Magnetic circular dichroic spectra of cobalt(II) substituted metalloenzymes.
Magnetic circular dichroic spectra of cobalt(II) substituted metalloenzymes.
复制标题
钴(II)取代的金属酶的磁性圆二向色光谱。
DOI:
10.1021/bi00678a016
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发表时间:
1975
期刊:
影响因子:
2.9
通讯作者:
B. Vallée
中科院分区:
文献类型:
--
作者:
B. Holmquist;T. Kaden;B. Vallée
The magnetic circular dichroic (MCD) spectra of cobalt(II) sugstituted metalloenzymes have been studied and compared to a series of four-, five-, and six-coordinate cobalt(II) model complexes previously examined (T. A. Kaden et al. (1974), Inorg. Chem. 13, 2582). The MCD spectra of cobalt substituted carboxypeptidase A, procarboxypeptidase ta, and thermolysin are consistent with earlier deductions of tetrahedral coordination from absorption spectra and also with X-ray structure analysis. Inhibitors fail to alter their MCD spectra significantly. The MCD spectra of cobalt alkaline phosphatase and carbonic anhydrase are more complex and their pH dependence and alteration by inhibitors are discussed in terms of known cobalt(II) models.