锌（II）与脱辅基（牛红细胞超氧化物歧化酶）的结合
Zinc(II) binding to apo-(bovine erythrocyte superoxide dismutase).
作者信息
Cass A E, Hill H A, Bannister J V, Bannister W H
出版信息
Biochem J. 1979 Feb 1;177(2):477-86. doi: 10.1042/bj1770477.
Abstract
The binding of zinc(II) ions to apo-(bovine erythrocytes superoxide dismutase) was studied by 1H n.m.r. spectroscopy. Two zinc(II) ions bind to each subunit of the apoenzyme, and the first has a binding constant at least an order of magnitude larger than the second. The nature of the spectral changes that occur on binding the first zinc(II) ion are interpreted in terms of a change in the structure of the protein around the active site to one very similar to that of the holoenzyme, thus pre-forming the second zinc(II) binding site. The binding of the second zinc(II) ion effects changes in the environment of only those residues involved in its co-ordination.
摘要
通过核磁共振氢谱研究了锌（II）离子与脱辅基（牛红细胞超氧化物歧化酶）的结合。两个锌（II）离子与脱辅基酶的每个亚基结合，第一个锌（II）离子的结合常数比第二个至少大一个数量级。结合第一个锌（II）离子时发生的光谱变化的性质，被解释为活性位点周围蛋白质结构向与全酶非常相似的结构转变，从而预先形成第二个锌（II）结合位点。第二个锌（II）离子的结合仅影响参与其配位的那些残基环境的变化。
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本文引用的文献
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