Publication
Title
EPR analysis of cyanide complexes of wild-type human neuroglobin and mutants in comparison to horse heart myoglobin
Author
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.
Language
English
Source (journal)
Biophysical chemistry. - Amsterdam
Publication
Amsterdam : 2014
ISSN
0301-4622
Volume/pages
190(2014), p. 8-16
ISI
000337213500002
Full text (Publisher's DOI)
Full text (publisher's version - intranet only)
UAntwerpen
Faculty/Department
Research group
Publication type
Subject
Affiliation
Publications with a UAntwerp address
External links
Web of Science
Record
Identification
Creation 28.08.2014
Last edited 18.06.2017
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