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首页> 外文期刊>Chemistry: A European journal >Surface-Tuned Electron Transfer and Electrocatalysis of Hexameric Tyrosine-Coordinated Heme Protein
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Surface-Tuned Electron Transfer and Electrocatalysis of Hexameric Tyrosine-Coordinated Heme Protein

机译：六聚酪氨酸配位的血红素蛋白的表面调谐电子转移和电催化

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摘要

Molecular modeling, electrochemical methods, and quartz crystal microbalance were used to characterize immobilized hexameric tyrosine-coordinated heme protein (HTHP) on bare carbon or on gold electrodes modified with positively and negatively charged self-assembled monolayers (SAMs), respectively. HTHP binds to the positively charged surface but no direct electron transfer (DET) is found due to the long distance of the active sites from the electrode surfaces. At carboxyl-terminated surfaces, the neutrally charged bottom of HTHP can bind to the SAM. For this "disc" orientation all six hemes are close to the electrode and their direct electron transfer should be efficient. HTHP on all negatively charged SAMs showed a quasi-reversible redox behavior with rate constant k(s) values between 0.93 and 2.86 s(-1) and apparent formal potentials E-app(0)' between -131.1 and -249.1 mV. On the MUA/MU-modified electrode, the maximum surface concentration corresponds to a complete monolayer of the hexameric HTHP in the disc orientation. HTHP electrostatically immobilized on negatively charged SAMs shows electrocatalysis of peroxide reduction and enzymatic oxidation of NADH.
机译：分子模型，电化学方法和石英晶体微量天平用于表征固定的六聚酪氨酸配位的血红素蛋白（HTHP）在裸碳上或在带正电和负电自组装单分子膜（SAMs）修饰的金电极上。 HTHP结合到带正电的表面上，但由于活性位点距电极表面的距离较长，因此未发现直接电子转移（DET）。在羧基末端的表面，HTHP的中性电荷底部可以与SAM结合。对于这种“盘”取向，所有六个血红素都靠近电极，它们的直接电子转移应该是有效的。 HTHP在所有带负电荷的SAM上显示出准可逆的氧化还原行为，速率常数k（s）值在0.93至2.86 s（-1）之间，表观形式电位E-app（0）'在-131.1至-249.1 mV之间。在MUA / MU修饰的电极上，最大表面浓度对应于盘方向上六聚HTHP的完整单层。静电固定在带负电荷的SAM上的HTHP显示出过氧化物还原的电催化作用和NADH的酶促氧化作用。

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