Modification of Spectroscopic Properties and Catalytic Activity of Escherichia coli CueO by Mutations of Methionine 510, the Axial Ligand to the Type I Cu

被引：11

作者：

Kurose, Shinji ^{[1
]}

Kataoka, Kunishige ^{[1
]}

Shinohara, Naoya ^{[1
]}

Miura, Yuko ^{[2
]}

Tsutsumi, Maiko ^{[2
]}

Tsujimura, Seiya ^{[2
]}

Kano, Kenji ^{[2
]}

Sakurai, Takeshi ^{[1
]}

机构：

[1] Kanazawa Univ, Grad Sch Nat Sci & Technol, Kanazawa, Ishikawa 9201192, Japan

[2] Kyoto Univ, Grad Sch Agr, Sakyo Ku, Kyoto 6068502, Japan

来源：

BULLETIN OF THE CHEMICAL SOCIETY OF JAPAN | 2009年 / 82卷 / 04期

关键词：

CONTAINING NITRITE REDUCTASE; VERRUCARIA BILIRUBIN-OXIDASE; COPPER SITE; STRUCTURAL-CHARACTERIZATION; PSEUDOMONAS-AERUGINOSA; MULTICOPPER OXIDASES; ELECTRONIC-STRUCTURE; COTA LACCASE; PROTON DONOR; MUTANT;

D O I：

10.1246/bcsj.82.504

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Replacement of Mct510, the axial ligand to the type I Cu in a cuprous oxidase CueO, with Len afforded the three-coordinated type I Cu, while Gln, Ala, and Thr mutations led to the replacement of the thioether ligand with oxygen ligands (amide carbonyl group and water), and characteristic properties of absorption, circular dichroism, and electron paramagnetic resonance spectra of a variety of Met510 mutants were correlated with the changes in redox potential and enzyme activities.

引用

页码：504 / 508

页数：5

共 27 条

[1]

[Anonymous], [No title captured]

[2] Spectroscopic studies of the Met182Thr mutant of nitrite reductase: Role of the axial ligand in the geometric and electronic structure of blue and green copper sites [J].

Basumallick, L ;

Szilagyi, RK ;

Zhao, YW ;

Shapleigh, JP ;

Scholes, CP ;

Solomon, EI .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2003, 125 (48) :14784-14792

[3] Generation of novel copper sites by mutation of the axial ligand of amicyanin. Atomic resolution structures and spectroscopic properties [J].

Carrell, Christopher J. ;

Ma, John K. ;

Antholine, William E. ;

Hosler, Jonathan P. ;

Mathews, F. Scott ;

Davidson, Victor L. .

BIOCHEMISTRY, 2007, 46 (07) :1900-1912

[4] Perturbations of the T1 copper site in the CotA laccase from Bacillus subtilis:: structural, biochemical, enzymatic and stability studies [J].

Durao, P ;

Bento, I ;

Fernandes, AT ;

Melo, EP ;

Lindley, PF ;

Martins, LO .

JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 2006, 11 (04) :514-526

[5] Proximal mutations at the type 1 copper site of CotA laccase: spectroscopic, redox, kinetic and structural characterization of I494A and L386A mutants [J].

Durao, Paulo ;

Chen, Zhenjia ;

Silva, Catarina S. ;

Soares, Claudio M. ;

Pereira, Manuela M. ;

Todorovic, Smilja ;

Hildebrandt, Peter ;

Bento, Isabel ;

Lindley, Peter F. ;

Martins, Ligia O. .

BIOCHEMICAL JOURNAL, 2008, 412 :339-346

[6] Biochemical and crystallographic studies of the Met144Ala, Asp92Asn and His254Phe mutants of the nitrite reductase from Alcaligenes xylosoxidans provide insight into the enzyme mechanism [J].

Ellis, MJ ;

Prudêncio, M ;

Dodd, FE ;

Strange, RW ;

Sawers, G ;

Eady, RR ;

Hasnain, SS .

JOURNAL OF MOLECULAR BIOLOGY, 2002, 316 (01) :51-64

[7] Met144A1a mutation of the copper-containing nitrite reductase from Alcaligenes xylosoxidans reverses the intramolecular electron transfer [J].

Farver, O ;

Eady, RR ;

Sawers, G ;

Prudêncio, M ;

Pecht, I .

FEBS LETTERS, 2004, 561 (1-3) :173-176

[8]

Hough MA, 2001, ACTA CRYSTALLOGR D, V57, P355, DOI 10.1107/S0907444900010156

[9] Characterization and function of Met150Gln mutant of copper-containing nitrite reductase from Achromobacter cycloclastes IAM1013 [J].

Kataoka, K ;

Yamaguchi, K ;

Sakai, S ;

Takagi, K ;

Suzuki, S .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2003, 303 (02) :519-524

[10] Spectroscopic and electrochemical properties of the Met86Gln mutant of Achromobacter cycloclastes pseudoazurin [J].

Kataoka, K ;

Kondo, A ;

Yamaguchi, K ;

Suzuki, S .

JOURNAL OF INORGANIC BIOCHEMISTRY, 2000, 82 (1-4) :79-84

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