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用于胞外电子传递的周质蛋白流动性 于……中

Periplasmic Protein Mobility for Extracellular Electron Transport in .

作者信息

Li Daobo, Zheng Xiaodan, Yang Yonggang, Xu Meiying

机构信息

Guangdong Provincial Key Laboratory of Microbial Culture Collection and Application, State Key Laboratory of Applied Microbiology Southern China, Institute of Microbiology, Guangdong Academy of Sciences, Guangzhou 510070, China.

Guangdong Provincial Key Laboratory of Environmental Protection Microbiology and Regional Ecological Security, Guangzhou 510070, China.

出版信息

Microorganisms. 2025 May 16;13(5):1144. doi: 10.3390/microorganisms13051144.

DOI:10.3390/microorganisms13051144
PMID:40431315
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12114092/
Abstract

Extracellular electron transport (EET) supports the survival of specific microorganisms on the Earth's surface by facilitating microbial respiration with diverse electron acceptors. A key aspect of EET is the organization of electron relays, i.e., multi-heme c-type cytochromes (MHCs), within the periplasmic space of microbial cells. In this study, we investigated the mobility of periplasmic electron relays in MR-1, a model strain capable of EET, using in vivo protein crosslinking to the MHCs. First, we established that crosslinking efficiency correlates with the spatial proximity and diffusion coefficient of protein molecules through in vitro tests. Based on these findings, we identified distinct molecular behaviors of periplasmic MHCs, showing that the tetraheme flavocytochrome FccA, which also serves as a periplasmic fumarate reductase, forms protein complexes with limited motility, while the small tetraheme c-type cytochrome CctA remains discrete and mobile. Both MHCs contribute to EET for bioelectrochemical nitrate and nitrite reduction. These findings reveal dual mechanisms for organizing periplasmic electron relays in EET, advancing our understanding of microbial extracellular respiration.

摘要

细胞外电子传递(EET)通过促进微生物与多种电子受体的呼吸作用,支持特定微生物在地球表面的生存。EET的一个关键方面是在微生物细胞周质空间内组织电子传递体,即多血红素c型细胞色素(MHCs)。在本研究中,我们使用对MHCs进行体内蛋白质交联的方法,研究了能够进行EET的模式菌株MR-1中周质电子传递体的流动性。首先,我们通过体外试验确定交联效率与蛋白质分子的空间接近度和扩散系数相关。基于这些发现,我们确定了周质MHCs的不同分子行为,表明同时作为周质延胡索酸还原酶的四血红素黄素细胞色素FccA形成了运动性有限的蛋白质复合物,而小四血红素c型细胞色素CctA则保持离散且可移动。这两种MHCs都有助于生物电化学硝酸盐和亚硝酸盐还原的EET过程。这些发现揭示了EET中组织周质电子传递体的双重机制,增进了我们对微生物细胞外呼吸的理解。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed28/12114092/252fa0e196c3/microorganisms-13-01144-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed28/12114092/00685ea7309f/microorganisms-13-01144-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed28/12114092/4b84ece262f8/microorganisms-13-01144-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed28/12114092/f0d767efcd76/microorganisms-13-01144-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed28/12114092/bf164a95565e/microorganisms-13-01144-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed28/12114092/252fa0e196c3/microorganisms-13-01144-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed28/12114092/00685ea7309f/microorganisms-13-01144-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed28/12114092/4b84ece262f8/microorganisms-13-01144-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed28/12114092/f0d767efcd76/microorganisms-13-01144-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed28/12114092/bf164a95565e/microorganisms-13-01144-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed28/12114092/252fa0e196c3/microorganisms-13-01144-g005.jpg

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本文引用的文献

1
Single-protein Diffusion in the Periplasm of Escherichia coli.大肠杆菌周质中单蛋白的扩散。
J Mol Biol. 2024 Feb 15;436(4):168420. doi: 10.1016/j.jmb.2023.168420. Epub 2023 Dec 22.
2
Quantitative Interpretation of Protein Diffusion Coefficients in Mixed Protiated-Deuteriated Aqueous Solvents.定量解释混合氘代质子化水溶剂中蛋白质扩散系数。
J Phys Chem B. 2022 Aug 11;126(31):5887-5895. doi: 10.1021/acs.jpcb.2c03554. Epub 2022 Aug 2.
3
Molecular Mechanisms of Microbial Extracellular Electron Transfer: The Importance of Multiheme Cytochromes.
微生物细胞外电子转移的分子机制:多血红素细胞色素的重要性。
Front Biosci (Landmark Ed). 2022 Jun 1;27(6):174. doi: 10.31083/j.fbl2706174.
4
The hitchhiker's guide to the periplasm: Unexpected molecular interactions of polymyxin B1 in E. coli.周质空间漫游指南:多粘菌素 B1 在大肠杆菌中的意外分子相互作用。
Structure. 2021 May 6;29(5):444-456.e2. doi: 10.1016/j.str.2021.01.009. Epub 2021 Feb 11.
5
Periplasmic Targets for the Development of Effective Antimicrobials against Gram-Negative Bacteria.开发针对革兰氏阴性菌的有效抗菌药物的周质靶点
ACS Infect Dis. 2020 Sep 11;6(9):2337-2354. doi: 10.1021/acsinfecdis.0c00384. Epub 2020 Aug 24.
6
Mass spectrometry reveals the chemistry of formaldehyde cross-linking in structured proteins.质谱分析揭示了结构蛋白中甲醛交联的化学性质。
Nat Commun. 2020 Jun 19;11(1):3128. doi: 10.1038/s41467-020-16935-w.
7
The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire.生物绝缘跨膜分子线的晶体结构
Cell. 2020 Apr 30;181(3):665-673.e10. doi: 10.1016/j.cell.2020.03.032. Epub 2020 Apr 13.
8
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FEMS Microbiol Rev. 2020 Mar 1;44(2):155-170. doi: 10.1093/femsre/fuz031.
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Protein Sci. 2020 Apr;29(4):830-842. doi: 10.1002/pro.3787. Epub 2019 Nov 28.
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