@article {446,
	title = {Alignment of the c-type cytochrome OmcS along pili of Geobacter sulfurreducens.},
	journal = {Appl Environ Microbiol},
	volume = {76},
	year = {2010},
	month = {2010 Jun},
	pages = {4080-4},
	abstract = {Immunogold localization revealed that OmcS, a cytochrome that is required for Fe(III) oxide reduction by Geobacter sulfurreducens, was localized along the pili. The apparent spacing between OmcS molecules suggests that OmcS facilitates electron transfer from pili to Fe(III) oxides rather than promoting electron conduction along the length of the pili.},
	keywords = {Cytochromes c, Ferric Compounds, Fimbriae, Bacterial, Geobacter, Immunohistochemistry, Microscopy, Immunoelectron},
	issn = {1098-5336},
	doi = {10.1128/AEM.00023-10},
	author = {Leang, Ching and Qian, Xinlei and Mester, T{\"u}nde and Lovley, Derek R}
}
@article {496,
	title = {Evidence that OmcB and OmpB of Geobacter sulfurreducens are outer membrane surface proteins.},
	journal = {FEMS Microbiol Lett},
	volume = {277},
	year = {2007},
	month = {2007 Dec},
	pages = {21-7},
	abstract = {The c-type cytochrome (OmcB) and the multicopper protein (OmpB) required for Fe(III) oxide reduction by Geobacter sulfurreducens were predicted previously to be outer membrane proteins, but it is not clear whether they are positioned in a manner that permits the interaction with Fe(III). Treatment of whole cells with proteinase K inhibited Fe(III) reduction, but had no impact on the inner membrane-associated fumarate reduction. OmcB was digested by protease, resulting in a smaller peptide. However, immunogold labeling coupled with transmission electron microscopy did not detect OmcB, suggesting that it is only partially exposed on the cell surface. In contrast, OmpB was completely digested with 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 of a protein required for optimal Fe(III) citrate reduction at least partially accessible on the cell surface.},
	keywords = {Bacterial Outer Membrane Proteins, Cell Membrane, Cytochromes c, Ferric Compounds, Geobacter, Microscopy, Electron, Transmission, Oxidation-Reduction, Peptide Hydrolases},
	issn = {0378-1097},
	doi = {10.1111/j.1574-6968.2007.00915.x},
	author = {Qian, Xinlei and Reguera, Gemma and Mester, T{\"u}nde and Lovley, Derek R}
}
@article {521,
	title = {Two putative c-type multiheme cytochromes required for the expression of OmcB, an outer membrane protein essential for optimal Fe(III) reduction in Geobacter sulfurreducens.},
	journal = {J Bacteriol},
	volume = {188},
	year = {2006},
	month = {2006 Apr},
	pages = {3138-42},
	abstract = {Deletion of two homologous Geobacter sulfurreducens c-type cytochrome genes, omcG and omcH, decreased the rate of Fe(III) reduction and decreased the level of an outer membrane cytochrome critical for Fe(III) reduction, OmcB, without affecting its transcription. Expression of either gene restored Fe(III) reduction and OmcB expression, suggesting functional similarity.},
	keywords = {Bacterial Outer Membrane Proteins, Bacterial Proteins, Blotting, Northern, Blotting, Western, Cytochromes c, Ferric Compounds, Gene Deletion, Gene Expression, Genes, Bacterial, Geobacter, Oxidation-Reduction, RNA, Bacterial, RNA, Messenger},
	issn = {0021-9193},
	doi = {10.1128/JB.188.8.3138-3142.2006},
	author = {Kim, Byoung-Chan and Qian, Xinlei and Leang, Ching and Coppi, Maddalena V and Lovley, Derek R}
}
