Diiron azadithiolates as models for the iron-only hydrogenase active site: Synthesis, structure, and stereoelectronics

Joshua D. Lawrence, Hongxiang Li, Thomas B. Rauchfuss, Marc Bénard, Marie Madeleine Rohmer

Research output: Contribution to journalArticlepeer-review

Abstract

Most hydrogenase enzymes have organometallic active sites with CO and CN- as ligands and metal-metal bonds. Recent evidence points to a novel 2-aza-1,3propanedithiolate cofactor that directly participates in the heterolytic processing of dihydrogen. A close analogue of this cofactor and its organometallic subunit has been synthesized (see picture); spectroscopic, structural, and theoretical analysis of this model provides detailed insights into the properties of the proposed enzyme active site.

Original languageEnglish (US)
Pages (from-to)1768-1771
Number of pages4
JournalAngewandte Chemie - International Edition
Volume40
Issue number9
DOIs
StatePublished - May 4 2001

Keywords

  • Anomeric effect
  • Cyanides
  • Density functional calculations
  • Hydrogenases
  • S ligands

ASJC Scopus subject areas

  • Chemistry(all)

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