Faculty of Environmental Earth Science, Hokkaido University, N10W5, Kita-ku, Sapporo 060-0810, Japan.
Graduate School of Environmental Science, Hokkaido University, N10W5, Kita-ku, Sapporo 060-0810, Japan.
J Phys Chem Lett. 2022 Oct 6;13(39):9165-9170. doi: 10.1021/acs.jpclett.2c01765. Epub 2022 Sep 27.
Effects of interfacial interactions on the electrocatalytic activity of protein-tethered bilayer lipid membranes (ptBLMs) containing cytochrome oxidase (CO) for the oxygen reduction reaction are studied by using protein film electrochemistry and surface-enhanced infrared absorption (SEIRA) spectroscopy. Mammalian CO was immobilized on a gold electrode via self-assembled monolayers (SAMs) of mixed alkanethiols. The protein orientation on the electrode is controlled by SAM-CO interactions and is critical to the cytochrome (cyt ) binding. The CO-phospholipid and CO-cyt interactions modulate the electrocatalytic activity of CO, and more densely packed ptBLMs show higher electrocatalytic activity. Our study indicates that spectroscopic and electrochemical studies of ptBLMs can provide insights into the effects of relatively weak protein-protein and protein-lipid interactions on the enzymatic activity of transmembrane enzymes.
通过蛋白质膜电化学和表面增强红外吸收（SEIRA）光谱法研究了界面相互作用对含细胞色素氧化酶（CO）的蛋白质束缚双层脂质膜（ptBLM）在氧还原反应中电催化活性的影响。通过混合烷硫醇的自组装单层（SAM）将哺乳动物 CO 固定在金电极上。电极上的蛋白质取向受 SAM-CO 相互作用控制，这对细胞色素（cyt ）结合至关重要。CO-磷脂和 CO-cyt 相互作用调节 CO 的电催化活性，更致密的 ptBLM 显示出更高的电催化活性。我们的研究表明，ptBLM 的光谱和电化学研究可以深入了解相对较弱的蛋白质-蛋白质和蛋白质-脂质相互作用对跨膜酶酶活性的影响。
