Spectral properties of Co(II)- and Ni(II)-activated rabbit muscle pyruvate kinase.
Spectral properties of Co(II)- and Ni(II)-activated rabbit muscle pyruvate kinase.
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Co(II) 和 Ni(II) 激活的兔肌肉丙酮酸激酶的光谱特性。
DOI:
10.1016/s0021-9258(19)41143-5
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发表时间:
1975
期刊:
影响因子:
--
通讯作者:
R. Davis
中科院分区:
文献类型:
--
作者:
C. Kwan;K. Erhard;R. Davis
Stoichiometry, kinetics, and optical properties of rabbit muscle pyruvate kinase activated with Co(II), Ni(II), Mg(II), and Mn(II) were studied. The stoichiometry of metal binding to enzyme was found to be 4 metal ions per tetrameric enzyme for Co(II) and Ni(II) by carrying out circular dichroic titrations. Cu(II) and Fe(II) were inactive. Ca(II) and Zn(II) were not activating, and were inhibitory with respect to all of the active cations. The temperature dependence of the optimal velocity is similar for all activating metals. The pH rate profiles suggest that there are two classes of enzyme activation by metal ions. Mg(II) and Mn(II) are quite similar to each other while Co(II) and Ni(II) are different from them but similar to each other. Absorption, natural, and magnetic CD in the visible region were used to probe the environment of the activating divalent cation in Ni(II)- and Co(II)-activated pyruvate kinase and their complexes with substrates and inhibitors...