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[FeFe]-hydrogenase-catalyzed H2 production in a photoelectrochemical biofuel cell.

Hambourger M, Gervaldo M, Svedruzic D, King PW, Gust D, Ghirardi M, Moore AL, Moore TA.

Center for Bioenergy and Photosynthesis and Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287-1604, USA.

The Clostridium acetobutylicum [FeFe]-hydrogenase HydA has been investigated as a hydrogen production catalyst in a photoelectrochemical biofuel cell. Hydrogenase was adsorbed to pyrolytic graphite edge and carbon felt electrodes. Cyclic voltammograms of the immobilized hydrogenase films reveal cathodic proton reduction and anodic hydrogen oxidation, with a catalytic bias toward hydrogen evolution. When corrected for the electrochemically active surface area, the cathodic current densities are similar for both carbon electrodes, and approximately 40% of those obtained with a platinum electrode. The high surface area carbon felt/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. Similar photocurrents and hydrogen production rates were observed in the photoelectrochemical biofuel cell using either hydrogenase or platinum cathodes.

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PMID: 18205358 [PubMed - indexed for MEDLINE]