Protein Dynamics and Enzymatic Chemical Barrier Passage
Protein Dynamics and Enzymatic Chemical Barrier Passage
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DOI：
10.1021/jp207876k
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发表时间：
2011-12-29
影响因子：
3.3
通讯作者：
Schwartz, Steven D.
中科院分区：
文献类型：
--
作者：
Antoniou, Dimitri;Schwartz, Steven D.
经过几十年的研究，酶提高化学反应速率的方式，有时是相应的溶液反应速率的10（17）倍，仍然是不透明的。在过去5-10年的文献中，一个重要的讨论主题是蛋白质动力学在这一过程中的重要性。这篇专题文章将讨论作者在这个仍然有争议的话题上的工作，重点是方法论和在实际系统中的应用。这项工作的最终结论是，对于正在研究的特定酶，在快速时间尺度上的屏障穿越（作者称之为促进振动）和构象波动的蛋白质动力学是生物催化剂功能的核心。在我们将要讨论的另一种酶中，结果就不那么清楚了。化学与蛋白质动力学耦合的方式对蛋白质结构有着深刻的影响，无论是天然的还是人造的，最近的研究结果加强了蛋白质形式的复杂性，这种形式已经进化到支持这些功能。
After many decades of investigation, the manner in which enzymes increase the rate of chemical reactions, at times by a factor of 10(17) compared to the rate of the corresponding solution phase reaction, is still opaque. A topic of significant discussion in the literature of the past 5-10 years has been the importance of protein dynamics in this process. This Feature Article will discuss the authors' work on this still controversial topic with focus on both methodology and application to real systems. The end conclusion of this work has been that for specific enzymes under study protein dynamics on both rapid time scales of barrier crossing (termed promoting vibrations by the authors) and of conformational fluctuations are central to the function of biological catalysts. In another enzyme we will discuss, the results are far less clear. The manner of the coupling of chemistry to protein dynamics has deep implications for protein architecture, both natural and created, and recent results reinforce the complexity of the protein form that has evolved to support these functions.