Abstract
High resolution nuclear magnetic resonance (n.m.r.) spectroscopy of the copper-zinc superoxide dismutase from Saccharomyces cerevisiae has revealed a substantial structural homology with the bovine enzyme. N.m.r. spectra of the apo enzyme and the holo-reduced and holo-oxidized enzymes are reported and assignments are made to the histidines in the active site and the single tyrosine residue. All the assignments are in agreement with the known amino-acid sequence and the geometry of the active site is virtually unchanged. Addition of halide ions to the reduced holo enzyme results in the perturbation of the chemical shift of three histidine C2 protons and the degree of perturbation is Cl−∼Br−>I−>F− for 1m solutions of the anions. The enzyme has also been shown to retain its structure at 75°C.
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