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

Amanda S. Hakemian; Christine E. Tinberg; Kalyan C. Kondapalli; Joshua Telser; Brian M. Hoffman; Timothy L. Stemmler; Amy C. Rosenzweig

doi:10.1021/ja0558140

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

Amanda S. Hakemian, Christine E. Tinberg, Kalyan C. Kondapalli, Joshua Telser, Brian M. Hoffman, Timothy L. Stemmler^*, Amy C. Rosenzweig

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

51 Scopus citations

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).

Original language	English (US)
Pages (from-to)	17142-17143
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	127
Issue number	49
DOIs	https://doi.org/10.1021/ja0558140
State	Published - Dec 14 2005

Funding

ASJC Scopus subject areas

General Chemistry
Biochemistry
Catalysis
Colloid and Surface Chemistry

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title = "The copper chelator methanobactin from Methylosinus trichosporium OB3b binds copper(I)",

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).",

author = "Hakemian, {Amanda S.} and Tinberg, {Christine E.} and Kondapalli, {Kalyan C.} and Joshua Telser and Hoffman, {Brian M.} and Stemmler, {Timothy L.} and Rosenzweig, {Amy C.}",

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T1 - The copper chelator methanobactin from Methylosinus trichosporium OB3b binds copper(I)

AU - Hakemian, Amanda S.

AU - Tinberg, Christine E.

AU - Kondapalli, Kalyan C.

AU - Telser, Joshua

AU - Hoffman, Brian M.

AU - Stemmler, Timothy L.

AU - Rosenzweig, Amy C.

PY - 2005/12/14

Y1 - 2005/12/14

N2 - 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).

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

Abstract

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