A. Grinvald, R.D. Frostig, et al.
Physiological Reviews
We have measured the magnetic susceptibility in the temperature range 1.4-77°K of three derivatives of bovine superoxide dismutase in which Co2+ was substituted for Zn2+: (1) 2Co2+ - in which Co2+ binds to the normal Zn2+ site and the Cu2+ site is unoccupied, (2) 2Co2+2Cu2+ - in which the Zn2+ site is occupied by Co2+ and the copper sites contains Cu2+ and (3) 2Co2+2Cu+ - which is the reduced form of the second derivative. The 2Co2+ protein exhibits Curie paramagnetism indicating S′ = 1 2 and the zero-field splitting must be greater than {similar or greater-than}20 cm-1. The same propeties have been observed with the 2Co2+2Cu+-protein. By contrast, the 2Co2+2Cu2+-derivative exhibits relatively little paramagnetism, some of which arises from non-specifically associated metal ions. The lower susceptibility is due to antiferromagnetic coupling between Co2+ and Cu2+, and the magnitude of the coupling constant is probably ≫5 cm-1. © 1975.
A. Grinvald, R.D. Frostig, et al.
Physiological Reviews
Peter N. Ayittey, John S. Walker, et al.
Pflugers Archiv European Journal of Physiology
Adam Ertel, Aristotelis Tsirigos, et al.
Cell Cycle
Laxmi Parida, Pier F. Palamara, et al.
BMC Bioinformatics