Inorganic iron-sulfur clusters enhance electron transport when used for wiring the NAD-glucose dehydrogenase based redox system.
Overview
Research
Identity
Additional Document Info
Other
View All
Overview
abstract
Wiring the active site of an enzyme directly to an electrode is the key to ensuring efficient electron transfer for the proper performance of enzyme-based bioelectronic systems. Iron-sulfur complexes, the first link between proteins and mediating molecules in the biological electron transport chain(s), possess an intrinsic electron transport capability. The authors demonstrate the application of inorganic iron-sulfur clusters (Fe-S) viz. FeS, FeS2, Fe2S3, and Fe3S4, as molecular wires to mediate electron transport between a glucose-selective redox enzyme and the gold electrode. It is shown that Fe-S can emulate the functionality of the natural electron transport chain. Voltammetric studies indicate a significant improvement in electron transport, surface coverage, and resilience achieved by the Fe-S-based glucose anodes when compared to a conventional pyrroloquinoline quinone (PQQ)-based electrode. The Fe-S-based glucose anodes showed glucose oxidation at a potential of +0.5V vs. Ag/AgCl with Tris-HCl buffer (pH8) acting as a carrier. The current densities positively correlated with the concentrations of glucose in the range 0.1-100mM displaying detection limits of 0.77mM (FeS), 1.22mM (FeS2), 2.95mM (Fe2S3), and 14.57mM (Fe3S4). The metal-anchorable sulfur atom, the strong -coordinating iron atom, the favorable redox properties, low cost, and natural abundance make Fe-S an excellent electron-mediating relay capable of wiring redox active sites to electrode surfaces. Graphical abstract Schematic representation of inorganic iron-sulfur clusters used as molecular wires to facilitate direct electron transfer between NAD-glucose dehydrogenase and the gold electrode. The iron-sulfur based glucose anodes improve current response to selectively sense glucose concentrations in the range 0.1-100mM.
