Magnesium vs manganese cofactors for metallonuclease enzymes. A critical evaluation of thermodynamic binding parameters and stoichiometry
Magnesium vs manganese cofactors for metallonuclease enzymes. A critical evaluation of thermodynamic binding parameters and stoichiometry
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DOI：
10.1039/cc9960001813
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发表时间：
1996-08-07
影响因子：
4.9
通讯作者：
Cowan, JA
中科院分区：
文献类型：
--
作者：
Casareno, RLB;Cowan, JA
通过等温滴定量热法对 Mg2+ 与 Mn2+ 与大肠杆菌核糖核酸酶 H 和核酸外切酶 III 酶的结合进行实验分析，清楚地表明金属与核糖核酸酶 H 结合的化学计量为 1:1，但核酸外切酶 III 具有明显的金属依赖性行为，这表明在解释和概括有关晶体学和核酸外切酶的 Mg2+ 结合位点的位置和化学计量的结果时要谨慎。 Mn2+ 的机理实验。
An experimental analysis of Mg2+ vs, Mn2+ binding to Escherichia coli ribonuclease H and exonuclease III enzymes by isothermal titration calorimetry clearly demonstrates a 1:1 stoichiometry for metal binding to ribonuclease H, hut distinct metal-dependent behaviour for exonuclease III, suggesting caution in the interpretation and generalization of results concerning the location and stoichiometry of Mg2+ binding sites from crystallographic and mechanistic experiments with Mn2+.