Document Detail


Nitric oxide, a biological effector. Electron paramagnetic resonance detection of nitrosyl-iron-protein complexes in whole cells.
MedLine Citation:
PMID:  1657584     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Nitric oxide has been used for more than 20 years as an electron paramagnetic resonance probe of oxygen binding sites in oxygen-carriers and oxygen-metabolizing metalloenzymes. The high reactivity of NO with oxygen and the superoxide anion and its high affinity for metalloproteins led biochemists to consider NO as a highly toxic compound for a living cell. This assertion has recently been reconsidered following a number of discoveries of great significance: the finding of the activation of guanylate cyclase by NO, the recognition that NO is the precursor of nitrite and nitrate ions released in the activation of macrophages by endotoxin and cytokines, evidence that NO is an Endothelium-Derived Relaxing Factor, and the discovery of NO-biosynthesis from L-arginine, a pathway common in various biological cell-to-cell signalling processes. It is now admitted that NO plays a key bioregulatory role within mammalian cells, between cells of different types and in the host defence response. In the present review we have attempted to give a general picture of what is known of the chemical, physical, biochemical and biophysical properties of NO among the various nitrogen oxides. We have focussed on the structural information that can be obtained by electron paramagnetic resonance spectroscopy of nitrosyl-metalloprotein complexes. Finally we have shown how molecular targets of nitric oxide can be characterized, within whole cells, by electron paramagnetic resonance spectroscopy.
Authors:
Y Henry; C Ducrocq; J C Drapier; D Servent; C Pellat; A Guissani
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  European biophysics journal : EBJ     Volume:  20     ISSN:  0175-7571     ISO Abbreviation:  Eur. Biophys. J.     Publication Date:  1991  
Date Detail:
Created Date:  1991-11-25     Completed Date:  1991-11-25     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  8409413     Medline TA:  Eur Biophys J     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  1-15     Citation Subset:  IM    
Affiliation:
Institut Curie, Unité INSERM 219, Orsay, France.
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MeSH Terms
Descriptor/Qualifier:
Animals
Arginine / metabolism
Biophysical Phenomena
Biophysics
Electron Spin Resonance Spectroscopy
Humans
Iron / metabolism
Macrophages / metabolism
Metalloproteins / metabolism
Nitric Oxide / metabolism*
Nitroglycerin / metabolism
Chemical
Reg. No./Substance:
0/Metalloproteins; 10102-43-9/Nitric Oxide; 55-63-0/Nitroglycerin; 74-79-3/Arginine; 7439-89-6/Iron

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


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