期刊
MOLECULES
卷 28, 期 2, 页码 -出版社
MDPI
DOI: 10.3390/molecules28020832
关键词
cytochrome; ion tethering; equilibrium binding; molecular dynamics
We investigated the impact of structural dynamic conformational behavior on the catalytic activity of Cytochrome P450 OleP. By combining equilibrium-binding experiments and all-atom molecular dynamics simulations, we found that the closed-catalytic competent-form is favored under high-ionic strength conditions. Interestingly, different mechanisms can be used to explain this effect, depending on the chemistry of the cations.
Cytochrome P450 OleP catalytic activity is strongly influenced by its structural dynamic conformational behavior. Here, we combine equilibrium-binding experiments with all-atom molecular dynamics simulations to clarify how different environments affect OleP conformational equilibrium between the open and the closed-catalytic competent-forms. Our data clearly show that at high-ionic strength conditions, the closed form is favored, and, very interestingly, different mechanisms, depending on the chemistry of the cations, can be used to rationalize such an effect.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据