Protein Binding and Orientation Matter: Bias-Induced Conductance Switching in a Mutated Azurin Junction.
Protein Binding and Orientation Matter: Bias-Induced Conductance Switching in a Mutated Azurin Junction.
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蛋白质结合和方向物质：突变天青蛋白连接中的偏压诱导电导转换。
DOI：
10.1021/jacs.0c08836
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发表时间：
2020-11-11
影响因子：
15
通讯作者：
Cahen D
中科院分区：
文献类型：
--
作者：
Fereiro JA;Bendikov T;Pecht I;Sheves M;Cahen D
我们通过蓝铜蛋白天青蛋白突变体N42 C Az观察到可逆的，偏压诱导的电导转换，|V|> 0.8 V。对于野生型天青蛋白WT Az，没有发现这样的转换，高达100%。|1.2 V|超过这个范围就会发生不可逆转的变化。当N42 C Az突变体位于固态Au-蛋白质-Au结中的电极之间时，其相对于电极的取向与WT Az的取向相反。通过这两种蛋白质的电流是温度无关的，与量子力学隧穿作为主要的传输机制一致。两种蛋白质在电导和非弹性电子隧穿谱中没有明显的差异，|0.5 V|偏压开关行为持续从15 K到室温。电导峰与系统随着偏压的变化而进入和脱离谐振一致。通过对Au-蛋白质系统进行紫外光电子发射测量的进一步输入，通过使N42 C Az突变体中的Cu（II）配位球的位置靠近蛋白质化学结合的（较大的）基底电极，这些电导的显着差异得到了合理化，而对于WT Az，该配位球最接近另一个Au电极，仅与其进行物理接触。我们的研究结果建立了蛋白质的方向和结合性质的电极在确定电子传输隧道势垒发挥的关键作用。
We observe reversible, bias-induced switching of conductance via a blue copper protein azurin mutant, N42C Az, with a nearly 10-fold increase at |V| > 0.8 V than at lower bias. No such switching is found for wild-type azurin, WT Az, up to |1.2 V|, beyond which irreversible changes occur. The N42C Az mutant will, when positioned between electrodes in a solid-state Au–protein–Au junction, have an orientation opposite that of WT Az with respect to the electrodes. Current(s) via both proteins are temperature-independent, consistent with quantum mechanical tunneling as dominant transport mechanism. No noticeable difference is resolved between the two proteins in conductance and inelastic electron tunneling spectra at <|0.5 V| bias voltages. Switching behavior persists from 15 K up to room temperature. The conductance peak is consistent with the system switching in and out of resonance with the changing bias. With further input from UV photoemission measurements on Au–protein systems, these striking differences in conductance are rationalized by having the location of the Cu(II) coordination sphere in the N42C Az mutant, proximal to the (larger) substrate-electrode, to which the protein is chemically bound, while for the WT Az that coordination sphere is closest to the other Au electrode, with which only physical contact is made. Our results establish the key roles that a protein’s orientation and binding nature to the electrodes play in determining the electron transport tunnel barrier.
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影响因子：
4
作者：
Baldacchini, Chiara;Bizzarri, Anna Rita;Cannistraro, Salvatore
通讯作者：
Cannistraro, Salvatore
DOI：
10.1046/j.1432-1033.2000.01501.x
发表时间：
2000-07-01
期刊：
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子：
--
作者：
Bonander, N;Leckner, J;Sjölin, L
通讯作者：
Sjölin, L
影响因子：
2.4
作者：
Frascerra, V;Calabi, F;Rinaldi, R
通讯作者：
Rinaldi, R
影响因子：
56.9
作者：
Chen, Zibo;Kibler, Ryan D.;Baker, David
通讯作者：
Baker, David
影响因子：
17.1
作者：
Artes, Juan M.;Diez-Perez, Ismael;Gorostiza, Pau
通讯作者：
Gorostiza, Pau