Direct electrochemistry of the decaheme cytochrome, MtrA, from Shewanella oneidensis MR-1

BIOL 194

Mackenzie A. Firer-Sherwood, mafs@bu.edu and Sean J. Elliott. Department of Chemistry, Boston University, 24 Cummington St., Boston, MA 02215
Shewanella oneidensis MR-1 is a gram-negative microbe than can grow both aerobically and anaerobically using an assortment of terminal electron acceptors in the absence of oxygen. The anaerobic respiratory versatility of S. oneidensis is likely the result of an intricate electron transfer pathway involving many redox-active proteins, which include c-type cytochromes. MtrA, a periplasmic decaheme c-type cytochrome from S. oneidensis, is believed to be a component of the electron transport chain that leads to Fe(III) reduction. At this point, the process by which electrons are transferred to and from MtrA is unknown. Here we report the purification of MtrA, and characterization of the protein as a decaheme cytochrome amendable to protein film voltammetry (PFV). Initial characterization of MtrA by PFV has revealed a broad envelope indicative of redox cofactors of overlapping potentials.
 

Frontiers in Chemical Biology
5:00 PM-7:00 PM, Wednesday, August 22, 2007 BCEC -- Exhibit Hall - B2, Poster

Division of Biological Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007