INOR 612 |
| The active site hydrogen producing Fe-hydrogenases consist of a diiron core with a thiolate-linked [Fe4S4] cluster, cyanide and carbonyl ligands and an azadithiolate bridge. Mimics of these azadithiolate-bridged diiron complexes clusters have been shown to offer a favorable pathway for the catalytic reduction of protons. In this class of active site mimics, a new complex has been prepared which contains electron donating phosphine ligands. Due to the increased electron density around the diiron core, the Fe-Fe bond can be protonated and a bridging hydride is formed. This is the first mimic which can simultaneously hold a hydride and a proton at the basic nitrogen in the azadithiolate bridge, resulting in a milder reduction potential required for the reduction then any other mimics of the Fe-H2ase active site. Due to a remarkable difference in deprotonation kinetics, four protonation states can selectively be prepared and characterized. In this presentation, we will present our latest data on the phosphine complex and discuss further developments of mimics with unexplored ligand patterns. |
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Bioinorganic Chemistry
1:30 PM-5:30 PM, Tuesday, 12 September 2006 Moscone Center -- Room 304, Oral
Division of Inorganic Chemistry |