调查传染病中的铁硫蛋白:表征技术综述

IF 3.1 4区 化学 Q2 CHEMISTRY, INORGANIC & NUCLEAR
Md Kausar Raza, V. R. Jeyachandran, Sania Bashir
{"title":"调查传染病中的铁硫蛋白:表征技术综述","authors":"Md Kausar Raza, V. R. Jeyachandran, Sania Bashir","doi":"10.3390/inorganics12010025","DOIUrl":null,"url":null,"abstract":"Iron-sulfur [Fe-S] clusters, comprising coordinated iron and sulfur atoms arranged in diverse configurations, play a pivotal role in redox reactions and various biological processes. Diverse structural variants of [Fe-S] clusters exist, each possessing distinct attributes and functions. Recent discovery of [Fe-S] clusters in infectious pathogens, such as Mycobacterium tuberculosis, and in viruses, such as rotavirus, polyomavirus, hepatitis virus, mimivirus, and coronavirus, have sparked interest in them being a potential therapeutics target. Recent findings have associated these [Fe-S] cluster proteins playing a critical role in structural and host protein activity. However, for a very long time, metalloenzymes containing iron-sulfur clusters have been prone to destabilization in the presence of oxygen, which led to a delayed understanding of [Fe-S] proteins compared to other non-heme iron-containing proteins. Consequently, working with [Fe-S] proteins require specialized equipment, such as anaerobic chambers to maintain cofactor integrity, and tools like ultraviolet visible (UV-Vis) spectroscopy, mass spectrometry, X-ray crystallography, nuclear magnetic resonance (NMR), electron paramagnetic resonance (EPR), Mössbauer spectroscopy and electrochemical characterization. Many of these [Fe-S] cluster proteins have been misannotated as Zinc-binding proteins when purified aerobically. Moreover, the assembly of these iron-sulfur cluster cofactors have not been fully understood since it is a multi-step assembly process. Additionally, disruptions in this assembly process have been linked to human diseases. With rapid advancements in anaerobic gloveboxes and spectroscopic techniques, characterization of these [Fe-S] cluster-containing proteins that are essential for the pathogens can open up new avenues for diagnostics and therapeutics.","PeriodicalId":13572,"journal":{"name":"Inorganics","volume":"14 1","pages":""},"PeriodicalIF":3.1000,"publicationDate":"2024-01-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Investigating Iron-Sulfur Proteins in Infectious Diseases: A Review of Characterization Techniques\",\"authors\":\"Md Kausar Raza, V. R. Jeyachandran, Sania Bashir\",\"doi\":\"10.3390/inorganics12010025\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Iron-sulfur [Fe-S] clusters, comprising coordinated iron and sulfur atoms arranged in diverse configurations, play a pivotal role in redox reactions and various biological processes. Diverse structural variants of [Fe-S] clusters exist, each possessing distinct attributes and functions. Recent discovery of [Fe-S] clusters in infectious pathogens, such as Mycobacterium tuberculosis, and in viruses, such as rotavirus, polyomavirus, hepatitis virus, mimivirus, and coronavirus, have sparked interest in them being a potential therapeutics target. Recent findings have associated these [Fe-S] cluster proteins playing a critical role in structural and host protein activity. However, for a very long time, metalloenzymes containing iron-sulfur clusters have been prone to destabilization in the presence of oxygen, which led to a delayed understanding of [Fe-S] proteins compared to other non-heme iron-containing proteins. Consequently, working with [Fe-S] proteins require specialized equipment, such as anaerobic chambers to maintain cofactor integrity, and tools like ultraviolet visible (UV-Vis) spectroscopy, mass spectrometry, X-ray crystallography, nuclear magnetic resonance (NMR), electron paramagnetic resonance (EPR), Mössbauer spectroscopy and electrochemical characterization. Many of these [Fe-S] cluster proteins have been misannotated as Zinc-binding proteins when purified aerobically. Moreover, the assembly of these iron-sulfur cluster cofactors have not been fully understood since it is a multi-step assembly process. Additionally, disruptions in this assembly process have been linked to human diseases. With rapid advancements in anaerobic gloveboxes and spectroscopic techniques, characterization of these [Fe-S] cluster-containing proteins that are essential for the pathogens can open up new avenues for diagnostics and therapeutics.\",\"PeriodicalId\":13572,\"journal\":{\"name\":\"Inorganics\",\"volume\":\"14 1\",\"pages\":\"\"},\"PeriodicalIF\":3.1000,\"publicationDate\":\"2024-01-07\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Inorganics\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://doi.org/10.3390/inorganics12010025\",\"RegionNum\":4,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"CHEMISTRY, INORGANIC & NUCLEAR\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Inorganics","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.3390/inorganics12010025","RegionNum":4,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"CHEMISTRY, INORGANIC & NUCLEAR","Score":null,"Total":0}
引用次数: 0

