scholarly journals Electron paramagnetic resonance determination of a low-lying excited state in Chromatium vinosum high-potential iron protein

1977 ◽  
Vol 20 (1) ◽  
pp. 23-31 ◽  
Author(s):  
H. Blum ◽  
J.C. Salerno ◽  
R.C. Prince ◽  
J.S. Leigh ◽  
T. Ohnishi
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Excited State ◽  
High Potential ◽  
Chromatium Vinosum ◽  
Paramagnetic Resonance ◽  
Iron Protein ◽  
Electron Paramagnetic

Determination of the Stoichiometry of the Adducts Formed between some Heterocyclic Bases and Copper(II) Bis(diethyldithiocarbamate) in Various Solvents

1973 ◽  
Vol 51 (10) ◽  
pp. 1530-1534 ◽  
Author(s):  
J. B. Farmer ◽  
F. G. Herring ◽  
R. L. Tapping
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Paramagnetic Resonance ◽  
Benzene Toluene ◽  
Heterocyclic Bases ◽  
Electron Paramagnetic

The stoichiometry of the adducts formed between copper(II) bis(diethyldithiocarbamate) and pyridine in benzene, toluene, and chloroform and between 3-picoline, 4-picoline, and 3,4-lutidine in benzene are shown to be 1:1. The method employed is that of Scatchard using electron paramagnetic resonance studies.

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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