Abstract
The results of studies performed in the author's laboratory are surveyed, with particular emphasis on demonstrating the value of a multidisciplinary synthetic modeling approach for discovering new and unusual chemistry helpful for understanding the properties of the active sites of copper proteins or assessing the feasibility of mechanistic pathways they might follow during catalysis. The discussion focuses on the progress made to date toward comprehending the nitrite reductase catalytic site and mechanism, the electronic structures of copper thiolate electron transfer centers, the sulfidobridged "CuZ" site in nitrous oxide reductase, and the processes of dioxygen binding and activation by mono-and dicopper centers in oxidases and oxygenases.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 261-271 |
| Number of pages | 11 |
| Journal | Journal of Biological Inorganic Chemistry |
| Volume | 11 |
| Issue number | 3 |
| DOIs | |
| State | