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Methanobactin : ウィキペディア英語版 | Methanobactin
Methanobactin (mb) is a class of Mcopper-binding and reducing uchromophoric peptides initially identified in the methanotroph ''Methylococcus capsulatus'' Bath - and later in ''Methylosinus trichosporium'' OB3b - during the isolation of the membrane-associated or particulate methane monooxygenase (pMMO). 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. Additionally, methanobactin can reduce Cu(II), which is toxic to cells, to Cu(I), the form used in pMMO.〔(Amanda S. Hakemian, ''et al.'' "The Copper Chelator Methanobactin from Methylosinus trichosporium OB3b Binds Copper(I)" ''Journal of the American Chemical Society'' 2005, 127 (49), 17142-17143 )〕 Moreover, different species of methanobactin are hypothesized to be ubiquitous within the biosphere, especially in light of the discovery of molecules produced by other type II methanotrophs that similarly bind and reduce copper (II) to copper (I).〔 == Strains of Methanobactin ==
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