文献类型：期刊文章

作　　者：盛良全[1] 刘少民[2] 叶纪华[2] 徐小龙[1] 解永树[1] 刘清亮[1]

机构地区：[1]中国科学技术大学化学系,合肥230026 [2]中国科学技术大学食品系,合肥230052

出　　处：《无机化学学报》

年　　份：2003

卷　　号：19

期　　号：2

起止页码：191-195

语　　种：中文

收录情况：BDHX、BDHX2000、CAS、CSCD、CSCD2011_2012、IC、JST、RCCSE、RSC、SCIE、SCOPUS、WOS、ZGKJHX、核心刊

摘　　要：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 Frster theory.

关 键 词：烟草 相互作用 CuZnSODⅢ  荧光光谱 外源铜离子  超氧化物歧化酶

分 类 号：Q554.9] S572]