Magnetic studies of the four-iron high-potential, non-heme protein from Chromatium vinosum.

Abstract

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 degrees 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.

Cite this paper

@article{Antanaitis1975MagneticSO, title={Magnetic studies of the four-iron high-potential, non-heme protein from Chromatium vinosum.}, author={B C Antanaitis and Thomas H. Moss}, journal={Biochimica et biophysica acta}, year={1975}, volume={405 2}, pages={262-79} }