title: Crystal structure and biochemical features of dye-decolorizing peroxidase YfeX from Escherichia coli O157 Asp143and Arg232play divergent roles toward different substrates.
abstract: YfeX from Escherichia coli O157 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 Å resolution. The YfeX monomer resembles a ferredoxin-like fold and contains two domains. The three conserved residues surrounding the heme group are His215, Asp143and Arg232. His215functions as the proximal axial ligand of the heme iron atom. Biochemical data show that the catalytic significance of the conserved Asp143and Arg232depends 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.
authors.affiliation: College of Life Sciences, Hebei University, Baoding, 071002, China. Electronic address: liuxiuhua_2004@163.com.
authors.forename: Xiuhua
authors.initials: X
authors.lastname: Liu
authors.affiliation: State Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, China.
authors.forename: Zenglin
authors.initials: Z
authors.lastname: Yuan
authors.affiliation: College of Life Sciences, Hebei University, Baoding, 071002, China.
authors.forename: Jiaxu
authors.initials: J
authors.lastname: Wang
authors.affiliation: College of Life Sciences, Hebei University, Baoding, 071002, China.
authors.forename: Yaqi
authors.initials: Y
authors.lastname: Cui
authors.affiliation: College of Life Sciences, Hebei University, Baoding, 071002, China.
authors.forename: Shuang
authors.initials: S
authors.lastname: Liu
authors.affiliation: College of Life Sciences, Hebei University, Baoding, 071002, China.
authors.forename: Yinliang
authors.initials: Y
authors.lastname: Ma
authors.affiliation: State Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, China.
authors.forename: Lichuan
authors.initials: L
authors.lastname: Gu
authors.affiliation: State Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, China. Electronic address: xu_sujuan@sdu.edu.cn.
authors.forename: Sujuan
authors.initials: S
authors.lastname: Xu
mesh_terms: D001120:Arginine / Q000378:metabolism*; D001224:Aspartic Acid / Q000378:metabolism*; D002151:Calorimetry; D020134:Catalytic Domain; D027682:Cation Transport Proteins / Q000737:chemistry / Q000378:metabolism*; D003116:Color; D018360:Crystallography, X-Ray; D019453:Escherichia coli O157 / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D006418:Heme / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D027682:Cation Transport Proteins; D029968:Escherichia coli Proteins; C543326:YfeX protein, E coli; D001224:Aspartic Acid; D006418:Heme; D001120:Arginine; D006861:Hydrogen Peroxide
keywords: ABTS; Crystal structure; Dye-decolorizing peroxidase; Guaiacol; Reactive blue 19; YfeX