Electrochemistry of Strongly Adsorbed Heme Proteins

这个项目属于分析化学和表面化学的一般领域，以及生物电化学、电子转移和修饰电极的子领域。将对固定化蛋白质在电极上发生氧化还原反应的界面电子转移反应进行基础研究。该结果将有助于阐明酶与导电材料之间的电子耦合。它们还将提供对生物电子转移过程的见解，因为“蛋白质/电极复合物”可以被认为是生理蛋白质/蛋白质复合物的类似物。将采用各种电化学和光谱方法。吸附等温线、蛋白质取向、吸附物原生性和电子转移激活参数将被确定。将研究吸附在氧化锡电极上的血红素蛋白细胞色素c、细胞色素c552和细胞色素c过氧化物酶，以评估电子转移距离和静电表面相互作用作为速率控制因素的作用。系统地研究氧化还原反应中吸附蛋白的电化学特性将有助于阐明电子转移在生物系统中的作用。研究结果也将有助于设计高效的生物探针和传感器。

This project is in the general area of analytical and surface chemistry and in the subfields of bioelectrochemistry, electron transfer and modified electrodes. A fundamental investigation of the interfacial electron transfer reactions of immobilized proteins that undergo oxidation-reduction reactions on electrodes will be undertaken. The results will help to elucidate the electronic coupling between enzymes and electronically conducting materials. They will also provide insight into biological electron transfer processes as "protein/electrode complexes" can be considered analogues of physiological protein/protein complexes. A variety of electrochemical and spectroscopic methods will be employed. Adsorption isotherms, protein orientation, adsorbate nativeness and electron transfer activation parameters will be determined. The heme proteins cytochrome c, cytochrome c552, and cytochrome c peroxidase, adsorbed on tin oxide electrodes, will be investigated to enable evaluation of the roles of electron transfer distance and electrostatic surface interactions as rate-controlling factors. Systematic study of the electrochemical characteristics of adsorbed proteins that undergo oxidation-reduction reactions will aid in elucidating the role of electron transfer in biological systems. The results will also aid in the design of efficient biological probes and sensors.