• 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

氧桥非血红素双铁蛋白的结构和功能多样性。

Diversity of structures and functions of oxo-bridged non-heme diiron proteins.

机构信息

Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, FL, 32827, United States.

Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, FL, 32827, United States.

出版信息

Arch Biochem Biophys. 2021 Jul 15;705:108917. doi: 10.1016/j.abb.2021.108917. Epub 2021 May 12.

DOI:10.1016/j.abb.2021.108917
PMID:33991497
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8165033/
Abstract

Oxo-bridged diiron proteins are a distinct class of non-heme iron proteins. Their active sites are composed of two irons that are coordinated by amino acid side chains, and a bridging oxygen that interacts with each iron. These proteins are members of the ferritin superfamily and share the structural feature of a four α-helix bundle that provides the residues that coordinate the irons. The different proteins also display a wide range of structures and functions. A prototype of this family is hemerythrin, which functions as an oxygen transporter. Several other hemerythrin-like proteins have been described with a diversity of functions including oxygen and iron sensing, and catalytic activities. Rubrerythrins react with hydrogen peroxide and rubrerythrin-like proteins possess a rubredoxin domain, in addition to the oxo-bridged diiron center. Other redox enzymes with oxo-bridged irons include flavodiiron proteins that act as O or NO reductases, ribonucleotide reductase and methane monooxygenase. Ferritins have an oxo-bridged diiron in the ferroxidase center of the protein, which plays a role in the iron storage function of these proteins. There are also bacterial ferritins that exhibit catalytic activities. The structures and functions of this broad class of oxo-bridged diiron proteins are described and compared in this review.

摘要

氧桥双核铁蛋白是一类独特的非血红素铁蛋白。它们的活性部位由两个铁原子组成,由氨基酸侧链配位,一个桥接氧原子与每个铁原子相互作用。这些蛋白是铁蛋白超家族的成员,具有由四个α-螺旋束组成的结构特征,为配位铁原子提供残基。不同的蛋白质也显示出广泛的结构和功能。该家族的原型是血蓝蛋白,它作为氧气转运蛋白发挥作用。已经描述了几种其他类似血蓝蛋白的蛋白,具有多种功能,包括氧气和铁感应以及催化活性。Rubrerythrins 与过氧化氢反应,Rubrerythrins 样蛋白除了具有氧桥双核铁中心外,还具有 rubredoxin 结构域。其他具有氧桥铁的氧化还原酶包括作为 O 或 NO 还原酶的黄素铁蛋白、核苷酸还原酶和甲烷单加氧酶。铁蛋白在蛋白的亚铁氧化酶中心具有氧桥双核铁,在这些蛋白的铁储存功能中起作用。还有具有催化活性的细菌铁蛋白。本文综述了这一大类氧桥双核铁蛋白的结构和功能,并对其进行了比较。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/c0dc8addb387/nihms-1705309-f0013.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/dc8ef1b6fbe9/nihms-1705309-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/02997b6b1f1b/nihms-1705309-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/345e95c01017/nihms-1705309-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/23ed78015063/nihms-1705309-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/a04e8278ec84/nihms-1705309-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/f13e4b5f3e03/nihms-1705309-f0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/c2600916d71e/nihms-1705309-f0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/2ab8046abb3c/nihms-1705309-f0008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/1d2b093219fb/nihms-1705309-f0009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/c48418e529bd/nihms-1705309-f0010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/e4e5db59f5ce/nihms-1705309-f0011.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/81f530f21184/nihms-1705309-f0012.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/c0dc8addb387/nihms-1705309-f0013.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/dc8ef1b6fbe9/nihms-1705309-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/02997b6b1f1b/nihms-1705309-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/345e95c01017/nihms-1705309-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/23ed78015063/nihms-1705309-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/a04e8278ec84/nihms-1705309-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/f13e4b5f3e03/nihms-1705309-f0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/c2600916d71e/nihms-1705309-f0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/2ab8046abb3c/nihms-1705309-f0008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/1d2b093219fb/nihms-1705309-f0009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/c48418e529bd/nihms-1705309-f0010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/e4e5db59f5ce/nihms-1705309-f0011.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/81f530f21184/nihms-1705309-f0012.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6102/8165033/c0dc8addb387/nihms-1705309-f0013.jpg

