EPR analysis of cyanide complexes of wild-type human neuroglobin and mutants in comparison to horse heart myoglobin

Van Doorslaer, Sabine, Trandafir, Florin, Harmer, Jeffrey R., Moens, Luc and Dewilde, Sylvia (2014) EPR analysis of cyanide complexes of wild-type human neuroglobin and mutants in comparison to horse heart myoglobin. Biophysical Chemistry, 190-191 8-16. doi:10.1016/j.bpc.2014.03.007

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Author Van Doorslaer, Sabine
Trandafir, Florin
Harmer, Jeffrey R.
Moens, Luc
Dewilde, Sylvia
Title EPR analysis of cyanide complexes of wild-type human neuroglobin and mutants in comparison to horse heart myoglobin
Journal name Biophysical Chemistry   Check publisher's open access policy
ISSN 1873-4200
0301-4622
Publication date 2014-06
Year available 2014
Sub-type Article (original research)
DOI 10.1016/j.bpc.2014.03.007
Open Access Status
Volume 190-191
Start page 8
End page 16
Total pages 9
Place of publication Amsterdam, Netherlands
Publisher Elsevier
Collection year 2015
Language eng
Formatted abstract
Electron paramagnetic resonance (EPR) data reveal large differences between the ferric (13C-)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 13C 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 13C NMR data and a theoretical model reveal significant flaws in the model assumptions. The same ENDOR procedure allowed also partial determination of the corresponding 13C hyperfine tensor of cyanide-ligated NGB and H64QNGB. These 13C 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.
Keyword Neuroglobin
Electron paramagnetic resonance
Cyanide binding
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
Centre for Advanced Imaging Publications
 
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