DEPLETION AND REPLACEMENT OF PROTEIN METAL LIGANDS
DEPLETION AND REPLACEMENT OF PROTEIN METAL LIGANDS
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DOI：
10.1016/0958-1669(95)80070-0
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发表时间：
1995-08-01
影响因子：
7.7
通讯作者：
BARRICK, D
中科院分区：
文献类型：
--
作者：
BARRICK, D
最近，定点诱变已经以允许蛋白质配体的反式置换的方式应用于蛋白质衍生的金属配体。使用该方法可获得的配体的化学多样性远远超过使用标准诱变可获得的。非保守配体置换可以产生具有改变的配体结合、酶活性和光谱性质的新型金属蛋白。保守的配体取代，或“配体取代”，允许配体和蛋白质之间的共价键的结构和功能的影响进行评估;这种连接通常被认为在调节金属中心的结构和反应性中发挥关键作用。此外，这种方法可以用来研究分子识别的结构，热力学和动力学水平的细节。
Recently, site-directed mutagenesis has been applied to protein-derived metal ligands in a way that permits the replacement in trans of protein ligands. The chemical diversity of ligands available using this method far exceeds that attainable using standard mutagenesis. Non-conservative ligand replacement can yield novel metalloproteins with altered ligand-binding, enzymatic activities, and spectroscopic properties. Conservative ligand substitution, or 'ligand detachment', allows the structural and functional effects of the covalent linkage between the ligand and the protein to be evaluated; this linkage is often proposed to play a critical role in modulating the structure and reactivity of the metal center. Furthermore, this method can be exploited to study the details of molecular recognition at the structural, thermodynamic, and dynamic levels.