A [RuRu] Analogue of an [FeFe]‐Hydrogenase Traps the Key Hydride Intermediate of the Catalytic Cycle |
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Authors: | Constanze Sommer Dr. Casseday P. Richers Prof. Dr. Wolfgang Lubitz Prof. Dr. Thomas B. Rauchfuss Dr. Edward J. Reijerse |
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Affiliation: | 1. Max-Planck-Institut für Chemische Energiekonversion, Mülheim an der Ruhr, Germany;2. School of Chemical Sciences, University of Illinois at Urbana-Champaign, Urbana, IL, USA |
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Abstract: | The active site of the [FeFe]‐hydrogenases features a binuclear [2Fe]H sub‐cluster that contains a unique bridging amine moiety close to an exposed iron center. Heterolytic splitting of H2 results in the formation of a transient terminal hydride at this iron site, which, however is difficult to stabilize. We show that the hydride intermediate forms immediately when [2Fe]H is replaced with [2Ru]H analogues through artificial maturation. Outside the protein, the [2Ru]H analogues form bridging hydrides, which rearrange to terminal hydrides after insertion into the apo‐protein. H/D exchange of the hydride only occurs for [2Ru]H analogues containing the bridging amine moiety. |
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Keywords: | hydrides hydrogenases iron metalloenzymes ruthenium |
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