相似文献

1
Diversity of structures and functions of oxo-bridged non-heme diiron proteins.氧桥非血红素双铁蛋白的结构和功能多样性。
Arch Biochem Biophys. 2021 Jul 15;705:108917. doi: 10.1016/j.abb.2021.108917. Epub 2021 May 12.
2
Resonance Raman evidence for an Fe-O-Fe center in stearoyl-ACP desaturase. Primary sequence identity with other diiron-oxo proteins.硬脂酰-ACP去饱和酶中Fe-O-Fe中心的共振拉曼证据。与其他双铁-氧蛋白的一级序列同一性。
Biochemistry. 1994 Nov 1;33(43):12776-86. doi: 10.1021/bi00209a008.
3
The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains.普通脱硫弧菌红素铁氧还蛋白的结构揭示了类红氧还蛋白FeS4和类铁蛋白双铁结构域的独特组合。
Nat Struct Biol. 1996 Jun;3(6):539-46. doi: 10.1038/nsb0696-539.
4
X-ray crystal structures of reduced rubrerythrin and its azide adduct: a structure-based mechanism for a non-heme diiron peroxidase.还原型红藓红素及其叠氮化物加合物的X射线晶体结构:非血红素二铁过氧化物酶的基于结构的作用机制
J Am Chem Soc. 2002 Aug 21;124(33):9845-55. doi: 10.1021/ja026587u.
5
Di-iron-carboxylate proteins.二价铁羧酸盐蛋白
Curr Opin Struct Biol. 1995 Dec;5(6):758-66. doi: 10.1016/0959-440x(95)80008-5.
6
Spectroscopic characterization of 57Fe-reconstituted rubrerythrin, a non-heme iron protein with structural analogies to ribonucleotide reductase.57Fe重组红素铁蛋白的光谱表征,一种与核糖核苷酸还原酶具有结构相似性的非血红素铁蛋白。
Biochemistry. 1993 Aug 24;32(33):8487-91. doi: 10.1021/bi00084a013.
7
The Ferritin-like superfamily: Evolution of the biological iron storeman from a rubrerythrin-like ancestor.铁蛋白样超家族:从类红素铁蛋白样祖先演化而来的生物铁储存蛋白
Biochim Biophys Acta. 2010 Aug;1800(8):691-705. doi: 10.1016/j.bbagen.2010.05.010. Epub 2010 May 27.
8
The ferroxidase reaction of ferritin reveals a diferric mu-1,2 bridging peroxide intermediate in common with other O2-activating non-heme diiron proteins.铁蛋白的铁氧化酶反应揭示了一种与其他激活O₂的非血红素双铁蛋白共有的双铁μ-1,2桥连过氧化物中间体。
Biochemistry. 1999 Apr 27;38(17):5290-5. doi: 10.1021/bi990095l.
9
Recombinant Desulfovibrio vulgaris rubrerythrin. Isolation and characterization of the diiron domain.重组普通脱硫弧菌红素。二铁结构域的分离与表征。
Biochemistry. 1995 Mar 14;34(10):3310-8. doi: 10.1021/bi00010a021.
10
Structure, function and evolution of the hemerythrin-like domain superfamily.血红素结合蛋白样结构域超家族的结构、功能和进化。
Protein Sci. 2018 Apr;27(4):848-860. doi: 10.1002/pro.3374. Epub 2018 Jan 30.

引用本文的文献

1
New molecular components of high and low affinity iron import systems in Drosophila.果蝇中高亲和力和低亲和力铁导入系统的新分子成分
Nat Commun. 2025 Jul 1;16(1):5662. doi: 10.1038/s41467-025-60758-6.
2
A [FeFe] Hydrogenase-Rubrerythrin Chimeric Enzyme Functions to Couple H Oxidation to Reduction of HO in the Foodborne Pathogen .一种[铁铁]氢化酶-红氧还蛋白嵌合酶在食源性病原体中发挥作用,将氢氧化与过氧化氢还原偶联起来。
J Am Chem Soc. 2025 Mar 19;147(11):9764-9773. doi: 10.1021/jacs.4c18425. Epub 2025 Mar 6.
3
[Fe(µ-OH)] Linked FeO Triads: Mössbauer Evidence for Trigonal µ-O or µ-OH Groups in Bridged versus Unbridged Complexes.

