomedical and Veterinary Sciences . Biomedical Sciences
Publication type
article
Publication
Amsterdam ,
Subject
Physics
Chemistry
Biology
Source (journal)
Biophysical chemistry. - Amsterdam
Volume/pages
190(2014) , p. 8-16
ISSN
0301-4622
ISI
000337213500002
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
Electron paramagnetic resonance (EPR) data reveal large differences between the ferric (C-13-)cyanide complexes of wild-type human neuroglobin (NGB) and its H64Q and F28L point mutants and the cyanide complexes of mammalian myo- and haemoglobin. The point mutations, which involve residues comprising the distal haem pocket in NGB, induce smaller, but still significant changes, related to changes in the stabilization of the cyanide ligand. Furthermore, for the first time, the full C-13 hyperfine tensor of the cyanide carbon of cyanide-ligated horse heart myoglobin (hhMb) was determined using Davies ENDOR (electron nuclear double resonance). Disagreement of these experimental data with earlier predictions based on C-13 NMR data and a theoretical model reveal significant flaws in the model assumptions. The same ENDOR procedure allowed also partial determination of the corresponding C-13 hyperfine tensor of cyanide-ligated NGB and H64QNGB. These C-13 parameters differ significantly from those of cyanide-ligated hhMb and challenge our current theoretical understanding of how the haem environment influences the magnetic parameters obtained by EPR and NMR in cyanide-ligated haem proteins. (C) 2014 Elsevier B.V. All rights reserved.
E-info
https://repository.uantwerpen.be/docman/iruaauth/7e5f79/b997856.pdf
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