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Disease relevance of Desulfuromonas


High impact information on Desulfuromonas

  • Unlike the two c(7) molecules with known structures, one from G. sulfurreducens (PpcA) and one from Desulfuromonas acetoxidans where all three hemes are bishistidine coordinated, this domain contains a heme which is coordinated by a methionine and a histidine residue [4].
  • Tenax-TA, a solid-phase sorbent, was used as an alternative to hexadecane for continuous delivery of tetrachloroethene (PCE) to Desulfuromonas strain BB1, a chloro-respiring microorganism [5].
  • One chloroethene-contaminated aquifer tested positive with the Dehalococcoides-targeted primers, and another contaminated aquifer tested positive with the Desulfuromonas dechlorinator-targeted primer pair [6].
  • Hydrogenases, which are ubiquitous in sulfate-reducing bacteria, were previously thought to be absent from Desulfuromonas acetoxidans [7].
  • Desulfuromonas palmitatis sp. nov., a marine dissimilatory Fe(III) reducer that can oxidize long-chain fatty acids [8].

Chemical compound and disease context of Desulfuromonas


Gene context of Desulfuromonas


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  4. Structure of a novel c7-type three-heme cytochrome domain from a multidomain cytochrome c polymer. Pokkuluri, P.R., Londer, Y.Y., Duke, N.E., Erickson, J., Pessanha, M., Salgueiro, C.A., Schiffer, M. Protein Sci. (2004) [Pubmed]
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  6. 16S rRNA gene-based detection of tetrachloroethene-dechlorinating Desulfuromonas and Dehalococcoides species. Löffler, F.E., Sun, Q., Li, J., Tiedje, J.M. Appl. Environ. Microbiol. (2000) [Pubmed]
  7. First evidence for the presence of a hydrogenase in the sulfur-reducing bacterium Desulfuromonas acetoxidans. Brugna, M., Nitschke, W., Toci, R., Bruschi, M., Giudici-Orticoni, M.T. J. Bacteriol. (1999) [Pubmed]
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