Publication date: 8th October 2020
Surface-enhanced infrared absorption (SEIRA) spectroscopy is a powerful technique to understand interfacial events including protein orientation/structure changes and enzymatic reactions at protein/electrode interfaces, which are well known to govern redox properties of redox-active proteins in protein film electrochemistry and redox-based biosensors. Particularly for enzymatic reactions involving infrared-active substrates, SEIRA spectroscopy of enzyme-modified electrodes under potential control allows us to observe reaction intermediates, leading us to gain the mechanistic insight into enzymatic reactions [1]. For example, IR-active nitric oxide (NO) can be efficiently converted to nitrous oxide (N2O) at the binuclear reaction center consisting of a heme and a nonheme iron in a transmembrane metalloenzyme of cytochrome-c-dependent nitric oxide reductase (cNOR). Since NO is highly cytotoxic and reactive with biomolecules, understanding the enzymatic NO reduction mechanism, which remains under debate, would provide insights into the regulation dynamics of cytotoxic NO in biological processes.
Herein, we report electrochemical SEIRA spectra of cNOR-modified gold electrodes under catalytic conditions. The cNOR was immobilized on SEIRA-active gold electrodes via mixed self-assembled monolayers (SAMs) of alkanethiols and then protein-tethered bilayer lipid membranes (BLMs) were constructed at the electrode surface. We will discuss the protein orientation, the BLM assembly kinetics and the reaction intermediate of the enzymatic NO reduction.
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