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生物物理学报 1996
THE ACTIVE CHANNEL OF COPPER ZINC SUPEROXIDE DISMUTASE IN DENATURATION
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Abstract:
For the guanidine hydrochloride denaturation and thermal denaturation of copper zinc superoxide dismutase, electron transfer reaction and ESR methods were tried to be used to detect the conformational changes of the active site of the enzyme. From the changes of activity and conformation of the enzyme, it is concluded that the con formation of the active channel change first prior to that of the molecule as a whole. The conformational changes of the active channel occurs with inactivation simultanously.Although metal ions keep the higher stability of the active site, the active channel of copper zinc superoxide dismutase is raletive fragile.