Electrocatalytic hydrogen oxidation by an enzyme at high carbon monoxide or oxygen levels.
Use of hydrogen in fuel cells requires catalysts that are tolerant to oxygen and are able to function in the presence of poisons such as carbon monoxide. Hydrogen-cycling catalysts are widespread in the bacterial world in the form of hydrogenases, enzymes with unusual active sites composed of iron, or nickel and iron, that are buried within the protein. We have established that the membrane-bound hydrogenase from the beta-proteobacterium Ralstonia eutropha H16, when adsorbed at a graphite electrode, exhibits rapid electrocatalytic oxidation of hydrogen that is completely unaffected by carbon monoxide [at 0.9 bar (1 bar = 100 kPa), a 9-fold excess] and is inhibited only partially by oxygen. The practical significance of this discovery is illustrated with a simple fuel cell device, thus demonstrating the feasibility of future hydrogen-cycle technologies based on biological or biologically inspired electrocatalysts having high selectivity for hydrogen.
Vincent
Kylie A
KA
Inorganic Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QR, United Kingdom.
Cracknell
James A
JA
Lenz
Oliver
O
Zebger
Ingo
I
Friedrich
Bärbel
B
Armstrong
Fraser A
FA
D015374:Biosensing Techniques; D002248:Carbon Monoxide / Q000378:metabolism*; D002384:Catalysis; D020118:Cupriavidus necator / Q000201:enzymology*; D004563:Electrochemistry; D006864:Hydrogenase / Q000737:chemistry / Q000502:physiology*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism*; D017550:Spectroscopy, Fourier Transform Infrared
D002248:Carbon Monoxide; D006864:Hydrogenase; D010100:Oxygen