Superoxide dismutase nuclear magnetic resonance

Cass, A. E. G., Hill, H. A. O. Anion binding to copper(I) superoxide dismutase A high resolution H nuclear magnetic resonance spectroscopic study. In Chemical and Biochemical Aspects of Superoxide and Superoxide Dismutase (Bannister, J. V., Hill, H. A, O., eds.). New York-Amsterdam-Oxford, Elsevier/North-Holland, 1980, pp. 290-298... 

Two rather unusual assays have been developed for superoxide dismutase. Both these assays do not reflect the catalytic activity of the enzyme. The first assay utilizes the unique effect of the metal centers on the relaxation rate of F nucleus of fluoride which can be monitored by nuclear magnetic resonance, whereas the second assay is based on the antigenicity of the proteins. 

Cadmium-113 nuclear magnetic resonance studies of the cadmium substituted bovine superoxide dismutase were carried out Only a very small chemical-shift difference between the 2 Cd(Il) protein (Cd(II) is bound to the zinc site and the copper site is unoccupied) and the 2 Cd(ll)—2 Cu(I) enzyme (analogous to the reduced form of the native protein) was found. This was interpreted in that the imidazolate bridge is protonated at the Cu site after reduction. 

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