Hot Article: Hot-wiring enzymes for fuel cells
30 April 2007
Stable enzyme-modified graphite electrodes could be used in fuel cells, according to researchers in Oxford.
Laccases are copper-containing enzymes that use electrons to reduce oxygen to water efficiently, making them of interest as cathodic electrocatalysts in hydrogen-oxygen fuel cells. In this type of fuel cell, hydrogen is oxidised to hydrogen ions and electrons, which flow to the cathode (supplying power) where they reduce oxygen.
Fraser Armstrong and colleagues, at the University of Oxford, have chemically attached anthracene to graphite electrodes to form a stable attachment between the electrode and laccase. Armstrong describes anthracene as 'a long hydrophobic molecule, similar to laccase's own substrate molecules, which can penetrate the active site pocket and approach closely to one of the copper atoms' where the oxygen reduction takes place. The anthracene not only binds the laccase to the electrode, but, as it can conduct electrons, it also delivers the electrons deep into the enzyme close to the site for oxygen reduction.

The anthracene 'plug' modification of the electrode is essential to provide the high and long-term oxygen-reduction activity. Without it, the electrons are not delivered efficiently into the enzyme and the binding of the laccase to the electrode is not stable, both of which leads to reduced activity. The ability to use graphite is also an advantage; it is relatively cheap compared to precious metals, such as gold, which have been previously used as electrodes for laccases.
To complete the fuel cell, Armstrong says that in future research they would like to 'identify rational attachment strategies for other enzymes, particularly hydrogenases, which can be incorporated with laccases to produce small fuel cells'.
Nicola Convine
Link to journal article
A stable electrode for high-potential, electrocatalytic O2 reduction based on rational attachment of a blue copper oxidase to a graphite surface
Christopher F. Blanford, Rachel S. Heath and Fraser A. Armstrong, Chem. Commun., 2007, 1710
DOI: 10.1039/b703114a
