• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

确定腺苷甲硫氨酸自由基酶超家族中铁硫簇的氧化还原电位。

Determining Redox Potentials of the Iron-Sulfur Clusters of the AdoMet Radical Enzyme Superfamily.

作者信息

Maiocco Stephanie J, Walker Lindsey M, Elliott Sean J

机构信息

Department of Chemistry, Boston University, Boston, MA, United States.

Department of Chemistry, Boston University, Boston, MA, United States.

出版信息

Methods Enzymol. 2018;606:319-339. doi: 10.1016/bs.mie.2018.06.002. Epub 2018 Jul 5.

DOI:10.1016/bs.mie.2018.06.002
PMID:30097097
Abstract

While protein film electrochemistry (PFE) has proven to be an effective tool in the interrogation of redox cofactors and assessing the electrocatalytic activity of many different enzymes, recently it has been proven to be useful for the study of the redox potentials of the cofactors of AdoMet radical enzymes (AREs). In this chapter, we review the challenges and opportunities of examining the redox cofactors of AREs in a high level of detail, particularly for the deconvolution of redox potentials of multiple cofactors. We comment on how to best assess the electroactive nature of any given ARE, and we see that when applied well, PFE allows for not only determining redox potentials, but also determining proton-coupling and ligand-binding phenomena in the ARE superfamily.

摘要

虽然蛋白质膜电化学(PFE)已被证明是研究氧化还原辅因子和评估许多不同酶的电催化活性的有效工具,但最近已证明它对于研究腺苷甲硫氨酸自由基酶(AREs)辅因子的氧化还原电位很有用。在本章中,我们详细回顾了研究AREs氧化还原辅因子的挑战和机遇,特别是对于多个辅因子氧化还原电位的解卷积。我们评论了如何最好地评估任何给定ARE的电活性本质,并且我们发现,当应用得当时,PFE不仅允许确定氧化还原电位,还允许确定ARE超家族中的质子耦合和配体结合现象。

相似文献

1
Determining Redox Potentials of the Iron-Sulfur Clusters of the AdoMet Radical Enzyme Superfamily.确定腺苷甲硫氨酸自由基酶超家族中铁硫簇的氧化还原电位。
Methods Enzymol. 2018;606:319-339. doi: 10.1016/bs.mie.2018.06.002. Epub 2018 Jul 5.
2
A Rich Man, Poor Man Story of S-Adenosylmethionine and Cobalamin Revisited.重新审视 S-腺苷甲硫氨酸和钴胺素的富有者和贫穷者故事。
Annu Rev Biochem. 2018 Jun 20;87:555-584. doi: 10.1146/annurev-biochem-062917-012500.
3
Auxiliary iron-sulfur cofactors in radical SAM enzymes.自由基S-腺苷甲硫氨酸酶中的辅助铁硫辅因子。
Biochim Biophys Acta. 2015 Jun;1853(6):1316-34. doi: 10.1016/j.bbamcr.2015.01.002. Epub 2015 Jan 15.
4
Enzyme catalyzed formation of radicals from S-adenosylmethionine and inhibition of enzyme activity by the cleavage products.酶催化由S-腺苷甲硫氨酸形成自由基以及裂解产物对酶活性的抑制作用。
Biochim Biophys Acta. 2012 Nov;1824(11):1165-77. doi: 10.1016/j.bbapap.2012.03.013. Epub 2012 Apr 3.
5
Structural diversity in the AdoMet radical enzyme superfamily.S-腺苷甲硫氨酸自由基酶超家族中的结构多样性。
Biochim Biophys Acta. 2012 Nov;1824(11):1178-95. doi: 10.1016/j.bbapap.2012.04.006. Epub 2012 Apr 28.
6
The biosynthesis of thiol- and thioether-containing cofactors and secondary metabolites catalyzed by radical S-adenosylmethionine enzymes.由自由基S-腺苷甲硫氨酸酶催化的含硫醇和硫醚辅因子及次生代谢产物的生物合成。
J Biol Chem. 2015 Feb 13;290(7):3972-9. doi: 10.1074/jbc.R114.599308. Epub 2014 Dec 4.
7
Radical AdoMet enzymes in complex metal cluster biosynthesis.复杂金属簇生物合成中的自由基腺苷甲硫氨酸酶
Biochim Biophys Acta. 2012 Nov;1824(11):1254-63. doi: 10.1016/j.bbapap.2012.01.002. Epub 2012 Jan 14.
8
Electrochemical Resolution of the [4Fe-4S] Centers of the AdoMet Radical Enzyme BtrN: Evidence of Proton Coupling and an Unusual, Low-Potential Auxiliary Cluster.电化学拆分 AdoMet 自由基酶 BtrN 的 [4Fe-4S] 中心:质子偶联的证据和一个不寻常的、低电位辅助簇。
J Am Chem Soc. 2015 Jul 15;137(27):8664-7. doi: 10.1021/jacs.5b03384. Epub 2015 Jun 25.
9
Control of radical chemistry in the AdoMet radical enzymes.腺苷甲硫氨酸自由基酶中自由基化学的控制。
Curr Opin Chem Biol. 2009 Feb;13(1):74-83. doi: 10.1016/j.cbpa.2009.01.022. Epub 2009 Mar 9.
10
Spectroscopic and Electrochemical Characterization of the Iron-Sulfur and Cobalamin Cofactors of TsrM, an Unusual Radical S-Adenosylmethionine Methylase.TsrM的铁硫和钴胺素辅因子的光谱和电化学表征,TsrM是一种不寻常的自由基S-腺苷甲硫氨酸甲基转移酶。
J Am Chem Soc. 2016 Mar 16;138(10):3416-26. doi: 10.1021/jacs.5b12592. Epub 2016 Mar 3.

引用本文的文献

1
The redox landscape of pyruvate:ferredoxin oxidoreductases reveals often conserved Fe-S cluster potentials.丙酮酸:铁氧化还原蛋白氧化还原酶的氧化还原格局揭示了通常保守的铁硫簇电位。
J Biol Chem. 2025 Aug;301(8):110380. doi: 10.1016/j.jbc.2025.110380. Epub 2025 Jun 16.
2
Proteomic strategies to interrogate the Fe-S proteome.蛋白质组学策略探究铁硫蛋白组。
Biochim Biophys Acta Mol Cell Res. 2024 Oct;1871(7):119791. doi: 10.1016/j.bbamcr.2024.119791. Epub 2024 Jun 25.
3
Mössbauer-based molecular-level decomposition of the Saccharomyces cerevisiae ironome, and preliminary characterization of isolated nuclei.
基于穆斯堡尔谱的酿酒酵母全铁组学分子水平解析,以及分离核的初步特征描述。
Metallomics. 2022 Nov 1;14(11). doi: 10.1093/mtomcs/mfac080.
4
Deconvoluting the Reduction Potentials for the Three [4Fe-4S] Clusters in an AdoMet Radical SCIFF Maturase.解析腺苷甲硫氨酸自由基S-腺苷-L-高半胱氨酸异构酶中三个[4Fe-4S]簇的还原电位
Biochemistry. 2018 Oct 23;57(42):6050-6053. doi: 10.1021/acs.biochem.8b00846. Epub 2018 Oct 10.