人造血红素-铜酶的设计与制备。

4区 生物学 Q3 Biochemistry, Genetics and Molecular Biology
Methods in enzymology Pub Date : 2025-01-01 Epub Date: 2025-09-26 DOI:10.1016/bs.mie.2025.08.004
Hirbod Heidari, Duong Phan, Danielle Lawson, Yi Lu
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引用次数: 0

摘要

天然和人工金属蛋白在生物化学中起着至关重要的作用,第一个x射线晶体结构已被解决属于血红素蛋白。由于它们能够在室温下进行各种具有挑战性的反应,有效的金属酶设计和分离策略是非常需要的。控制活性位点的几何形状往往是催化的关键要求,其诱变有助于探测各种生物和非生物反应。在小分子活化的情况下,将新的金属结合位点引入非天然血红素支架可以开启新的化学反应。在本章中,我们将提供在实验室中使用的方法来设计和实验制备含有血红素-铜中心的人工金属酶,以模拟和理解血红素-铜氧化酶。该方法可应用于设计其他含血红素的异双核中心,如硝酸氧化酶还原酶中的血红素-非血红素铁中心。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Design and preparation of artificial heme-copper enzymes.

Natural and artificial metalloproteins play a critical role in biochemistry, with the first X-ray crystal structures ever solved belonging to heme proteins Due to their ability to carry out a diverse array of challenging reactions at ambient temperature, effective metalloenzyme design and isolation strategies are highly desirable. Control of active site geometry is often the key requirement for catalysis and its mutagenesis helps probe a wide variety of biological and abiological reactions. In the case of small-molecule activation, introduction of new metal-binding sites to non-native heme scaffolds can unlock new chemistry. In this chapter, we will provide methods used in our lab for the design and experimental preparation of artificial metalloenzymes containing a heme-copper center to mimic and understand heme-copper oxidases. The methods can be applied to design other heterobinuclear centers containing heme, such as the heme-nonheme iron center in nitric oxidase reductases.

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来源期刊
Methods in enzymology
Methods in enzymology 生物-生化研究方法
CiteScore
2.90
自引率
0.00%
发文量
308
审稿时长
3-6 weeks
期刊介绍: The critically acclaimed laboratory standard for almost 50 years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Each volume is eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with over 500 volumes the series contains much material still relevant today and is truly an essential publication for researchers in all fields of life sciences, including microbiology, biochemistry, cancer research and genetics-just to name a few. Five of the 2013 Nobel Laureates have edited or contributed to volumes of MIE.
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