柔性趋化酶的扩散和稳态分布
Diffusion and steady state distributions of flexible chemotactic enzymes
摘要：
近年来的许多实验报道，当暴露于其相应的底物时，催化酶经历增强的扩散以及趋化性（在底物梯度方向上的偏置运动）。在其他可能的机制中，在最近的一些工作中，我们已经探索了几种增强扩散和趋化性的被动机制，在这个意义上，它们只需要酶与底物的结合和解结合，而不是催化反应本身。这些机制依赖于由于结合引起的酶的构象变化，以及由于酶和底物之间的非接触相互作用引起的电泳。在这里，在回顾和概括我们以前的发现之后，我们以两种不同的方式扩展它们。在增强扩散的情况下，我们表明，酶的长时间扩散系数的精确结果可以得到使用广义泰勒色散理论，这导致更简单和透明的解析表达式的扩散增强。在趋化性的情况下，我们表明，在非平凡的稳态分布的酶，它可以积累或耗尽从特定的底物浓度的区域中的电泳和结合诱导的变化之间的竞争扩散的结果。
英文摘要：
Many experiments in recent years have reported that, when exposed to their corresponding substrate, catalytic enzymes undergo enhanced diffusion as well as chemotaxis (biased motion in the direction of a substrate gradient). Among other possible mechanisms, in a number of recent works we have explored several passive mechanisms for enhanced diffusion and chemotaxis, in the sense that they require only binding and unbinding of the enzyme to the substrate rather than the catalytic reaction itself. These mechanisms rely on conformational changes of the enzyme due to binding, as well as on phoresis due to non-contact interactions between enzyme and substrate. Here, after reviewing and generalizing our previous findings, we extend them in two different ways. In the case of enhanced diffusion, we show that an exact result for the long-time diffusion coefficient of the enzyme can be obtained using generalized Taylor dispersion theory, which results in much simpler and transparent analytical expressions for the diffusion enhancement. In the case of chemotaxis, we show that the competition between phoresis and binding-induced changes in diffusion results in non-trivial steady state distributions for the enzyme, which can either accumulate in or be depleted from regions with a specific substrate concentration.
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