150 related articles for article (PubMed ID: 23933321)
1. Crystal structure of the CueO mutants at Glu506, the key amino acid located in the proton transfer pathway for dioxygen reduction.
Komori H; Kajikawa T; Kataoka K; Higuchi Y; Sakurai T
Biochem Biophys Res Commun; 2013 Sep; 438(4):686-90. PubMed ID: 23933321
[TBL] [Abstract][Full Text] [Related]
2. Modifications on the hydrogen bond network by mutations of Escherichia coli copper efflux oxidase affect the process of proton transfer to dioxygen leading to alterations of enzymatic activities.
Kajikawa T; Kataoka K; Sakurai T
Biochem Biophys Res Commun; 2012 May; 422(1):152-6. PubMed ID: 22564733
[TBL] [Abstract][Full Text] [Related]
3. Enhancement of laccase activity through the construction and breakdown of a hydrogen bond at the type I copper center in Escherichia coli CueO and the deletion mutant Δα5-7 CueO.
Kataoka K; Hirota S; Maeda Y; Kogi H; Shinohara N; Sekimoto M; Sakurai T
Biochemistry; 2011 Feb; 50(4):558-65. PubMed ID: 21142169
[TBL] [Abstract][Full Text] [Related]
4. Reaction mechanisms of the multicopper oxidase CueO from Escherichia coli support its functional role as a cuprous oxidase.
Djoko KY; Chong LX; Wedd AG; Xiao Z
J Am Chem Soc; 2010 Feb; 132(6):2005-15. PubMed ID: 20088522
[TBL] [Abstract][Full Text] [Related]
5. Amino acids located in the outer-sphere of the trinuclear copper center in a multicopper oxidase, CueO as the putative electron donor in the four-electron reduction of dioxygen.
Sakurai T; Yamamoto M; Ikeno S; Kataoka K
Biochim Biophys Acta Proteins Proteom; 2017 Aug; 1865(8):997-1003. PubMed ID: 28473295
[TBL] [Abstract][Full Text] [Related]
6. Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase.
Sakurai T; Kataoka K
Chem Rec; 2007; 7(4):220-9. PubMed ID: 17663447
[TBL] [Abstract][Full Text] [Related]
7. A novel resting form of the trinuclear copper center in the double mutant of a multicopper oxidase, CueO, Cys500Ser/Glu506Ala.
Kajikawa T; Sugiyama R; Kataoka K; Sakurai T
J Inorg Biochem; 2015 Aug; 149():88-90. PubMed ID: 25840508
[TBL] [Abstract][Full Text] [Related]
8. Four-electron reduction of dioxygen by a multicopper oxidase, CueO, and roles of Asp112 and Glu506 located adjacent to the trinuclear copper center.
Kataoka K; Sugiyama R; Hirota S; Inoue M; Urata K; Minagawa Y; Seo D; Sakurai T
J Biol Chem; 2009 May; 284(21):14405-13. PubMed ID: 19297322
[TBL] [Abstract][Full Text] [Related]
9. The functional roles of the three copper sites associated with the methionine-rich insert in the multicopper oxidase CueO from E. coli.
Cortes L; Wedd AG; Xiao Z
Metallomics; 2015 May; 7(5):776-85. PubMed ID: 25679350
[TBL] [Abstract][Full Text] [Related]
10. Mutations at Asp112 adjacent to the trinuclear Cu center in CueO as the proton donor in the four-electron reduction of dioxygen.
Ueki Y; Inoue M; Kurose S; Kataoka K; Sakurai T
FEBS Lett; 2006 Jul; 580(17):4069-72. PubMed ID: 16828082
[TBL] [Abstract][Full Text] [Related]
11. Study on dioxygen reduction by mutational modifications of the hydrogen bond network leading from bulk water to the trinuclear copper center in bilirubin oxidase.
Morishita H; Kurita D; Kataoka K; Sakurai T
Biochem Biophys Res Commun; 2014 Jul; 450(1):767-72. PubMed ID: 24952160
[TBL] [Abstract][Full Text] [Related]
12. Structure and function of the engineered multicopper oxidase CueO from Escherichia coli--deletion of the methionine-rich helical region covering the substrate-binding site.
Kataoka K; Komori H; Ueki Y; Konno Y; Kamitaka Y; Kurose S; Tsujimura S; Higuchi Y; Kano K; Seo D; Sakurai T
J Mol Biol; 2007 Oct; 373(1):141-52. PubMed ID: 17804014
[TBL] [Abstract][Full Text] [Related]
13. Biochemical, spectroscopic and X-ray structural analysis of deuterated multicopper oxidase CueO prepared from a new expression construct for neutron crystallography.
Akter M; Inoue C; Komori H; Matsuda N; Sakurai T; Kataoka K; Higuchi Y; Shibata N
Acta Crystallogr F Struct Biol Commun; 2016 Oct; 72(Pt 10):788-794. PubMed ID: 27710945
[TBL] [Abstract][Full Text] [Related]
14. X-ray-induced catalytic active-site reduction of a multicopper oxidase: structural insights into the proton-relay mechanism and O2-reduction states.
Serrano-Posada H; Centeno-Leija S; Rojas-Trejo SP; Rodríguez-Almazán C; Stojanoff V; Rudiño-Piñera E
Acta Crystallogr D Biol Crystallogr; 2015 Dec; 71(Pt 12):2396-411. PubMed ID: 26627648
[TBL] [Abstract][Full Text] [Related]
15. Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli.
Roberts SA; Weichsel A; Grass G; Thakali K; Hazzard JT; Tollin G; Rensing C; Montfort WR
Proc Natl Acad Sci U S A; 2002 Mar; 99(5):2766-71. PubMed ID: 11867755
[TBL] [Abstract][Full Text] [Related]
16. ATR-FTIR study of the protonation states of the Glu residue in the multicopper oxidases, CueO and bilirubin oxidase.
Iwaki M; Kataoka K; Kajino T; Sugiyama R; Morishita H; Sakurai T
FEBS Lett; 2010 Sep; 584(18):4027-31. PubMed ID: 20727354
[TBL] [Abstract][Full Text] [Related]
17. Structural and functional characterisation of multi-copper oxidase CueO from lignin-degrading bacterium Ochrobactrum sp. reveal its activity towards lignin model compounds and lignosulfonate.
Granja-Travez RS; Wilkinson RC; Persinoti GF; Squina FM; Fülöp V; Bugg TDH
FEBS J; 2018 May; 285(9):1684-1700. PubMed ID: 29575798
[TBL] [Abstract][Full Text] [Related]
18. Modifications of laccase activities of copper efflux oxidase, CueO by synergistic mutations in the first and second coordination spheres of the type I copper center.
Kataoka K; Kogi H; Tsujimura S; Sakurai T
Biochem Biophys Res Commun; 2013 Feb; 431(3):393-7. PubMed ID: 23337502
[TBL] [Abstract][Full Text] [Related]
19. Glutamates 99 and 107 in transmembrane helix III of subunit I of cytochrome bd are critical for binding of the heme b595-d binuclear center and enzyme activity.
Mogi T; Endou S; Akimoto S; Morimoto-Tadokoro M; Miyoshi H
Biochemistry; 2006 Dec; 45(51):15785-92. PubMed ID: 17176101
[TBL] [Abstract][Full Text] [Related]
20. Kinetics of electron and proton transfer during the reaction of wild type and helix VI mutants of cytochrome bo3 with oxygen.
Svensson-Ek M; Thomas JW; Gennis RB; Nilsson T; Brzezinski P
Biochemistry; 1996 Oct; 35(42):13673-80. PubMed ID: 8885847
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]