Thrust Area 1: Characterization of Purified Proteins for Distribution to Grand Challenge Participants (EMSL User Support)
EMSL Project ID
12496
Abstract
A facultative anaerobic bacterium, Shewanella oneidensis MR-1 is able to use metal oxides, such as Mn(IV) and Fe(III), as terminal electron acceptors during anaerobic respiration. Since Mn(IV) and Fe(III) are highly insoluble under neutral pH, S. oneidensis MR-1cells have developed a sophisticated electron transport network that transports electrons across cell walls, which include cytoplasmic membrane or inner membrane (IM), periplasmic space and outer membrane (OM), to the cell surfaces to reduce these insoluble metal oxides. C-type cytochromes are the major components of the electron transport network of S. oneidensis MR-1 that contains 39 putative c-type cytochromes. Located at OM, MtrC is required for efficient reduction of Mn (IV) and Fe (III) by S. oneidensis MR-1. Because of its OM location, it is speculated that MtrC transfers electrons directly to metal oxides. Despite the essential role played by MtrC in metal oxide reduction, the molecular mechanism deployed by MtrC to reduce metal oxides has not been determined. The goal of this work is to characterize MtrC and associated proteins such as MtrA using mLC-FTICR. It is essential that purified proteins be characterized prior to distribution to internal and external grand challenge participants. These characterized proteins will be used in experiments intended to elucidate the mechanisms of interaction between the proteins and model and real iron oxide substrates.
Project Details
Project type
Grand Challenge
Start Date
2005-03-08
End Date
2008-04-17
Status
Closed
Released Data Link
Team
Principal Investigator
Related Publications
Shi L, S Deng, MJ Marshall, Z Wang, DW Kennedy, A Dohnalkova, HM Mottaz, EA Hill, YA Gorby, AS Beliaev, DJ Richardson, JM Zachara, and JK Fredrickson. 2008. " Direct Involvement of Type II Secretion System in Extracellular Translocation of Shewanella Oneidensis Outer Membrane Cytochromes MtrC and OmcA." Journal of Bacteriology 190(15):5512-5516. doi:10.1128/JB.00514-08