摘要

铁硫[Fe-S]团簇由以不同构型排列的配位铁原子和硫原子组成,在氧化还原反应和各种生物过程中发挥着关键作用。Fe-S]簇存在多种结构变体,每种变体都具有不同的属性和功能。最近在结核分枝杆菌等传染病病原体和轮状病毒、多瘤病毒、肝炎病毒、米米病毒和冠状病毒等病毒中发现的[Fe-S]簇引发了人们对它们作为潜在治疗靶点的兴趣。最近的研究结果表明,这些[Fe-S]簇蛋白质在结构和宿主蛋白质活性中发挥着关键作用。然而,长期以来,含有铁硫簇的金属酶在氧气存在下容易失稳,这导致人们对[Fe-S]蛋白的了解迟于对其他非含血红素铁蛋白的了解。因此,研究[Fe-S]蛋白质需要专门的设备,例如厌氧室,以保持辅因子的完整性,还需要紫外可见光(UV-Vis)光谱、质谱、X 射线晶体学、核磁共振(NMR)、电子顺磁共振(EPR)、莫斯鲍尔光谱和电化学表征等工具。其中许多[Fe-S]簇蛋白质在有氧纯化时被误标为锌结合蛋白。此外,由于这些铁硫簇辅助因子的组装是一个多步骤的组装过程,因此还没有完全弄清其组装过程。此外,这一组装过程的中断还与人类疾病有关。随着厌氧手套箱和光谱技术的快速发展,这些对病原体至关重要的含[Fe-S]簇蛋白质的特征描述可以为诊断和治疗开辟新的途径。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Investigating Iron-Sulfur Proteins in Infectious Diseases: A Review of Characterization Techniques
Iron-sulfur [Fe-S] clusters, comprising coordinated iron and sulfur atoms arranged in diverse configurations, play a pivotal role in redox reactions and various biological processes. Diverse structural variants of [Fe-S] clusters exist, each possessing distinct attributes and functions. Recent discovery of [Fe-S] clusters in infectious pathogens, such as Mycobacterium tuberculosis, and in viruses, such as rotavirus, polyomavirus, hepatitis virus, mimivirus, and coronavirus, have sparked interest in them being a potential therapeutics target. Recent findings have associated these [Fe-S] cluster proteins playing a critical role in structural and host protein activity. However, for a very long time, metalloenzymes containing iron-sulfur clusters have been prone to destabilization in the presence of oxygen, which led to a delayed understanding of [Fe-S] proteins compared to other non-heme iron-containing proteins. Consequently, working with [Fe-S] proteins require specialized equipment, such as anaerobic chambers to maintain cofactor integrity, and tools like ultraviolet visible (UV-Vis) spectroscopy, mass spectrometry, X-ray crystallography, nuclear magnetic resonance (NMR), electron paramagnetic resonance (EPR), Mössbauer spectroscopy and electrochemical characterization. Many of these [Fe-S] cluster proteins have been misannotated as Zinc-binding proteins when purified aerobically. Moreover, the assembly of these iron-sulfur cluster cofactors have not been fully understood since it is a multi-step assembly process. Additionally, disruptions in this assembly process have been linked to human diseases. With rapid advancements in anaerobic gloveboxes and spectroscopic techniques, characterization of these [Fe-S] cluster-containing proteins that are essential for the pathogens can open up new avenues for diagnostics and therapeutics.
求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Inorganics
Inorganics Chemistry-Inorganic Chemistry
CiteScore
2.80
自引率
10.30%
发文量
193
审稿时长
6 weeks
期刊介绍: Inorganics is an open access journal that covers all aspects of inorganic chemistry research. Topics include but are not limited to: synthesis and characterization of inorganic compounds, complexes and materials structure and bonding in inorganic molecular and solid state compounds spectroscopic, magnetic, physical and chemical properties of inorganic compounds chemical reactivity, physical properties and applications of inorganic compounds and materials mechanisms of inorganic reactions organometallic compounds inorganic cluster chemistry heterogenous and homogeneous catalytic reactions promoted by inorganic compounds thermodynamics and kinetics of significant new and known inorganic compounds supramolecular systems and coordination polymers bio-inorganic chemistry and applications of inorganic compounds in biological systems and medicine environmental and sustainable energy applications of inorganic compounds and materials MD
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信