In this paper, we have studied the interaction of CuZnSODⅢand Outer Copper, enzyme activity experiments expressed that 0.1mmol·L-1 Cu2+addition reduced the enzyme activity sharply, but this reduced action had no...In this paper, we have studied the interaction of CuZnSODⅢand Outer Copper, enzyme activity experiments expressed that 0.1mmol·L-1 Cu2+addition reduced the enzyme activity sharply, but this reduced action had not been found for the additions of 0.1mmol·L-1 1∶1 Cu2+and Zn2+, and 0.1mmol·L-1 Zn2+, respectively. This was due to the Cu2+exchanged the Zn2+in CuZnSODⅢ,and it was proved by the experiment of determination of metal content. Meanwhile, the static fluorescence quenching mechanism revealed the exist of molecular complex of CuZnSOD with Cu2+. The binding constant was obtained from lineweaver burk and double lg plot. The distance of active site to Trp is about 2.83nm, was calculated according to Frster theory.展开更多
文摘In this paper, we have studied the interaction of CuZnSODⅢand Outer Copper, enzyme activity experiments expressed that 0.1mmol·L-1 Cu2+addition reduced the enzyme activity sharply, but this reduced action had not been found for the additions of 0.1mmol·L-1 1∶1 Cu2+and Zn2+, and 0.1mmol·L-1 Zn2+, respectively. This was due to the Cu2+exchanged the Zn2+in CuZnSODⅢ,and it was proved by the experiment of determination of metal content. Meanwhile, the static fluorescence quenching mechanism revealed the exist of molecular complex of CuZnSOD with Cu2+. The binding constant was obtained from lineweaver burk and double lg plot. The distance of active site to Trp is about 2.83nm, was calculated according to Frster theory.
