Crystal structure of the CueO mutants at Glu506, the key amino acid located in the proton transfer pathway for dioxygen reduction

被引:9
作者
Komori, Hirofumi [1 ]
Kajikawa, Takao [2 ]
Kataoka, Kunishige [2 ]
Higuchi, Yoshiki [3 ]
Sakurai, Takeshi [2 ]
机构
[1] Kagawa Univ, Fac Educ, Takamatsu, Kagawa 7608522, Japan
[2] Kanazawa Univ, Grad Sch Nat Sci & Technol, Kanazawa, Ishikawa 9201192, Japan
[3] Univ Hyogo, Grad Sch Life Sci, Kamigori, Ako 6781297, Japan
关键词
CueO; Multicopper oxidase; Proton transfer; O-2-reduction; Hydrogen bond network; X-ray crystal structure; Site-directed mutagenesis; COPPER EFFLUX OXIDASE; MULTICOPPER OXIDASE; 4-ELECTRON REDUCTION; BILIRUBIN-OXIDASE; I COPPER; MUTATIONS; INTERMEDIATE; CLEAVAGE; ADJACENT; ROLES;
D O I
10.1016/j.bbrc.2013.07.121
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Glu506 involved in the hydrogen bond network leading from solvent waters to the trinuclear copper center in a multicopper oxidase, CueO plays a crucial role to transport protons in the four-electron reduction of dioxygen to water. We performed X-ray crystal structure analyses of the Glu506Ala and Glu506Ile mutants, showing the formation of a compensatory proton transport pathway with only water molecules and a disruption of the hydrogen bond network due to the bulky side chain, respectively. We discuss the efficiency of proton transport through the hydrogen bond network based on the present results and our previous modification of the proton transport pathway by the Glu506 to Gln mutation, which have allowed us to trap and characterize the reaction intermediates. (C) 2013 Elsevier Inc. All rights reserved.
引用
收藏
页码:686 / 690
页数:5
相关论文
共 30 条
  • [1] Spectroscopic and kinetic studies of perturbed trinuclear copper clusters: The role of protons in reductive cleavage of the O-O bond in the multicopper oxidase Fet3p
    Augustine, Anthony J.
    Quintanar, Liliana
    Stoj, Christopher S.
    Kosman, Daniel J.
    Solomon, Edward I.
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2007, 129 (43) : 13118 - 13126
  • [2] THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY
    BAILEY, S
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 : 760 - 763
  • [3] Ceruloplasmin revisited: structural and functional roles of various metal cation-binding sites
    Bento, Isabel
    Peixoto, Cristina
    Zaitsev, Vjacheslav N.
    Lindley, Peter F.
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2007, 63 : 240 - 248
  • [4] FREE R-VALUE - A NOVEL STATISTICAL QUANTITY FOR ASSESSING THE ACCURACY OF CRYSTAL-STRUCTURES
    BRUNGER, AT
    [J]. NATURE, 1992, 355 (6359) : 472 - 475
  • [5] The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis
    Chen, Zhenjia
    Durao, Paulo
    Silva, Catarina S.
    Pereira, Manuela M.
    Todorovic, Smilja
    Hildebrandt, Peter
    Bento, Isabel
    Lindley, Peter F.
    Martins, Ligia O.
    [J]. DALTON TRANSACTIONS, 2010, 39 (11) : 2875 - 2882
  • [6] MolProbity: structure validation and all-atom contact analysis for nucleic acids and their complexes
    Davis, IW
    Murray, LW
    Richardson, JS
    Richardson, DC
    [J]. NUCLEIC ACIDS RESEARCH, 2004, 32 : W615 - W619
  • [7] Coot:: model-building tools for molecular graphics
    Emsley, P
    Cowtan, K
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2004, 60 : 2126 - 2132
  • [8] Functional Hydration and Conformational Gating of Proton Uptake in Cytochrome c Oxidase
    Henry, Rowan M.
    Yu, Ching-Hsing
    Rodinger, Tomas
    Pomes, Regis
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2009, 387 (05) : 1165 - 1185
  • [9] Spectroscopic and kinetic studies on the oxygen-centered radical formed during the four-electron reduction process of dioxygen by Rhus vernicifera laccase
    Huang, HW
    Zoppellaro, G
    Sakurai, T
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (46) : 32718 - 32724
  • [10] ATR-FTIR study of the protonation states of the Glu residue in the multicopper oxidases, CueO and bilirubin oxidase
    Iwaki, Masayo
    Kataoka, Kunishige
    Kajino, Tsutomu
    Sugiyama, Ryosuke
    Morishita, Hirotoshi
    Sakurai, Takeshi
    [J]. FEBS LETTERS, 2010, 584 (18) : 4027 - 4031