Electrochemical interaction of Shewanella oneidensis MR-1 and its outer membrane cytochromes OmcA and MtrC with hematite electrodes |
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| Authors: | Leisa A Meitl Carrick M Eggleston Patricia JS Colberg Nidhi Khare Catherine L Reardon Liang Shi |
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| Institution: | aDepartment of Geology and Geophysics, University of Wyoming, Laramie, WY 82071, USA;bDepartment of Civil and Architectural Engineering, University of Wyoming, Laramie, WY 82071, USA;cMicrobiology Group, Pacific Northwest National Laboratory, P.O. Box 999, MSIN: P7-50, Richland, WA 99354, USA |
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| Abstract: | Bacterial metal reduction is an important biogeochemical process in anaerobic environments. An understanding of electron transfer pathways from dissimilatory metal-reducing bacteria (DMRB) to solid phase metal (hydr)oxides is important for understanding metal redox cycling in soils and sediments, for utilizing DMRB in bioremedation, and for developing technologies such as microbial fuel cells. Here we hypothesize that the outer membrane cytochromes OmcA and MtrC from Shewanella oneidensis MR-1 are the only terminal reductases capable of direct electron transfer to a hematite working electrode. Cyclic voltammetry (CV) was used to study electron transfer between hematite electrodes and protein films, S. oneidensis MR-1 wild-type cell suspensions, and cytochrome deletion mutants. After controlling for hematite electrode dissolution at negative potential, the midpoint potentials of adsorbed OmcA and MtrC were measured (−201 mV and −163 mV vs. Ag/AgCl, respectively). Cell suspensions of wild-type MR-1, deletion mutants deficient in OmcA (ΔomcA), MtrC (ΔmtrC), and both OmcA and MtrC (ΔmtrC–ΔomcA) were also studied; voltammograms for ΔmtrC–ΔomcA were indistinguishable from the control. When the control was subtracted from the single deletion mutant voltammograms, redox peaks were consistent with the present cytochrome (i.e., ΔomcA consistent with MtrC and ΔmtrC consistent with OmcA). The results indicate that OmcA and MtrC are capable of direct electron exchange with hematite electrodes, consistent with a role as terminal reductases in the S. oneidensis MR-1 anaerobic respiratory pathway involving ferric minerals. There was no evidence for other terminal reductases operating under the conditions investigated. A Marcus-based approach to electron transfer kinetics indicated that the rate constant for electron transfer ket varies from 0.025 s−1 in the absence of a barrier to 63.5 s−1 with a 0.2 eV barrier. |
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