Voltammetry of dehaloperoxidase on self-assembled monolayers: Reversible adsorptive immobilization of a globin
Voltammetry of dehaloperoxidase on self-assembled monolayers: Reversible adsorptive immobilization of a globin
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DOI：
10.1016/j.elecom.2012.10.011
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发表时间：
2013-01-01
影响因子：
5.4
通讯作者：
Bowden, Edmond F.
中科院分区：
文献类型：
--
作者：
D'Antonio, Edward L.;Chen, Thomas K.;Bowden, Edmond F.
在低离子强度条件下，将单体血红蛋白去卤过氧化物酶（DHP）吸附在羟基端和羧基端烷基硫醇组成的二元自组装单层膜上。其Fe(III)/Fe（II）反应的伏安法表明吸附的DHP在厌氧和好氧条件下都具有电活性和天然性。通过伏安解吸/再吸附实验确定了吸附固定的化学可逆性质。电活性表面浓度的循环伏安测定揭示了一种不寻常的反扫描速率依赖关系，这种依赖关系通过Hoffman的动态对接电子转移模型得到了合理化。Liang et al.， J. Am。化学。社会科学学报，2004(3):387。这一结果代表了电化学环境下蛋白质电子转移动态对接控制的第一个证据。(C) 2012 Elsevier B.V.版权所有
Dehaloperoxidase (DHP), a monomeric hemoglobin, was adsorptively immobilized under low ionic strength conditions on binary self-assembled monolayers composed of OH- and COOH-terminated alkylthiols. Voltammetry of its Fe(III)/Fe(II) reactions revealed adsorbed DHP to be electroactive and native under both anaerobic and aerobic conditions. The chemically reversible nature of the adsorptive immobilization was established from voltammetric desorption/re-adsorption experiments. Cyclic voltammetric determination of electroactive surface concentration uncovered an unusual inverse scan rate dependence that was rationalized by means of Hoffman's dynamic docking electron transfer model [Z.-X. Liang et al., J. Am. Chem. Soc. 126 (2004) 2785]. This result represents the first evidence for dynamic docking control of protein electron transfer in an electrochemical setting. (C) 2012 Elsevier B.V. All rights reserved.