School of Chemistry, The University of New South Wales, Sydney, NSW 2052, Australia.
Chemistry. 2010 May 25;16(20):5961-8. doi: 10.1002/chem.200903316.
This paper demonstrates the direct electron transfer between the heme moiety of horse hearth cytochrome c and a pyridinyl group on self-assembled-monolayer-modified Si(100) electrodes. Self-assembled monolayers (SAMs) containing the putative receptor ligand were prepared by a step-wise procedure using "click" reactions of acetylene-terminated alkyl monolayers and isonicotinic acid azide derivatives. Unoxidized Si(100) electrodes, possessing either isonicotinate or isonicotinamide receptor ligands, were characterized using X-ray photoelectron spectroscopy, contact-angle goniometry, cyclic voltammetry, and electrochemical impedance spectroscopy. The ability of isonicotinic acid terminated layers to coordinatively bind the redox center of cytochrome c was found to be restricted to pyridinyl assemblies with a para-ester linkage present. The protocol detailed here offers an experimentally simple modular approach to producing chemically well-defined SAMs on silicon surfaces for direct electrochemistry of a well-studied model redox protein.
本文证明了马心细胞色素 c 的血红素部分与自组装单层修饰的 Si(100) 电极上的吡啶基之间的直接电子转移。通过使用乙炔封端的烷基单层和异烟酸叠氮衍生物的“点击”反应，采用逐步程序制备了包含假定受体配体的自组装单层(SAM)。使用 X 射线光电子能谱、接触角测量、循环伏安法和电化学阻抗谱对具有异烟酸酯或异烟酰胺受体配体的未氧化 Si(100)电极进行了表征。发现具有对位酯键的吡啶基组装体限制了终止于异烟酸的层与细胞色素 c 氧化还原中心的配位结合能力。这里详述的方案为在硅表面上产生化学上定义明确的 SAM 提供了一种实验上简单的模块化方法，用于研究充分的模型氧化还原蛋白的直接电化学。
