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arXiv 0903.4255cond-mat.mes-hallcond-mat.othercond-mat.soft
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蛋白质作为生物电子材料:固态蛋白质单层结的电子输运

Proteins as Bioelectronic Materials: Electron Transport Through Solid-State, Protein Monolayer Junctions

Izhar Ron, Lior Sepunaro, Stella Izhakov, Noga Friedman, Israel Pecht, Mordechai Sheves, David Cahen

摘要:

蛋白质中的电子传递是许多生物化学反应的基本元素,在溶液中的电子传递已经被深入研究。我们报告的结果,电子输运(ETp)测量跨蛋白质,夹在两个固体电极之间的长期目标的理解在多远的蛋白质特性表示(和可以利用)在这样的配置。虽然迄今为止大多数这样的研究进行了一个或几个分子的交界处,我们提出了高产率,可重复的大面积单层连接的蛋白质从三个不同的家庭:天青蛋白(AZ),蓝铜ET蛋白,细菌视紫红质(bR),膜蛋白质生色团复合物与质子泵功能,和牛血清白蛋白(BSA)的制备。令人惊讶的是,这种结上的电流-电压(I-V)测量,这是高度可重复的,显示Az和bR之间的差异相对较小,即使后者缺乏一个已知的ET功能。穿过Az和bR的ETp比穿过BSA的效率高得多,但对于后者,电流仍然很高,并且衰减系数太低而与相干隧穿不一致。相反,非弹性跳跃,建议占主导地位的ETP在这些结。其他特征如不对称的I-V曲线和不同蛋白质的不同行为可以被视为固态电导中的分子特征。

英文摘要:

Electron transfer (ET) through proteins, a fundamental element of many biochemical reactions, has been studied intensively in solution. We report the results of electron transport (ETp) measurements across proteins, sandwiched between two solid electrodes with a long-range goal of understanding in how far protein properties are expressed (and can be utilized) in such a configuration. While most such studies to date were conducted with one or just a few molecules in the junction, we present the high yield, reproducible preparation of large area monolayer junctions of proteins from three different families: Azurin (Az), a blue-copper ET protein, Bacteriorhodopsin (bR), a membrane protein-chromophore complex with a proton pumping function, and Bovine Serum Albumin (BSA). Surprisingly, the current-voltage (I-V) measurements on such junctions, which are highly reproducible, show relatively minor differences between Az and bR, even though the latter lacks a known ET function. ETp across both Az and bR is much more efficient than across BSA, but also for the latter the currents are still high, and the decay coefficients too low to be consistent with coherent tunneling. Rather, inelastic hopping is proposed to dominate ETp in these junctions. Other features such as asymmetrical I-V curves and distinct behavior of different proteins can be viewed as molecular signatures in the solid-state conductance.

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