Making the H-Cluster from Scratch

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Science  24 Jan 2014:
Vol. 343, Issue 6169, pp. 378-379
DOI: 10.1126/science.1249276

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Many microorganisms use dihydrogen (H2) as an energy vector between and within cells. This process is underpinned by FeFe and NiFe hydrogenases (1), which reversibly combine protons with electrons to give H2 at very high rates. An understanding of the chemical mechanism by which they operate may lead to new technology for biological or bioinspired catalysis (2, 3). Some 15 years ago, crystallographic and spectroscopic studies revealed the essential features of the active site of FeFe hydrogenase, the H-cluster (4). In the H-cluster, a dithiolate-bridged diiron subsite with cyanide and carbon monoxide ligands is linked through a cysteinyl bridge to a 4Fe4S cubane cluster (see the figure). On page 424 of this issue, Kuchenreuther et al. (5) provide insights into the biosynthesis of this unusual structure.