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J. Biol. Chem., Vol. 264, Issue 17, 9742-9744, Jun, 1989

Cyanide and azide behave in a similar fashion versus cuprozinc- superoxide dismutase

L Banci, I Bertini, C Luchinat and A Scozzafava
Department of Chemistry, University of Florence, Italy.

The 1H NMR spectra of the cyanide adduct of Cu2Co2-superoxide dismutase have been remeasured at pH 7.5. The exchange rate of CN- is slow on the NMR time scale. The correlation with the spectrum of the unligated enzyme has been established through saturation-transfer techniques of the system in which 50% of the cyanide adduct is formed and through comparison with the spectrum of a Cu2Co2-superoxide dismutase-CN- sample in which the histidines have been deuterium labeled at the position epsilon 1. The similarities between the spectra of the CN- and N-3 derivatives are stressed, in particular with respect to the removal from copper coordination of the same histidine, assigned as His-46.
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