{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hakemian AS"],"funding":["NIDDK NIH HHS","NHLBI NIH HHS","NIGMS NIH HHS"],"pagination":["17142-3"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2864604"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["127(49)"],"pubmed_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)."],"journal":["Journal of the American Chemical Society"],"pubmed_title":["The copper chelator methanobactin from Methylosinus trichosporium OB3b binds copper(I)."],"pmcid":["PMC2864604"],"funding_grant_id":["DK068139","R01 HL013531","GM070473","R01 GM070473","HL13531","R01 DK068139","R01 DK068139-01A1"],"pubmed_authors":["Stemmler TL","Hakemian AS","Telser J","Hoffman BM","Rosenzweig AC","Tinberg CE","Kondapalli KC"],"additional_accession":[]},"is_claimable":false,"name":"The copper chelator methanobactin from Methylosinus trichosporium OB3b binds copper(I).","description":"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).","dates":{"release":"2005-01-01T00:00:00Z","publication":"2005 Dec","modification":"2024-11-06T00:43:03.472Z","creation":"2019-03-26T23:28:37Z"},"accession":"S-EPMC2864604","cross_references":{"pubmed":["16332035"],"doi":["10.1021/ja0558140"]}}