厌氧二氧化碳固定过程中一种关键酶的表达、纯化和活化:Carboxydothermus hydrogenoformans 的一氧化碳脱氢酶 II。

4区 生物学 Q3 Biochemistry, Genetics and Molecular Biology
Methods in enzymology Pub Date : 2024-01-01 Epub Date: 2024-10-29 DOI:10.1016/bs.mie.2024.10.016
Kareem Aboulhosn, Stephen Wiley Ragsdale
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引用次数: 0

摘要

到 2030 年,人为排放造成的气候变化将使全球气温上升至少 1.5 °C。降低气候变化影响严重程度的策略之一是通过自然生化循环封存二氧化碳。一氧化碳脱氢酶(CODH)具有催化一氧化碳还原为一氧化碳的非凡能力,既不会产生过电位,也不会产生还原质子。它也是伍德-荣格达尔途径(WLP)中的一种关键酶,该途径是唯一已知的厌氧碳固定途径,每年固定地球上 10% 的碳。对这一途径进行表征至关重要,因为它可以利用二氧化碳生产生物燃料、化学原料和聚合物,从而成为减缓气候变化的工具。在 WLP 中,CODH 与乙酰辅酶 A 合成酶(ACS)结合,后者催化 CODH 中的 CO、依赖 B12 的甲基转移酶产生的甲基和 CoA 缩合,形成乙酰辅酶 A。在这个复合体中,CO 通过 138 Å 的气体隧道穿梭于两个酶之间。研究 CODH/ACS 的 CODH 成分的一个重要模型是来自 Carboxydothermus hydrogenoformans 的 CODH-II,因为它是独立的,有利于重组表达。在这里,我们描述了在大肠杆菌中生产高活性 CODH-II 的详细方案。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Expression, purification, and activation of one key enzyme in anaerobic CO2 fixation: Carbon monoxide dehydrogenase II from Carboxydothermus hydrogenoformans.

Climate change due to anthropomorphic emissions will increase global temperature by at least 1.5 °C by the year 2030. One strategy to reduce the severity of the effects of climate change is to sequester carbon dioxide via natural biochemical cycles. Carbon monoxide dehydrogenase (CODH) has the remarkable ability to catalyze the reversible reduction of CO2 to CO without an overpotential and without reducing protons. It also is a key enzyme in the Wood-Ljungdahl pathway (WLP), which is the only known anaerobic carbon fixation pathway and fixes 10 % of carbon on earth every year. Characterization of this pathway is crucial because it may enable tools to mitigate climate change by using CO2 to produce biofuels, chemical feedstocks, and polymers. In the WLP, CODH associates with Acetyl-Coenzyme A synthase (ACS), which catalyzes the condensation of CO from CODH, a methyl group from a B12-dependent methyltransferase, and CoA to form acetyl-CoA. In this complex, CO is shuttled through a 138 Å gas tunnel between the two enzymes. One valuable model for studying the CODH component of CODH/ACS is CODH-II from Carboxydothermus hydrogenoformans because it is stand-alone and is conducive to recombinant expression. Here we describe a detailed protocol for producing high-activity CODH-II in E. coli.

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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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