Impact of membrane protein-lipid interactions on formation of bilayer lipid membranes on SAM-modified gold electrode

Abstract

In protein film electrochemistry for redox-active membrane proteins, the reconstitution of protein-tethered bilayer lipid membranes (ptBLMs) can maximize their functionality and stability at electrolyte/electrode interfaces. To understand the impact of protein–lipid interactions on the ptBLM formation, we tracked the reconstitution process of a lipid bilayer in the presence or the absence of a transmembrane enzyme of cytochrome c-dependent nitric oxide reductase (cNOR) on a mixed self-assembled monolayer (SAM)/Au electrode. Time-resolved surface-enhanced infrared absorption (SEIRA) spectroscopy and electrochemical measurements revealed that the protein–lipid interaction affected the formation kinetics for the phospholipid bilayer and the electrocatalytic stability of the cNOR-modified electrode but not the fluidity of the phospholipid bilayer.