Kinetics of redox polymer-mediated enzyme electrodes.
Oxygen-reducing enzyme electrodes are prepared from laccase of Trametes versicolor and a series of osmium-based redox polymer mediators covering a range of redox potentials from 0.11 to 0.85 V. Experimentally obtained current density generated by the film electrodes is analyzed using a one-dimensional numerical model to obtain kinetic parameters. The bimolecular rate constant for mediation is found to vary with mediator redox potential from 250 s(-1) M(-1) when mediator and enzyme are close in redox potential to 9.4 x 10(4) s(-1) M(-1) when the redox potential difference is large. The value of the bimolecular rate constant for the simultaneously occurring laccase-oxygen reaction is found to be 2.4 x 10(5) s(-1) M(-1). The relationship between mediator-enzyme overpotential and bimolecular rate constant is used to determine the optimum mediator redox potential for maximum power output of a hypothetical biofuel cell with a planar cathode and a reversible hydrogen anode. For laccase of T. versicolor (E(e)(0) = 0.82), the optimum mediator potential is 0.66 V (SHE), and a molecular structure is presented to achieve this result.
Department of Chemical Engineering, Columbia University, New York, New York 10027, USA.
Joshua W
JW
Gallaway
Scott A
SA
Calabrese Barton
D004566:Electrodes; D004798:Enzymes; D007700:Kinetics; D042845:Laccase / Q000737:chemistry* / Q000378:metabolism; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism; D011108:Polymers; D011487:Protein Conformation
D004798:Enzymes; D011108:Polymers; D042845:Laccase; D010100:Oxygen