| Abstract
| - The Clostridium acetobutylicum [FeFe]-hydrogenase HydA has been investigated as a hydrogenproduction catalyst in a photoelectrochemical biofuel cell. Hydrogenase was adsorbed to pyrolytic graphiteedge and carbon felt electrodes. Cyclic voltammograms of the immobilized hydrogenase films reveal cathodicproton reduction and anodic hydrogen oxidation, with a catalytic bias toward hydrogen evolution. Whencorrected for the electrochemically active surface area, the cathodic current densities are similar for bothcarbon electrodes, and ∼40% of those obtained with a platinum electrode. The high surface area carbonfelt/hydrogenase electrode was subsequently used as the cathode in a photoelectrochemical biofuel cell.Under illumination, this device is able to oxidize a biofuel substrate and reduce protons to hydrogen. Similarphotocurrents and hydrogen production rates were observed in the photoelectrochemical biofuel cell usingeither hydrogenase or platinum cathodes.
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