酶催化中质子转移的方向性特征。
Directional character of proton transfer in enzyme catalysis.
作者信息
Wang J H
出版信息
Proc Natl Acad Sci U S A. 1970 Jul;66(3):874-81. doi: 10.1073/pnas.66.3.874.
Abstract
Hydrogen bonding can facilitate proton transfer in certain directions and retard proton transfer in certain other directions. By assuming that directed proton transfer along strategically oriented hydrogen bonds in the enzyme-substrate complex plays an important role in determining the efficiency and specificity of the enzyme, we present a unified interpretation for the reported observations on carbonic anhydrase and alpha-chymotrypsin.
摘要
氢键可以促进质子在某些方向上的转移，而在其他某些方向上阻碍质子转移。通过假设沿着酶 - 底物复合物中策略性定向的氢键进行的定向质子转移在决定酶的效率和特异性方面起着重要作用，我们对已报道的关于碳酸酐酶和α - 胰凝乳蛋白酶的观察结果提出了一种统一的解释。
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2
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3
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4
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