Tracking Redox Reactions with Precision: How Top UK and EU Labs Used Advent Wires in Electrochemical-EPR Research

A recent collaboration between leading research groups at Queen Mary University of London, the University of Cambridge, Imperial College London, and the University of Turin has demonstrated a powerful new method to study redox processes in proteins—using materials supplied by Advent Research Materials.

The study, led by Kaltum Abdiaziz and colleagues, introduced a hybrid technique combining protein film electrochemistry (PFE) with electron paramagnetic resonance (EPR) spectroscopy to observe redox reactions directly on immobilised proteins. This method allows scientists to track how proteins exchange electrons—essential for understanding biochemical reactions in areas like enzymology, bioenergetics, and medical research.

High-purity wire for advanced R&D

Advent Research Materials supplied three of the critical components for the custom electrochemical cell:

• Titanium wire (Ti, 98%, 0.320 μm outer diameter): Used to connect the mesoporous indium tin oxide (meso-ITO) working electrode to the potentiostat. The Ti wire was coiled inside the meso-ITO structure to provide a reliable and stable electrical connection without disrupting the porous matrix.
• Platinum wire (Pt, 98%, 0.125 μm outer diameter): Served as the counter electrode within the three-electrode electrochemical system.
• Silver wire (Ag, 98%, 0.125 μm outer diameter): Used as a pseudo-reference electrode, later calibrated against a standard hydrogen electrode for accurate potential control.

All wires were incorporated into a precision-built cylindrical meso-ITO structure, a key innovation in this setup. This structure enabled reliable electrochemical control and allowed the team to freeze samples at specific redox states for subsequent EPR analysis.

Enabling precision spectroscopy in biological redox studies

Using this setup, the team immobilised either Superoxide Dismutase (SOD) or 4-aminoTEMPO molecules onto the electrode surface and investigated their redox behaviour under tightly controlled conditions. The experiments were conducted under anaerobic environments using degassed buffers to ensure data accuracy and protein stability.

The electrodes themselves were functionalised with a self-assembled monolayer using phosphonic acids, then either non-covalently loaded with SOD or covalently bound to 4-aminoTEMPO using EDC/NHS chemistry.

Subsequent EPR spectroscopy—conducted at both the Centre for Advanced ESR (University of Oxford) and Imperial College London—was used to quantify surface-bound molecules and simulate their behaviour. These measurements confirmed that the surface-bound setup offered significantly better sensitivity compared to solution-based methods.

Supporting world-class R&D

This work highlights how advanced materials—such as high-purity wires with precise diameters—play an essential role in cutting-edge bioelectrochemical research.

By supplying the titanium, platinum, and silver wires used in this multi-institutional study, Advent Research Materials continues to support some of the most respected academic labs across Europe and the UK.

We are proud to enable research at this level by supplying reliable, high-purity materials tailored to the demands of experimental science.

If you’re developing next-generation EPR or electrochemical setups and require precision wires or other research-grade metals, get in touch to discuss your requirements.

Full reference:

Study/Article can be found here - https://spiral.imperial.ac.uk/bitstreams/8f92be79-7c9e-462e-83be-31edbce58f2a/download Author(s) Kaltum Abdiaziz, Enrico Salvadori, Katarzyna P. Sokol, Erwin Reisner, Maxie M. Roessler. Protein film-electrochemical EPR spectroscopy as a technique to investigate redox reactions in biomolecules. Queen Mary University of London; University of Turin; University of Cambridge; Imperial College London. [Supplementary Information, 2025].