Formation of the inhibitory complex of p-mercuribenzoate with xanthine oxidase, evaluation of hyperfine and quadrupole couplings of mercury to molybdenum(V) from the electron paramagnetic resonance spectrum, and structure of the complex

Biochemistry ◽  
1983 ◽  
Vol 22 (23) ◽  
pp. 5443-5452 ◽  
Author(s):  
Graham N. George ◽  
Robert C. Bray
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Electron Paramagnetic Resonance Spectrum ◽  
Xanthine Oxidase ◽  
Resonance Spectrum ◽  
Paramagnetic Resonance ◽  
Electron Paramagnetic

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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