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 language | English (US) |
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Pages (from-to) | 1768-1771 |
Number of pages | 4 |
Journal | Angewandte Chemie - International Edition |
Volume | 40 |
Issue number | 9 |
DOIs | |
State | Published - May 4 2001 |
Keywords
- Anomeric effect
- Cyanides
- Density functional calculations
- Hydrogenases
- S ligands
ASJC Scopus subject areas
- General Chemistry