A [RuRu] Analogue of an [FeFe]-Hydrogenase Traps the Key Hydride Intermediate of the Catalytic Cycle

Constanze Sommer, Casseday P. Richers, Wolfgang Lubitz, Thomas B. Rauchfuss, Edward J. Reijerse

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)5429-5432
Number of pages4
JournalAngewandte Chemie - International Edition
Volume57
Issue number19
DOIs
StatePublished - May 4 2018

Keywords

  • hydrides
  • hydrogenases
  • iron
  • metalloenzymes
  • ruthenium

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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