Biological formation and consumption of molecular hydrogen (H ₂ ) are catalyzed by hydrogenases, of which three phylogenetically unrelated types are known: [NiFe]-hydrogenases, [FeFe]-hydrogenases, and [Fe]-hydrogenase. We present a crystal structure of [Fe]-hydrogenase at 1.75 angstrom resolution, showing a mononuclear iron coordinated by the sulfur of cysteine 176, two carbon monoxide (CO) molecules, and the sp ² -hybridized nitrogen of a 2-pyridinol compound with back-bonding properties similar to those of cyanide. The three-dimensional arrangement of the ligands is similar to that of thiolate, CO, and cyanide ligated to the low-spin iron in binuclear [NiFe]- and [FeFe]-hydrogenases, although the enzymes have evolved independently and the CO and cyanide ligands are not found in any other metalloenzyme. The related iron ligation pattern of hydrogenases exemplifies convergent evolution and presumably plays an essential role in H ₂ activation. This finding may stimulate the ongoing synthesis of catalysts that could substitute for platinum in applications such as fuel cells.

Methanogenic archaea metabolism: Most of the methane on Earth is produced by the metabolism of methanogenic archaea. The final step involves a reaction between methyl-coenzyme M and coenzyme B to give CoM-S-S-CoB and methane. Wagner et al. report a high-resolution structure of the methanogenic heterodisulfide reductase (HdtABC)-[NiFe]-hydrogenase, the enzyme that reduces the disulfide and couples this to the reduction of ferredoxin in an energy-conserving process known as flavin-based electron bifurcation (FBEB) (see the Perspective by Dobbek). The reduced ferredoxin, in turn, drives the first step of methanogenesis. The structure shows how two noncubane [4Fe-4S] clusters perform disulfide cleavage and gives insight into the mechanism of FBEB. Science , this issue p. 699 ; see also p. 642

The long and winding road to methane: The process by which archaea make methane involves a series of reactions and enzymes. First, CO ₂ and methanofuran (MFR) are reduced to formyl-MFR by an as yet unresolved mechanism. Wagner et al. solved the x-ray crystal structure of a tungsten-containing formyl-MFR dehydrogenase complex. Two active sites in the complex are separated by a 43-Å tunnel, which is responsible for transferring the formate made after CO ₂ reduction. The complex also contains a chain of 46 iron-sulfur clusters. Although the exact function of this chain is unclear, it may electronically couple the four tungsten redox centers. Science , this issue p. 114