PNAS: Bacterial "antenna" discharges promising new bio-batteries

Recently, scientists have discovered a miniature "antenna" on the cell wall of Serratia (Shewanella oneidensis), using these "antennas" to release excess energy generated by metabolism, to maintain the flow of energy in the cell, thereby maintaining cell vitality. The relevant conclusions were published in the Proceedings of the American Academy of Sciences (PNAS).

PNAS: Bacterial "antenna" discharges promising new bio-batteries

Serratia mainly live in a vacuum environment, they are both pressure-resistant bacteria and low-temperature bacteria. "We can use these bacteria to generate more electricity, and when we understand the discharge process of microorganisms, we can use them to generate electricity better." Tom Clark of the University of East Anglia in the UK said, "These Bacteria can be used to clean up oil spills or uranium contamination. Their 'antenna' structure can inspire scientists to design better electrodes and increase the sensitivity to electric shock. "

Although this kind of bioelectricity is relatively weak and has a short duration of only a few seconds, the new discovery brings hope to the development of bio batteries. Scientists pointed out that it may take more than ten years to develop these bacteria into products. (

doi: 10.1073 / pnas.1017200108



Structure of a bacterial cell surface decaheme electron conduit

Thomas A. Clarkea, Marcus J. Edwardsa, Andrew J. Gatesa, Andrea Halla, Gaye F. Whitea, Justin Bradleya, Catherine L. Reardonb, Liang Shib, Alexander S. Beliaevb, Matthew J. Marshallb, Zheming Wangb, Nicholas J. Watmougha, James K. Fredricksonb, John M. Zacharab, Julea N. Butta, and David J. Richardsona,

Some bacterial species are able to utilize extracellular mineral forms of iron and manganese as respiratory electron acceptors. In Shewanella oneidensis this involves decaheme cytochromes that are located on the bacterial cell surface at the termini of trans-outer-membrane electron transfer conduits. The cell surface cytochromes can potentially play multiple roles in mediating electron transfer directly to insoluble electron sinks, catalyzing electron exchange with flavin electron shuttles or participating in extracellular intercytochrome electron exchange along “nanowire” appendages. We present a 3.2-Å crystal structure of one of these decaheme cytochromes , MtrF, that allows the spatial organization of the 10 hemes to be visualized for the first time. The hemes are organized across four domains in a unique crossed conformation, in which a staggered 65-Å octaheme chain transects the length of the protein and is bisected by a planar 45-Å tetraheme chain that connects two extended Greek key split β-barrel domains. The structure provides molecular insight into how reduction of insoluble substrate (eg, minerals), soluble substrates (eg, flavins), and cytochrome redox partners might be possible in tandem at different termini of a trifurcated electron transport chain on the cell surface.

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