本文引用的文献

1
An Overview of Dps: Dual Acting Nanovehicles in Prokaryotes with DNA Binding and Ferroxidation Properties.Dps:具有 DNA 结合和铁氧化性质的原核生物双效纳米载体概述。
Subcell Biochem. 2021;96:177-216. doi: 10.1007/978-3-030-58971-4_3.
2
Correlation of Conservation of Sequence and Structures of Mycobacterial Hemerythrin-like Proteins with Evolutionary Relationship and Host Pathogenicity.分枝杆菌类蚯蚓血红蛋白样蛋白的序列和结构保守性与进化关系及宿主致病性的相关性
ACS Omega. 2020 Sep 1;5(36):23385-23392. doi: 10.1021/acsomega.0c03338. eCollection 2020 Sep 15.
3
Engineered Ferritin Nanoparticles for the Bioluminescence Tracking of Nanodrug Delivery in Cancer.
[Fe(µ-OH)]连接的FeO三元组:穆斯堡尔谱证据表明桥联和非桥联配合物中存在三角µ-O或µ-OH基团
Molecules. 2024 Jul 7;29(13):3218. doi: 10.3390/molecules29133218.
4
Drosophila Evi5 is a critical regulator of intracellular iron transport via transferrin and ferritin interactions.果蝇 Evi5 通过与转铁蛋白和铁蛋白的相互作用,是细胞内铁运输的关键调节因子。
Nat Commun. 2024 May 14;15(1):4045. doi: 10.1038/s41467-024-48165-9.
5
Iron Metabolism of the Skin: Recycling versus Release.皮肤的铁代谢:再循环与释放
Metabolites. 2023 Sep 12;13(9):1005. doi: 10.3390/metabo13091005.
6
Mobilization of iron stored in bacterioferritin, a new target for perturbing iron homeostasis and developing antibacterial and antibiofilm molecules.动员储存在细菌铁蛋白中的铁,这是干扰铁稳态以及开发抗菌和抗生物膜分子的一个新靶点。
J Inorg Biochem. 2023 Oct;247:112306. doi: 10.1016/j.jinorgbio.2023.112306. Epub 2023 Jun 26.
7
The Oxidative Stress-Induced Hypothetical Protein PG_0686 in Porphyromonas gingivalis W83 Is a Novel Diguanylate Cyclase.牙龈卟啉单胞菌W83中氧化应激诱导的假定蛋白PG_0686是一种新型二鸟苷酸环化酶。
Microbiol Spectr. 2023 Jan 31;11(2):e0441122. doi: 10.1128/spectrum.04411-22.
8
An Abundant and Diverse New Family of Electron Bifurcating Enzymes With a Non-canonical Catalytic Mechanism.具有非经典催化机制的丰富多样的新型电子分叉酶家族
Front Microbiol. 2022 Jul 8;13:946711. doi: 10.3389/fmicb.2022.946711. eCollection 2022.
9
Repair of Iron Center Proteins-A Different Class of Hemerythrin-like Proteins.铁中心蛋白的修复-一类不同的血蓝蛋白样蛋白。
Molecules. 2022 Jun 23;27(13):4051. doi: 10.3390/molecules27134051.
10
Genome-Scale Mutational Analysis of Cathode-Oxidizing ElOx9.阴极氧化酶ElOx9的全基因组规模突变分析
Front Microbiol. 2022 Jun 10;13:909824. doi: 10.3389/fmicb.2022.909824. eCollection 2022.
工程化铁蛋白纳米颗粒用于癌症中纳米药物递释的生物发光示踪
Small. 2020 Oct;16(39):e2001450. doi: 10.1002/smll.202001450. Epub 2020 Aug 28.
4
Ribonucleotide Reductases: Structure, Chemistry, and Metabolism Suggest New Therapeutic Targets.核苷酸还原酶:结构、化学和代谢提示新的治疗靶点。
Annu Rev Biochem. 2020 Jun 20;89:45-75. doi: 10.1146/annurev-biochem-013118-111843.
5
Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex.核糖核苷酸还原酶全酶复合物内捕获的自由基转移途径的结构。
Science. 2020 Apr 24;368(6489):424-427. doi: 10.1126/science.aba6794. Epub 2020 Mar 26.
6
Subunit Interaction Dynamics of Class Ia Ribonucleotide Reductases: In Search of a Robust Assay.I 类核糖核苷酸还原酶亚基相互作用动力学:寻找稳健的测定方法。
Biochemistry. 2020 Apr 14;59(14):1442-1453. doi: 10.1021/acs.biochem.0c00001. Epub 2020 Mar 30.
7
Stoichiometric Formation of an Oxoiron(IV) Complex by a Soluble Methane Monooxygenase Type Activation of O at an Iron(II)-Cyclam Center.通过可溶性甲烷单加氧酶在铁(II)-环戊二烯基中心对 O 的作用,形成氧合铁(IV)配合物的化学计量。
J Am Chem Soc. 2020 Apr 1;142(13):5924-5928. doi: 10.1021/jacs.9b13756. Epub 2020 Mar 18.
8
Identification and Characterization of a Redox Sensor Phosphodiesterase from sp. PN-J185 Containing Bacterial Hemerythrin and HD-GYP Domains.鉴定和表征含有细菌血蓝蛋白和 HD-GYP 结构域的 sp. PN-J185 中的氧化还原传感器磷酸二酯酶。
Biochemistry. 2020 Mar 3;59(8):983-991. doi: 10.1021/acs.biochem.0c00021. Epub 2020 Feb 20.
9
Iron, Ferritin, Hereditary Ferritinopathy, and Neurodegeneration.铁、铁蛋白、遗传性铁蛋白病与神经退行性变
Front Neurosci. 2019 Dec 11;13:1195. doi: 10.3389/fnins.2019.01195. eCollection 2019.
10
Crystal structure of a hemerythrin-like protein from Mycobacterium kansasii and homology model of the orthologous Rv2633c protein of M. tuberculosis.来自堪萨斯分枝杆菌的血晶蛋白样蛋白的晶体结构和结核分枝杆菌同源蛋白 Rv2633c 的同源模型。
Biochem J. 2020 Jan 31;477(2):567-581. doi: 10.1042/BCJ20190827.