Identifying residues that cause pH-dependent reduction potentials.
Identifying residues that cause pH-dependent reduction potentials.
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识别导致 pH 依赖性还原电位的残留物。
DOI：
10.1021/bi4002858
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发表时间：
2013
期刊：
影响因子：
2.9
通讯作者：
Ichiye,Toshiko
中科院分区：
文献类型：
--
作者：
PerrinJr,BScott;Ichiye,Toshiko
金属蛋白还原电位的pH依赖性表明，氧化还原位点附近至少一个残基的质子化状态发生了变化，这可能对其活性很重要。负责的残基通常通过位点特异性诱变来识别，这可能是耗时的。本文利用密度泛函理论和泊松-玻尔兹曼计算预测，如果只有唯一的组氨酸发生质子化变化，那么chromatium vinosum高电位铁硫蛋白的e°滴定值与实验结果很好地吻合。在一个用户友好的基于web的门户网站CHARMMing中实施这种方法，允许用户识别其他蛋白质中引起类似pH依赖的残基。
The pH dependence of the reduction potentialE° for a metalloprotein indicates that the protonation state of at least one residue near the redox site changes and may be important for its activity. The responsible residue is usually identified by site-specific mutagenesis, which may be time-consuming. Here, the titration ofE° forChromatium vinosumhigh-potential iron–sulfur protein is predicted to be in good agreement with experiment using density functional theory and Poisson–Boltzmann calculations if only the sole histidine undergoes changes in protonation. The implementation of this approach into CHARMMing, a user-friendly web-based portal, allows users to identify residues in other proteins causing similar pH dependence.