Characterization of the properties of the multiple metal binding sites in alkaline phosphatase by carbon-13 nuclear magnetic resonance.
Characterization of the properties of the multiple metal binding sites in alkaline phosphatase by carbon-13 nuclear magnetic resonance.
复制标题
通过碳 13 核磁共振表征碱性磷酸酶中多个金属结合位点的特性。
DOI：
10.1021/bi00558a020
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发表时间：
1980
期刊：
影响因子：
2.9
通讯作者：
Armitage,IM
中科院分区：
文献类型：
--
作者：
Otvos,JD;Armitage,IM
James D. Otvos** and Ian M. Armitage* abstract: Carbon-13 nuclear magnetic resonance(13C NMR) of Escherichia coli alkaline phosphatase labeled biosynthetically with ß, ß-[-13C] dideuteriohistidine has been used to determine the number and identity of the histidine residues that participate in metalion coordination at the three classes of binding sites in this dimeric Zn2+ metalloenzyme. Detailed 13C NMR titrations of the apoenzyme with U3Cd2+ and Mg2+, in conjunction with parallel 113Cd NMR mea-surements [Otvos, J. D., & Armitage, I. M.(1980) Biochemistry (thirdof three papers in this issue)], permitted the assignment of four histidine residues as ligands to the “catalytic”, or A site, metal ions, two coordinated via their NT imidazole nitrogens and two via Nr. In addition, a fifth histidyl ligand, coordinated through NT, was shown to be located at the “structural”, or B, sites on the dimer. The “regulatory”, or C, sites do not containhistidyl metal ligands.
