Line-Intensity Angular Dependence in Paramagnetic-Resonance Spectrum ofS-State Ions with Axial Crystalline Environments

1973 ◽  
Vol 7 (9) ◽  
pp. 4061-4064 ◽  
Author(s):  
P. Mialhe ◽  
A. Erbeia
1978 ◽  
Vol 175 (3) ◽  
pp. 955-957 ◽  
Author(s):  
D J Lowe

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.


The gas-phase paramagnetic resonance spectrum of NF in the J = 2 rotational level of the 1 ∆ state has been studied, and the dipole moment in this state is found to be 0.37 ± 0.60D. The rotational constant previously determined from the electronic spectrum is shown to be consistent with the electron resonance results, and the 14 N quadrupole coupling constant e 2 qQ is 4.1 ± 0.2 MHz. The hyperfine coupling constants of the 14 N and 19 F nuclei are + 109.92 ± 0.14 and +758.06 ± 0.23 MHz respectively.


1959 ◽  
Vol 38 (1) ◽  
pp. 291-296 ◽  
Author(s):  
J. E. Geusic ◽  
Martin Peter ◽  
E. O. Schulz-Du Bois

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