Document Detail


Paramagnetic NMR shifts in cyanoferricytochrome c. Investigation of thermal stability and deviations from Curie law behaviour.
MedLine Citation:
PMID:  9366264     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The paramagnetic shifts of 13C nuclei positioned alpha to the haem in cyanoferricytochrome c are reported and analysed in terms of molecular orbitals based on D4h symmetry with a rhombic perturbation. The temperature dependence of the Fermi contact and dipolar shifts of the haem and axial histidine ligand show deviations from Curie Law behaviour which are explained by a Boltzmann distribution between partially filled 3e(pi) molecular orbitals and the ground and first excited state Kramers doublets. The comprehensive explanation of the temperature dependence of the paramagnetic shifts leads to the conclusion that there is no detectable temperature dependence of the haem orientation or that of the His ligand orientation. This work also provides evidence for the role of the axial His ligand in determining the orientation of the magnetic z-axis.
Authors:
L Brennan; D L Turner
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1342     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1997 Sep 
Date Detail:
Created Date:  1997-12-08     Completed Date:  1997-12-08     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  1-12     Citation Subset:  IM    
Affiliation:
Department of Chemistry, University of Southampton, UK.
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MeSH Terms
Descriptor/Qualifier:
Cytochrome c Group / chemistry*
Cytochromes c*
Drug Stability
Electron Spin Resonance Spectroscopy
Heme
Kinetics
Models, Chemical*
Nuclear Magnetic Resonance, Biomolecular / methods
Thermodynamics
Chemical
Reg. No./Substance:
0/Cytochrome c Group; 0/cyanoferricytochrome C; 14875-96-8/Heme; 9007-43-6/Cytochromes c

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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