J.F. Ziegler
Nuclear Instruments and Methods
Extensive EPR studies on high-potential, iron-sulfur protein from Chromatium vinosum indicate that the singular spectrum of this four-iron, non-heme protein consists of a superposition of three distinct signals; namely, two principal signals of equal weight, one reflecting axial and the other rhombic symmetry, and a third nearly isotropic minority component. In addition, magnetic susceptibility experiments on two oxidation states of the protein from 4.2 to approx. 260 °K indicate antiferromagnetic exchange coupling between iron atoms. Possible origins of the complex EPR signals are discussed, and a preferred model that is consistent with EPR, magnetic susceptibility, NMR, X-ray, and Mössbauer data is presented. © 1975.
J.F. Ziegler
Nuclear Instruments and Methods
M. Pitman, W.K. Huber, et al.
J. Comput. Aided Mol. Des.
Jacqueline S. Dron, Minxian Wang, et al.
Circulation: Genomic and Precision Medicine
F. James Rohlf
Mathematical Biosciences