Copper methanobactin: a molecule whose time has come - PubMed (original) (raw)

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Copper methanobactin: a molecule whose time has come

Ramakrishnan Balasubramanian et al. Curr Opin Chem Biol. 2008 Apr.

Abstract

Copper plays a key role in the physiology of methanotrophs. One way that these bacteria meet their high copper requirement is by the biosynthesis and release of high affinity copper binding compounds called methanobactins. Recent advances in methanobactin characterization include the first crystal structure, detailed spectroscopic analyses, and studies of metal ion specificity. Methanobactin may function in copper uptake, regulation of methane monooxygenase expression, protection against copper toxicity, and particulate methane monooxygenase activity. Methanobactin can extract copper from insoluble minerals and could be important for mineral weathering. Many methanobactin properties are reminiscent of iron siderophores, suggesting a similar mechanism of handling. Methanobactin-like compounds have also been identified in yeast mitochondria, suggesting that these molecules are a more universal phenomenon.

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Figures

Figure 1

Figure 1

Structure of Cu-mb from M. trichosporium OB3b. (A) Schematic diagram. (B) Ball-and-stick representation of crystal structure (Cambridge Crystallographic Data Center deposition number CCDC 241254). The copper ion is shown as a brown sphere.

Figure 2

Figure 2

Possible functions of Cu-mb and proposed mechanism of uptake: mb is involved in extracellular copper uptake and is postulated to protect the cells from ROS. Cu-mb in the periplasmic space may be involved in pMMO catalytic activity. In the cytoplasm, Cu-mb may participate in the copper-dependent regulation of MMOs. Cu-mb may be recognized and internalized by integral outer membrane (OM) TonB receptors, inner membrane (IM) embedded TonB-ExbB-ExbD proteins, and ABC transporters.

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