Elucidating Film Loss and the Role of Hydrogen Bonding of Adsorbed Redox Enzymes by Electrochemical Quartz Crystal Microbalance Analysis.
Elucidating Film Loss and the Role of Hydrogen Bonding of Adsorbed Redox Enzymes by Electrochemical Quartz Crystal Microbalance Analysis.
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DOI：
10.1021/acscatal.1c04317
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发表时间：
2022-02-04
期刊：
影响因子：
12.9
通讯作者：
Reisner, Erwin
中科院分区：
文献类型：
--
作者：
Badiani, Vivek M.;Cobb, Samuel J.;Wagner, Andreas;Oliveira, Ana Rita;Zacarias, Sonia;Pereira, Ines A. C.;Reisner, Erwin
关键词：
将氧化还原酶固定在电极上能够有效和选择性地电催化有用的反应，例如分别用氢化酶（H2酶）和甲酸脱氢酶（FDH）将二氢（H2）可逆地相互转化为质子（H+）和将甲酸盐可逆地相互转化为二氧化碳（CO2）。然而，它们固定在电极上以产生电活性蛋白质膜用于蛋白质-电极界面处的直接电子转移（DET）尚不清楚，并且它们的活性损失的原因仍然模糊，将它们的性能限制在小时的时间尺度。在这里，我们报告的固定化[NiFeSe]-H2 ase和[W]-FDH脱硫弧菌的vulgaris Hildenborough的一系列带电和中性的自组装单层（SAM）修饰的金电极与不同的氢键（H-键）供体的能力。利用蛋白膜伏安法（PFV）、计时电流法（CA）和电化学石英晶体微天平（E-QCM）分析确定了影响固定化酶活性和稳定性的关键因素。静电和氢键相互作用的解决，与静电相互作用负责酶的方向，而酶的解吸是强烈限制当氢键存在于酶电极界面。相反，酶的稳定性大大降低，在H-键合的情况下，解吸酶的损失被确认为活性衰减的主要原因，通过E-QCM在CA。这项研究提供了深入了解固定化氧化还原酶的活性降低的可能原因和膜损失的作用，特别是H-键合，在稳定生物电极的性能，促进未来的生物电催化的改进途径。
The immobilization of redox enzymes on electrodes enables the efficient and selective electrocatalysis of useful reactions such as the reversible interconversion of dihydrogen (H2) to protons (H+) and formate to carbon dioxide (CO2) with hydrogenase (H2ase) and formate dehydrogenase (FDH), respectively. However, their immobilization on electrodes to produce electroactive protein films for direct electron transfer (DET) at the protein–electrode interface is not well understood, and the reasons for their activity loss remain vague, limiting their performance often to hour timescales. Here, we report the immobilization of [NiFeSe]-H2ase and [W]-FDH from Desulfovibrio vulgaris Hildenborough on a range of charged and neutral self-assembled monolayer (SAM)-modified gold electrodes with varying hydrogen bond (H-bond) donor capabilities. The key factors dominating the activity and stability of the immobilized enzymes are determined using protein film voltammetry (PFV), chronoamperometry (CA), and electrochemical quartz crystal microbalance (E-QCM) analysis. Electrostatic and H-bonding interactions are resolved, with electrostatic interactions responsible for enzyme orientation while enzyme desorption is strongly limited when H-bonding is present at the enzyme–electrode interface. Conversely, enzyme stability is drastically reduced in the absence of H-bonding, and desorptive enzyme loss is confirmed as the main reason for activity decay by E-QCM during CA. This study provides insights into the possible reasons for the reduced activity of immobilized redox enzymes and the role of film loss, particularly H-bonding, in stabilizing bioelectrode performance, promoting avenues for future improvements in bioelectrocatalysis.
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DOI：
10.1002/anie.201805027
发表时间：
2018-08-13
期刊：
Angewandte Chemie (International ed. in English)
影响因子：
--
作者：
Nam DH;Zhang JZ;Andrei V;Kornienko N;Heidary N;Wagner A;Nakanishi K;Sokol KP;Slater B;Zebger I;Hofmann S;Fontecilla-Camps JC;Park CB;Reisner E
通讯作者：
Reisner E
影响因子：
3.9
作者：
Gutierrez-Sanchez, Cristina;Olea, David;De Lacey, Antonio L.
通讯作者：
De Lacey, Antonio L.
影响因子：
15
作者：
Fourmond, Vincent;Infossi, Pascale;Leger, Christophe
通讯作者：
Leger, Christophe
影响因子：
9.5
作者：
Alvarez-Malmagro J;Oliveira AR;Gutiérrez-Sánchez C;Villajos B;Pereira IAC;Vélez M;Pita M;De Lacey AL
通讯作者：
De Lacey AL
影响因子：
3.9
作者：
Gao, W;Dickinson, L;Reven, L
通讯作者：
Reven, L