The copper chelator methanobactin from Methylosinus trichosporium OB3b binds copper(I)

被引：54

作者：

Hakemian, AS

Tinberg, CE

Kondapalli, KC

Telser, J

Hoffman, BM

Stemmler, TL ^{[1
]}

Rosenzweig, AC

机构：

[1] Wayne State Univ, Sch Med, Dept Biochem & Mol Biol, Detroit, MI 48201 USA

[2] Northwestern Univ, Dept Biochem, Evanston, IL 60208 USA

[3] Northwestern Univ, Dept Mol Biol, Evanston, IL 60208 USA

[4] Northwestern Univ, Dept Cell Biol, Evanston, IL 60208 USA

[5] Northwestern Univ, Dept Chem, Evanston, IL 60208 USA

[6] Roosevelt Univ, Dept Chem Biol & Phys Sci, Chicago, IL 60605 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2005年 / 127卷 / 49期

关键词：

D O I：

10.1021/ja0558140

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The oxidation state of copper bound to methanobactin, a small siderophore-like molecule from the methanotroph Methylosinus trichosporium OB3b, was investigated. Purified methanobactin loaded with Cu(II) exhibits a weak EPR signal probably due to adventitious Cu(II). The EPR signal intensity increases significantly upon addition of the strong oxidant nitric acid. Features of the X-ray absorption near edge spectrum, including a 1s → 4p transition at 8985 eV, further indicate the presence of Cu(I). EXAFS data were best fit using a multiple scattering model generated from previously reported crystallographic parameters. These results establish definitively that M. trichosporium OB3b methanobactin binds Cu(I) and suggest that methanobactin itself reduces Cu(II) to Cu(I). Copyright © 2005 American Chemical Society.

引用

页码：17142 / 17143

页数：2

共 21 条

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