Crystal Structure Analysis of the Repair of Iron Centers Protein YtfE and Its Interaction with NO

NCUIR > college of Health Sciences and Technology > Department of Life Science > journal & Dissertation > Item 987654321/102516

Please use this identifier to cite or link to this item: https://ir.lib.ncu.edu.tw/handle/987654321/102516

Title:	Crystal Structure Analysis of the Repair of Iron Centers Protein YtfE and Its Interaction with NO
Authors:	陳青諭;Lo, Feng-Chun;Hsieh, Chang-Chih;Maestre-Reyna, Manuel;Chen, Chin-Yu;Ko, Tzu-Ping;Horng, Yih-Chern;Lai, Yei-Chen;Chiang, Yun-Wei;Chou, Chih-Mao;Chiang, Cheng-Hung;Huang, Wei-Ning;Lin, Yi-Hung;Bohle, D. Scott;Liaw, Wen-Feng
Contributors:	生醫理工學院生命科學系
Keywords:	Bridging;Chemistry;Circular Dichroism;Crystal structure;Crystallography, X-Ray;Iron;Iron - chemistry;Metalloproteins - chemistry;Metalloproteins - metabolism;Microorganisms;Models, Molecular;Nitric oxide;Nitric Oxide - chemistry;Nitric Oxide - metabolism;Nitrous oxide;Nitrous oxides;non-heme diiron;protein structures;Proteins;Repair;Structural analysis;Unsaturated
Date:	2016-01-01
Issue Date:	2026-04-23 11:12:12 (UTC+8)
Publisher:	Wiley-VCH Verlag;Germany: Blackwell Publishing Ltd
Abstract:	摘要： Molecular mechanisms underlying the repair of nitrosylated [Fe–S] clusters by the microbial protein YtfE remain poorly understood. The X‐ray crystal structure of YtfE, in combination with EPR, magnetic circular dichroism (MCD), UV, and 17O‐labeling electron spin echo envelope modulation measurements, show that each iron of the oxo‐bridged FeII–FeIII diiron core is coordinatively unsaturated with each iron bound to two bridging carboxylates and two terminal histidines in addition to an oxo‐bridge. Structural analysis reveals that there are two solvent‐accessible tunnels, both of which converge to the diiron center and are critical for capturing substrates. The reactivity of the reduced‐form FeII–FeII YtfE toward nitric oxide demonstrates that the prerequisite for N2O production requires the two iron sites to be nitrosylated simultaneously. Specifically, the nitrosylation of the two iron sites prior to their reductive coupling to produce N2O is cooperative. This result suggests that, in addition to any repair of iron centers (RIC) activity, YtfE acts as an NO‐trapping scavenger to promote the NO to N2O transformation under low NO flux, which precedes nitrosative stress. Repair proteins: There is considerable interest in microbial defense mechanisms against oxidative/nitrosative stress, such as the so‐called repair of iron centers (RIC) proteins, including the Escherichia coli protein YtfE. The X‐ray crystal structure of YtfE shows that each iron of the FeII–FeIII diiron core is coordinatively unsaturated and bound to two bridging carboxylates, two terminal histidines, and an oxo‐bridge (see scheme). 其他題名： Chem. Eur. J 出版者： Germany: Blackwell Publishing Ltd 出版日期： 2016-07-04 出處： Chemistry : a European journal, 2016-07, Vol.22 (28), p.9768-9776 版權： 2016 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim 版權： 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. 版權： 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim 識別號： ISSN: 0947-6539 識別號： ISSN: 1521-3765 識別號： EISSN: 1521-3765 識別號： DOI: 10.1002/chem.201600990 識別號： PMID: 27246459 識別號： CODEN: CEUJED
Appears in Collections:	[Department of Life Science] journal & Dissertation

Files in This Item:

File	Description	Size	Format
index.html		0Kb	HTML	19	View/Open

社群 sharing

Loading...