Access to the article is free, however registration and sign-in are required. The structure of a novel hydrogenase enzyme provides insights into how molecular hydrogen can be activated for use in biological processes. Hydrogenases are metalloenzymes that catalyze the activation of molecular hydrogen. Microbes usually use this reaction to produce or oxidize H2 in energy-related reactions that involve long-range electron transfer. Structures representing the two classes of "classic hydrogenases" have shown that both contain a binuclear metal center. On page 572 of this issue, Shima et al. (1) describe the structure of a third class of hydrogenase, which contains a mononuclear iron center. In this case, activation of an H2 molecule generates a hydride that is transferred directly to an organic substrate involved in microbial methane production. The structural details revealed by the study are relevant for understanding the H2-activation stage of the catalytic cycle of classic hydrogenases.


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      Hydrogenases,NSDL,NSDL_SetSpec_BEN,oai:nsdl.org:2200/20110722022742144T,H2 oxidation,production of H2 by microbial organisms



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