The copper chelator methanobactin from Methylosinus trichosporium OB3b binds copper(I)
The copper chelator methanobactin from Methylosinus trichosporium OB3b binds copper(I)
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DOI:
10.1021/ja0558140
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发表时间:
2005-12-14
影响因子:
15
通讯作者:
Rosenzweig, AC
中科院分区:
文献类型:
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作者:
Hakemian, AS;Tinberg, CE;Rosenzweig, AC
The oxidation state of copper bound to methanobactin, a small siderophore-like molecule from the methanotrophMethylosinustrichosporiumOB3b, 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 thatM.trichosporiumOB3b methanobactin binds Cu(I) and suggest that methanobactin itself reduces Cu(II) to Cu(I).