A Solid-State Protein Junction Serves as a Bias-Induced Current Switch
A Solid-State Protein Junction Serves as a Bias-Induced Current Switch
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DOI：
10.1002/anie.201906032
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发表时间：
2019-07-25
影响因子：
16.6
通讯作者：
Cahen, David
中科院分区：
文献类型：
--
作者：
Fereiro, Jerry A.;Kayser, Ben;Cahen, David
样品型蛋白质单层可以作为实用设备的垫脚石，可以作为电驱动开关。这一壮举是使用氧化还原蛋白质，细胞色素C（CytC），其血红素屏蔽与固态电极直接接触。对CytC-Au结构进行的从头算DFT计算表明，血红素（蛋白质前沿轨道的起源）与电极的耦合足够弱，可以防止费米能级钉扎。因此，外部偏压可以使这些轨道与电极共振或不共振。使用细胞色素C突变体进行直接S-Au键合，大约80%的Au-CytC-Au结在大于0.5 V的偏压下显示出明显的电导峰，与共振隧穿一致。开关变化持续到室温，证明了蛋白质集合体的可逆的、偏压控制的开关，其具有内置的冗余，为基于蛋白质的生物电子学提供了一条现实的道路。
A sample-type protein monolayer, that can be a stepping stone to practical devices, can behave as an electrically driven switch. This feat is achieved using a redox protein, cytochrome C (CytC), with its heme shielded from direct contact with the solid-state electrodes. Ab initio DFT calculations, carried out on the CytC-Au structure, show that the coupling of the heme, the origin of the protein frontier orbitals, to the electrodes is sufficiently weak to prevent Fermi level pinning. Thus, external bias can bring these orbitals in and out of resonance with the electrode. Using a cytochrome C mutant for direct S-Au bonding, approximately 80 % of the Au-CytC-Au junctions show at greater than 0.5 V bias a clear conductance peak, consistent with resonant tunneling. The on-off change persists up to room temperature, demonstrating reversible, bias-controlled switching of a protein ensemble, which, with its built-in redundancy, provides a realistic path to protein-based bioelectronics.