scholarly journals Highly resolved electron paramagnetic resonance spectrum of copper(II) ion pairs in CuCe oxide

1992 ◽  
Vol 88 (4) ◽  
pp. 615-620 ◽  
Author(s):  
Antoine Aboukaïs ◽  
Abdelrhani Bennani ◽  
Cossi Faustin Aïssi ◽  
Geneviève Wrobel ◽  
Michel Guelton ◽  
...  
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Electron Paramagnetic Resonance Spectrum ◽  
Resonance Spectrum ◽  
Ion Pairs ◽  
Paramagnetic Resonance ◽  
Electron Paramagnetic

The Electron Paramagnetic Resonance Spectrum of the Phenalane Anion

1972 ◽  
Vol 50 (10) ◽  
pp. 1523-1528 ◽  
Author(s):  
D. H. Paskovich ◽  
A. H. Reddoch
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Electron Paramagnetic Resonance Spectrum ◽  
Alkali Metals ◽  
Room Temperature ◽  
Resonance Spectrum ◽  
Ion Pairs ◽  
Coupling Constants ◽  
Paramagnetic Resonance ◽  
Conformational Interconversion ◽  
Electron Paramagnetic

The phenalane anion has been prepared by the reaction of alkali metals in ether solutions of both phenalane and phenalene. The electron paramagnetic resonance spectra of both the radical and of its ion pairs with sodium and with lithium in THF are reported. At room temperature there is an alternating linewidth involving the β protons caused by conformational interconversion of the axial and equatorial positions. At −80 °C the γ protons are not equivalent and the corresponding coupling constants are resolved.

scholarly journals Simulation of the electron-paramagnetic-resonance spectrum of the iron-protein of nitrogenase. A prediction of the existence of a second paramagnetic centre

1978 ◽  
Vol 175 (3) ◽  
pp. 955-957 ◽  
Author(s):  
D J Lowe
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Electron Paramagnetic Resonance Spectrum ◽  
Complex Formation ◽  
Resonance Spectrum ◽  
The Other ◽  
Paramagnetic Centre ◽  
Paramagnetic Resonance ◽  
Iron Protein ◽  
Integrated Intensities ◽  
Electron Paramagnetic

The e.p.r. spectra of the Fe-proteins of nitrogenase from all sources studied have unusual features in that they have very anisotropic linewidths and low integrated intensities. These characteristics can be explained by assuming that one of the two electrons accepted by these proteins is located at a rapidly relaxing paramagnetic centre that is unobservable by e.p.r., but causes anisotropic broadening of the e.p.r. signal of the other electron. Complex-formation between Fe-proteins and MgATP is described in terms of a 50-60 degrees rotation of the e.p.r.-observable centre.

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