biostudies-literatureHakemian ASNIDDK NIH HHSNHLBI NIH HHSNIGMS NIH HHS17142-3https://www.ebi.ac.uk/biostudies/studies/S-EPMC2864604biostudies-literatureUnknown127(49)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).Journal of the American Chemical SocietyThe copper chelator methanobactin from Methylosinus trichosporium OB3b binds copper(I).PMC2864604DK068139R01 HL013531GM070473R01 GM070473HL13531R01 DK068139R01 DK068139-01A1Stemmler TLHakemian ASTelser JHoffman BMRosenzweig ACTinberg CEKondapalli KCfalseThe copper chelator methanobactin from Methylosinus trichosporium OB3b binds copper(I).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).2005-01-01T00:00:00Z2005 Dec2024-11-06T00:43:03.472Z2019-03-26T23:28:37ZS-EPMC28646041633203510.1021/ja0558140