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Thomas Rauchfuss

Thomas Rauchfuss

Tue, Oct. 21, 2014, 4:30pm - 6:00pm
Frick Chemistry Laboratory, Taylor Auditorium

Synthetic Models for the Hydrogenase Enzymes

In the hydrogenases, Nature employs organometallic reaction centers for production and oxidation of H2. Synthetic models for the active sites show how these enzymes might function and provide powerful concepts for the inorganic chemist as well. Some themes to be discussed include:

  • Proton relays in regulating formation and deprotonation of metal hydrides.
  • Mixed valency in H2 binding and release.
  • M-H regiochemistry: terminal vs bridging hydrides, and in between.

Also discussed will be the mechanistic advantages for bimetallic centers and CO/CN- cofactors. These topics will be presented in the context of my research program that focuses on synthetic organometallic chemistry.

Leading references:

Zaffaroni, R.; Rauchfuss, T. B.; Gray, D. L.; De Gioia, L.; Zampella, G., “Terminal vs Bridging Hydrides of Diiron Dithiolates: Protonation of Fe2(dithiolate)(CO)2(PMe3)4”, J. Am. Chem. Soc. 2012, 134, 19260.

Carroll, M. E.; Barton, B. E.; Rauchfuss, T. B.; Carroll, P. J., “Synthetic Models for the Active Site of the [FeFe]-Hydrogenase: Catalytic Proton Reduction and the Structure of the Doubly Protonated Intermediate”, J. Am. Chem. Soc. 2012, 134, 18843.

Manor, B. C.; Rauchfuss, T. B., “Hydrogen Activation by Biomimetic [NiFe]-Hydrogenase Model Containing Protected Cyanide Cofactors”, J. Am. Chem. Soc. 2013, 135, 11895.

Huynh, M. T.; Schilter, D.; Hammes-Schiffer, S.; Rauchfuss, T. B., “Protonation of Nickel–Iron Hydrogenase Models Proceeds after Isomerization at Nickel”, J. Am. Chem. Soc. 2014, 136, 12385.