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Updated: Aug 15, 2026

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Published on: December 16, 2013
[Study on the interaction of copper-zinc superoxide dismutase with cobalt(II)-tryptophane by spectral analysis]
1Department of Bioengineering, Dalian University of Technology, Department of Chemistry and Chemical Engineering, Dalian University, Dalian.
Abstract:
The effect of changing the amount of external added Co(trp)n and pH values on the interaction of Cu2Zn2 SOD with organic metal compound (Cobalt(II)-Tryptophane) have been studied by means of ICP, VIS and measurement of enzyme activity. It has found that in aqueous solution, there exists a direct interaction of the metal ions of the active center in the metalloenzyme (Cu2Zn2 SOD) with external added Co(Trp)n. As a result, part of the metal ions in metalloenzyme were replaced and the corresponding metalloenzyme derivatives (Co(II)-substituted derivatives of SOD) were produced and the catalytic activity of enzyme were affected. It has also studied the intensity of interactions in different molar ratios (Cobalt(II)-Tryptophane) and pH values and got some results under the effect of corresponding factors.
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