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    請使用永久網址來引用或連結此文件: https://ir.lib.ncu.edu.tw/handle/987654321/102516


    題名: Crystal Structure Analysis of the Repair of Iron Centers Protein YtfE and Its Interaction with NO
    作者: 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
    貢獻者: 生醫理工學院生命科學系
    關鍵詞: 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
    日期: 2016-01-01
    上傳時間: 2026-04-23 11:12:12 (UTC+8)
    出版者: Wiley-VCH Verlag;Germany: Blackwell Publishing Ltd
    摘要: 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
    顯示於類別:[生命科學系] 期刊論文

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