The copper chelator methanobactin from Methylosinus trichosporium OB3b binds copper(I) |
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Authors: | Hakemian Amanda S Tinberg Christine E Kondapalli Kalyan C Telser Joshua Hoffman Brian M Stemmler Timothy L Rosenzweig Amy C |
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Institution: | Department of Biochemistry, Northwestern University, Evanston, Illinois 60208, USA. |
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Abstract: | 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). |
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