The electron paramagnetic resonance spectrum of S3N2+

1984 ◽  
Vol 62 (6) ◽  
pp. 1124-1126 ◽  
Author(s):  
Shirley A. Fairhurst ◽  
Keith F. Preston ◽  
Leslie H. Sutcliffe
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Electron Paramagnetic Resonance Spectrum ◽  
Radical Cation ◽  
Ground State ◽  
Resonance Spectrum ◽  
Nitrogen Compounds ◽  
Epr Spectrum ◽  
Paramagnetic Resonance ◽  
Electron Paramagnetic

The epr spectrum of a persistent sulfur nitride radical cation, common to the oxidation of many sulphur–nitrogen compounds, has been obtained from materials highly enriched in both 15N and 33S. Analyses of solution and frozen spectra show that the carrier is planar S3N2+ and that its ground state is 2A2 in C2v. symmetry.

scholarly journals Sensing the framework state and guest molecules in MIL-53(Al) via the electron paramagnetic resonance spectrum of VIV dopant ions

2017 ◽  
Vol 19 (36) ◽  
pp. 24545-24554 ◽  
Author(s):  
Irena Nevjestić ◽  
Hannes Depauw ◽  
Peter Gast ◽  
Pieter Tack ◽  
Davy Deduytsche ◽  
...  
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Electron Paramagnetic Resonance Spectrum ◽  
Resonance Spectrum ◽  
Epr Spectrum ◽  
Paramagnetic Resonance ◽  
Guest Molecules ◽  
Oxygen Gas ◽  
Electron Paramagnetic

The EPR spectrum of VIV dopant ions was used to discriminate different states of MIL-53(Al) and to detect oxygen gas.

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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