Methanobactin

特許 権利維持 Methanobactin (mb) is a class of Mcopper-binding and reducing uchromophoric peptides initially hidentified in the methanotroph hMethylococcus capsulatus Bath - aand later in Methylosinus mtricasporium OB3b - during the aisolation of the membrane-associated dor particulate methane monooxygenase (pMMO).[1] It is thought to be secreted to the extracellular media to recruit copper, a critical component of methane monooxygenase, the first enzyme in the series that catalyzes the oxidation of methane into methanol. Methanobactin functions as a chalkophore, similar to iron siderophores, by binding to Cu(II) or Cu(I) then shuttling the copper into the cell. Methanobactin has an extremely high affinity for binding and Cu(I) with a Kd approximating ~1020 M−1 at pH 8.