Better than platinum? Fuel cells energized by enzymes.

Dihydrogen (H2) gas has the potential to be a limitless source of clean energy if simple and efficient methods of production and utilization can be developed. In that regard, using H2 to store electrical energy by means of an electrochemical cell and returning that energy by means of a fuel cell would be among the cleanest and most efficient energy methodologies. This electrochemical apparatus needs to employ robust catalysts for proton reduction and dihydrogen oxidation. In a nonbiological setting, these processes are most readily accomplished at a platinum electrode. Unfortunately, platinum is resource-limited, expensive, and irreversibly inactivated by common trace impurities in H2 gas, such as H2S and CO.

[1]  T. Rauchfuss,et al.  First Generation Analogues of the Binuclear Site in the Fe-Only Hydrogenases: Fe2(μ-SR)2(CO)4(CN)22- , 1999 .

[2]  Michael B. Hall,et al.  Theoretical Characterization of the Reaction Intermediates in a Model of the Nickel−Iron Hydrogenase of Desulfovibrio gigas , 1999 .

[3]  A. Volbeda,et al.  Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases , 2005, JBIC Journal of Biological Inorganic Chemistry.

[4]  J. Meyer,et al.  Classification and phylogeny of hydrogenases. , 2001, FEMS microbiology reviews.

[5]  M. Blomberg,et al.  Mechanism of H-H Activation by Nickel-Iron Hydrogenase , 1998 .

[6]  X Vernede,et al.  The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center. , 1999, Structure.

[7]  W. Hagen,et al.  Direct electrochemistry of Megasphaera elsdenii iron hydrogenase. Definition of the enzyme's catalytic operating potential and quantitation of the catalytic behaviour over a continuous potential range. , 1997, European journal of biochemistry.

[8]  A. Volbeda,et al.  Structure–function relationships of nickel–iron sites in hydrogenase and a comparison with the active sites of other nickel–iron enzymes , 2005 .

[9]  M. Darensbourg,et al.  Carbon Monoxide and Cyanide Ligands in a Classical Organometallic Complex Model for Fe-Only Hydrogenase. , 1999, Angewandte Chemie.

[10]  D. Rittenberg,et al.  The Mechanism of Action of the Enzyme Hydrogenase1 , 1954 .

[11]  J. W. Peters,et al.  Structure and mechanism of iron-only hydrogenases. , 1999, Current opinion in structural biology.

[12]  F. Armstrong,et al.  Electrocatalytic hydrogen oxidation by an enzyme at high carbon monoxide or oxygen levels. , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[13]  M. Haumann,et al.  Structural and oxidation-state changes at its nonstandard Ni-Fe site during activation of the NAD-reducing hydrogenase from Ralstonia eutropha detected by X-ray absorption, EPR, and FTIR spectroscopy. , 2005, Journal of the American Chemical Society.

[14]  M. Adams,et al.  The structure and mechanism of iron-hydrogenases. , 1990, Biochimica et biophysica acta.

[15]  B J Lemon,et al.  A novel FeS cluster in Fe-only hydrogenases. , 2000, Trends in biochemical sciences.

[16]  E. Baerends,et al.  Relativistic DFT calculations of the paramagnetic intermediates of [NiFe] hydrogenase. Implications for the enzymatic mechanism. , 2001, Journal of the American Chemical Society.