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PNAS:新型生物电池前景可观

来源:EP环保网 2011-09-07 16:34

近日,科学家们在沙雷菌(Shewanella oneidensis)的细胞壁上发现一种微型“天线”,利用这些“天线”释放新陈代谢产生的多余能量,保持能量在细胞中的流动,从而维持细胞活力。相关结论发表在《美国科学院院刊》(PNAS)上。

沙雷菌主要生活在真空环境中,它们既是耐压菌,又是低温菌。“我们可以利用这些细菌产生更多的电,当了解微生物的放电进程时,就可以更好的用它们进行发电。”英国东安格利亚大学(University of East Anglia)汤姆·克拉克称,“这些细菌可以用来清理漏油或铀污染,它们的‘天线’结构,可以启发科学家们设计更好电极,增加触电灵敏性。”

虽然这种生物电电量比较微弱,持续时间短,仅有几秒钟,但是新的发现为生物电池的研发带来了希望,科学家指出要将这些细菌开发成产品可能需要十几年的时间。(生物谷 Bioon.com)

 

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 (e.g., minerals), soluble substrates (e.g., 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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