Biological Sciences Division
Cytochrome Studies Provide Biofuel Cell Potential
Electrical charge measurements may point way to miniature biofuel cell development
Results: Researchers from Pacific Northwest National Laboratory (PNNL) and collaborators from the U.S. Department of Energy's (DOE's) Biogeochemistry Grand Challenge have purified the protein called outer membrane cytochrome A (OmcA) from Shewanella oneidensis, a bacterium with promise for bioremediation of contaminants and the design of microbial fuel cells. They have measured its ability to bind and transfer electrons to mineral hematite, a solid ferric oxide. The team has shown that purified OmcA can directly reduce solid metals and that purified proteins are a next step in biofuel cell development. The work appeared in the Journal of the American Chemical Society.
Why it matters: Purified proteins could funnel the electrons right into a surface of a conductor, providing the first step to building a biofuel cell—using just proteins, not live cells. Bio-cells use enzymes to oxidize reduced materials in the cells and release electrons. An optimal enzyme system would directly transfer electrons captured from a chemical reaction to an electrode surface—ideally, to use enzymes immobilized on the surface of an electrode. Lack of a membrane permits miniaturization for use in biomedicine or other remote applications where self-sustaining systems are needed.
Methods: PNNL staff scientist Liang Shi devised a new protein expression system that enabled the team to isolate sufficient amounts of protein. The researchers used the techniques, such as fluorescent correlation spectroscopy and confocal microscopy, for measurements of protein-mineral binding. These yielded a "fluorescence intensity trace" whose brightness depended entirely on whether hematite was available to bind with OmcA in solution. No hematite, dim; hematite, bright. In addition to binding, they also detected direct electron transfer from OmcA to the hematite.
Next Steps: Using pure protein opens up the possibility of shrinking biofuel cells to power small electronic devices, according to senior author Thomas Squier. Whole-organism biofuel cells require engineers to design a space-adding membrane that prevents unwanted reactions between fuel, the charge-transporting agent and the electron-accepting metal, the latter being the electrode that carries the electricity to the device. In purified protein fuel cells, the seal made by the protein coating on the electrode effectively acts in place of the membrane.
Research team: Yijia Xiong and Liang Shi (lead investigators), Baowei Chen, Uljana Mayer, Brian Lower, Jim Fredrickson, and Thomas Squier, PNNL; Yuri Londer, Argonne National Laboratory; and Saumyaditya Bose and Michael Hochella, Virginia Polytechnic Institute.
SELF-SEALING BIOCELL: Artist's depiction of purified, electrified bacterial cell outer membrane protein binding with and passing electrons to the iron-rich mineral hematite. In this purified-protein fuel cell, the seal made by the protein coating on the electrode effectively acts in place of a membrane necessary in whole-organism biofuel cells. Eliminating the membrane could aid the design of bioreactors to power small electronic devices.
Source: "High-affinity binding and direct electron transfer to solid metals by the Shewanella oneidensis MR-1 outer membrane c-type cytochrome OmcA." 2006. Journal of the American Chemical Society 128(43):13978-13979 available online. Authors: Xiong Y, L Shi, B Chen, MU Mayer, BH Lower, Y Londer, S Bose, MF Hochella, JK Fredrickson, and TC Squier.
Sponsors: DOE's Office of Biological and Environmental Research's Genomics: GTL program and Biogeochemistry Grand Challenge at PNNL.
See news release "Biofuel cells without the bio cells."