Spencer P, Slade A, Atkinson T, Gore M G
Department of Biochemistry, University of Southampton, U.K.
Biochim Biophys Acta. 1990 Aug 1;1040(1):130-3. doi: 10.1016/0167-4838(90)90156-a.
The interactions of the essential divalent cation, Zn2+, with the binary complex formed between glycerol dehydrogenase (glycerol:NAD+ 2-oxidoreductase, EC 1.1.1.6) and its coenzyme NADH have been examined by fluorescence spectroscopy. Both the metallo and non-metallo form of the enzyme bind the coenzyme NADH. The addition of Zn2+ ions to a solution of the binary complex formed between metal-depleted enzyme and NADH results in a rapid increase in fluorescence emission at 430 nm. This has been used to determine the on rate for Zn2+ to the enzyme/binary complex. A dissociation constant of 3.02 +/- 0.25.10(-9) M for the equilibrium between Zn2+ ions and the enzyme has been determined.
通过荧光光谱法研究了必需二价阳离子Zn2+与甘油脱氢酶（甘油：NAD+ 2-氧化还原酶，EC 1.1.1.6）及其辅酶NADH形成的二元复合物之间的相互作用。该酶的金属形式和非金属形式均能结合辅酶NADH。向金属耗尽的酶与NADH形成的二元复合物溶液中加入Zn2+离子，会导致430nm处的荧光发射迅速增加。这已被用于确定Zn2+与酶/二元复合物的结合速率。已确定Zn2+离子与该酶之间平衡的解离常数为3.02±0.25×10−9M。
