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Investigation Of Fe(III) Reduction In Geobacter Sulfurreducens: Characterization Of Outer Surface Associated Electron Transfer Components.
Published 2009 · Chemistry
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The c-type cytochrome (OmcB) and the multicopper protein (OmpB) required for Fe(III) oxide reduction by G. sulfurreducens were previously predicted to be outer membrane proteins, but it is not clear whether they are positioned in a manner that permits interaction with Fe(III). Treatment of whole cells with proteinase K inhibited Fe(III) reduction, but had no impact on inner membrane-associated fumarate reduction. OmcB was digested by the protease, resulting in a smaller peptide. However, immunogold labeling coupled with transmission electron microscopy (TEM) did not detect OmcB, suggesting that is only partially exposed on the cell surface. In contrast, OmpB was completely digested by the protease. OmpB was loosely associated with the cell surface, as a substantial portion of it was recovered in the culture supernatant. Immunogold labeling demonstrated that OmpB associated with the cell was evenly distributed on the cell surface rather than localized to one side of the cell like the conductive pili. Although several proteins required for Fe(III) oxide reduction are shown to be exposed on the outer surface of G. sulfurreducens, the finding that OmcB is also surface-exposed is the first report that a protein required for optimal Fe(III) citrate reduction is at least partially accessible on the cell surface.
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