27 research outputs found

    Bridging the Gap between Sequence and Function

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    Proceedings of the conference on nearrings and nearfierlds

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    Nanomolar Copper Enhances Mercury Methylation by <i>Desulfovibrio desulfuricans</i> ND132

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    Methylmercury (MeHg) is produced by certain anaerobic microorganisms, such as the sulfate-reducing bacterium <i>Desulfovibrio desulfuricans</i> ND132, but environmental factors affecting inorganic mercury [Hg­(II)] uptake and methylation remain unclear. We report that the presence of a small amount of copper ions [Cu­(II), <100 nM] enhances Hg­(II) uptake and methylation by washed cells of ND132, while Hg­(II) methylation is inhibited at higher Cu­(II) concentrations because of the toxicity of copper to the microorganism. The enhancement or inhibitory effect of Cu­(II) is dependent on both time and concentration. The presence of nanomolar concentrations of Cu­(II) facilitates rapid uptake of Hg­(II) (within minutes) and doubles MeHg production within a 24 h period, but micromolar concentrations of Cu­(II) completely inhibit Hg­(II) methylation. Metal ions such as zinc [Zn­(II)] and nickel [Ni­(II)] also inhibit but do not enhance Hg­(II) methylation under the same experimental conditions. These observations suggest a synergistic effect of Cu­(II) on Hg­(II) uptake and methylation, possibly facilitated by copper transporters or metallochaperones in this organism, and highlight the fact that complex environmental factors affect MeHg production in the environment

    Global Proteome Response to Deletion of Genes Related to Mercury Methylation and Dissimilatory Metal Reduction Reveals Changes in Respiratory Metabolism in <i>Geobacter sulfurreducens</i> PCA

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    <i>Geobacter sulfurreducens</i> PCA can reduce, sorb, and methylate mercury (Hg); however, the underlying biochemical mechanisms of these processes and interdependent metabolic pathways remain unknown. In this study, shotgun proteomics was used to compare global proteome profiles between wild-type <i>G. sulfurreducens</i> PCA and two mutant strains: a Δ<i>hgcAB</i> mutant, which is deficient in two genes known to be essential for Hg methylation and a Δ<i>omcBESTZ</i> mutant, which is deficient in five outer membrane <i>c</i>-type cytochromes and thus impaired in its ability for dissimilatory metal ion reduction. We were able to delineate the global response of <i>G. sulfurreducens</i> PCA in both mutants and identify cellular networks and metabolic pathways that were affected by the loss of these genes. Deletion of <i>hgcAB</i> increased the relative abundances of proteins implicated in extracellular electron transfer, including most of the <i>c</i>-type cytochromes, PilA-C, and OmpB, and is consistent with a previously observed increase in Hg reduction in the Δ<i>hgcAB</i> mutant. Deletion of <i>omcBESTZ</i> was found to significantly increase relative abundances of various methyltransferases, suggesting that a loss of dissimilatory reduction capacity results in elevated activity among one-carbon (C1) metabolic pathways and thus increased methylation. We show that <i>G. sulfurreducens</i> PCA encodes only the folate branch of the acetyl-CoA pathway, and proteins associated with the folate branch were found at lower abundance in the Δ<i>hgcAB</i> mutant strain than the wild type. This observation supports the hypothesis that the function of HgcA and HgcB is linked to C1 metabolism through the folate branch of the acetyl-CoA pathway by providing methyl groups required for Hg methylation
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