Copying Biology's Ways with Hydrogen

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Science  08 Feb 2013:
Vol. 339, Issue 6120, pp. 658-659
DOI: 10.1126/science.1233210

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Hydrogen (H2), produced from solar energy and water, offers the ultimate solution for generation and storage of renewable energy. The challenge is to find catalysts suitable for economic large-scale production (made from earth-abundant elements) that can interconvert H2 and water rapidly without a large excess thermodynamic cost (which would waste available energy). The most efficient catalyst for electrolysis of water is the noble metal platinum, but microbes deal very well with H2 by exploiting iron (Fe) and nickel (Ni), dressed up with special ligands and buried inside enzymes known as hydrogenases (1). Hydrogenases are extremely efficient catalysts for producing and oxidizing H2 at rates exceeding thousands per second near the reversible potential, and establishing their mechanism is crucial for future H2 technology (2). On page 682 of this issue, Ogo et al. (3) describe a synthetic analog of the active site of [NiFe]hydrogenases that oxidizes H2 via a hydride-containing intermediate formally equivalent to the most reduced catalytic state of the enzyme.