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- W2547664102 abstract "Significance Copper is central to the metabolism of methanotrophs, methane-oxidizing bacteria that are of interest because of their potential applications in bioremediation and bioconversion processes. Methanotrophs convert methane to methanol using particulate methane monooxygenase (pMMO), a copper-dependent, membrane-bound enzyme. To fulfill pMMO’s high requirement for copper, methanotrophs secrete and re-internalize methanobactin, a peptide-derived, copper-chelating natural product (CuMbn). Here we characterize the protein machinery used for import and periplasmic transport of CuMbn. These data provide important insights into the molecular mechanisms of CuMbn recognition and handling." @default.
- W2547664102 created "2016-11-11" @default.
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- W2547664102 date "2016-11-02" @default.
- W2547664102 modified "2023-10-14" @default.
- W2547664102 title "Methanobactin transport machinery" @default.
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- W2547664102 doi "https://doi.org/10.1073/pnas.1603578113" @default.
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