High-affinity binding and direct electron transfer to solid metals by the Shewanella oneidensis MR-1 outer membrane c-type cytochrome OmcA.
High-affinity binding and direct electron transfer to solid metals by the Shewanella oneidensis MR-1 outer membrane c-type cytochrome OmcA.
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DOI：
10.1021/ja063526d
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发表时间：
2006-10
影响因子：
15
通讯作者：
Yijia Xiong;Liang Shi;Baowei Chen;M. Mayer;B. Lower;Y. Londer;Saumyaditya Bose;M. Hochella;J. Fredrickson;T. Squier
中科院分区：
文献类型：
--
作者：
Yijia Xiong;Liang Shi;Baowei Chen;M. Mayer;B. Lower;Y. Londer;Saumyaditya Bose;M. Hochella;J. Fredrickson;T. Squier
纯化的外膜细菌蛋白OmcA与赤铁矿（Fe2O3）表面紧密结合，允许电子直接转移到这种固体矿物上，以约1013电子/cm2/s的电子通量还原Fe （III）。在赤铁矿存在的情况下，与金属还原相关的内部蛋白质运动幅度大幅增加。结合是非常有利的，其分配系数约为2 × 105 (δ ago ' = -28 kJ/mol)，其中每平方厘米约有1014个OmcA蛋白结合到固体金属表面，表明使用纯化的OmcA在构建生物燃料电池中的效用。
The purified outer membrane bacterial protein OmcA binds densely to the surface of hematite (Fe2O3), permitting direct electron transfer to this solid mineral to reduce Fe (III) with an electron flux of about 1013 electrons /cm2/s. In the presence of hematite, there is a substantial increase in the amplitude of internal protein motions that correlate with metal reduction. Binding is highly favorable, with a partition coefficient of approximately 2 x 105 (DeltaGo' = -28 kJ/mol), where approximately 1014 OmcA proteins bind per cm2 to the solid metal surface, indicating the utility of using purified OmcA in the construction of a biofuel cell.