An expanded genetic code for probing the role of electrostatics in enzyme catalysis by vibrational Stark spectroscopy.
An expanded genetic code for probing the role of electrostatics in enzyme catalysis by vibrational Stark spectroscopy.
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DOI：
10.1016/j.bbagen.2017.02.009
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发表时间：
2017-11
期刊：
影响因子：
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通讯作者：
Jan-Stefan Völler;H. Biava;P. Hildebrandt;N. Budisa
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文献类型：
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作者：
Jan-Stefan Völler;H. Biava;P. Hildebrandt;N. Budisa
背景由于评估蛋白质结构内电场的实际限制，寻找催化反应必需的静电相互作用的实验验证是一项挑战。综述范围这篇综述研究了非规范氨基酸（ncAA）作为基因编码探针的应用，用于研究静电相互作用在酶催化中的作用。主要结论ncAA构成敏感的光谱探针，可利用振动斯塔克效应（VSE）检测局部电场，从而有可能绘制蛋白质静电图。一般意义蛋白质中的静电将提高我们对自然催化过程的理解，并且更有助于生物催化剂工程。本文是题为“合成生物学的生物化学 - 最新进展”特刊的一部分。客座编辑：Ilka Heinemann 博士和 Patrick O'Donoghue 博士。
BackgroundTo find experimental validation for electrostatic interactions essential for catalytic reactions represents a challenge due to practical limitations in assessing electric fields within protein structures.Scope of reviewThis review examines the applications of non-canonical amino acids (ncAAs) as genetically encoded probes for studying the role of electrostatic interactions in enzyme catalysis.Major conclusionsncAAs constitute sensitive spectroscopic probes to detect local electric fields by exploiting the vibrational Stark effect (VSE) and thus have the potential to map the protein electrostatics.General significanceMapping the electrostatics in proteins will improve our understanding of natural catalytic processes and, in beyond, will be helpful for biocatalyst engineering. This article is part of a Special Issue entitled “Biochemistry of Synthetic Biology - Recent Developments” Guest Editor: Dr. Ilka Heinemann and Dr. Patrick O'Donoghue.