标题:Crystal structure and biochemical features of dye-decolorizing peroxidase YfeX from Escherichia coli O157 Asp(143) and Arg(232) play divergent roles toward different substrates
作者:Liu, Xiuhua; Yuan, Zenglin; Wang, Jiaxu; Cui, Yaqi; Liu, Shuang; Ma, Yinliang; Gu, Lichuan; Xu, Sujuan
作者机构:[Liu, Xiuhua; Wang, Jiaxu; Cui, Yaqi; Liu, Shuang; Ma, Yinliang] Hebei Univ, Coll Life Sci, Baoding 071002, Peoples R China.; [Yuan, Zenglin; Gu, Li 更多
通讯作者:Liu, XH;Xu, SJ
通讯作者地址:[Liu, XH]Hebei Univ, Coll Life Sci, Baoding 071002, Peoples R China;[Xu, SJ]Shandong Univ, State Key Lab Microbial Technol, Jinan 250100, Peoples R Ch 更多
来源:BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
出版年:2017
卷:484
期:1
页码:40-44
DOI:10.1016/j.bbrc.2017.01.081
关键词:YfeX; Dye-decolorizing peroxidase; Crystal structure; Reactive blue 19;; ABTS; Guaiacol
摘要:YfeX from Escherichia coli 0157 is a bacterial dye-decolorizing peroxidase that represents both dye-decoloring activity and typical peroxidase activity. We reported the crystal structure of YfeX bound to heme at 2.09 A resolution. The YfeX monomer resembles a ferredoxin-like fold and contains two domains. The three conserved residues surrounding the heme group are His(215), Asp(143) and Arg(232). His(215) functions as the proximal axial ligand of the heme iron atom. Biochemical data show that the catalytic significance of the conserved Asp(143) and Arg(232) depends on the substrate types and that YfeX may adopt various catalytic mechanisms toward divergent substrates. In addition, it is observed that an access tunnel spans from the protein molecular surface to the heme distal region, it serves as the passageway for the entrance and binding of the H2O2. (C) 2017 Elsevier Inc. All rights reserved.
收录类别:SCOPUS;SCIE
WOS核心被引频次:2
Scopus被引频次:2
资源类型:期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-85010417221&doi=10.1016%2fj.bbrc.2017.01.081&partnerID=40&md5=033b0255eb878de77fdf6e228ecf8f03
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