Population Inversion and Microwave-Stimulated Emission in the Electron Paramagnetic Resonance Spectrum of Ruby after Rapid Reversal of the Magnetic Field

1964 ◽  
Vol 12 (24) ◽  
pp. 667-670 ◽  
Author(s):  
L. Rimai ◽  
R. W. Bierig ◽  
B. D. Silverman
Keyword(s):  
Magnetic Field ◽  
Electron Paramagnetic Resonance ◽  
Electron Paramagnetic Resonance Spectrum ◽  
Population Inversion ◽  
Resonance Spectrum ◽  
Stimulated Emission ◽  
Paramagnetic Resonance ◽  
Rapid Reversal ◽  
Electron Paramagnetic ◽  
The Magnetic Field

The Electron Paramagnetic Resonance Spectrum of γ-Irradiated Dimethyl Malonic Acid

2004 ◽  
Vol 59 (1-2) ◽  
pp. 103-104 ◽  
Author(s):  
Biray Aşik ◽  
Mehmet Birey
Keyword(s):  
Magnetic Field ◽  
Electron Paramagnetic Resonance ◽  
Electron Paramagnetic Resonance Spectrum ◽  
Single Crystals ◽  
Malonic Acid ◽  
Hyperfine Coupling ◽  
Resonance Spectrum ◽  
Coupling Constants ◽  
Paramagnetic Resonance ◽  
Electron Paramagnetic

The electron paramagnetic resonance of γ -Irradiated single crystals of dimethyl malonic acid [(CH3)2C(COOH)2] has been studied for different orientations of the crystal in a magnetic field. The radicals produced by gamma irradiation have been investigated between 123 and 300 K. The spectra were found to be temperature independent, and radiation damage centres were attributed to [(CH3)2C(COOH)2]+ radicals. The g factor and hyperfine coupling constants were found to be almost isotropic with average values g = 2.0036, a(COOH)2 = 0.5 mT, a(CH3)2 = 2.1 mT, respectively, and spin density ρ = 91% of the [(CH3)2C(COOH)2]+ radical.

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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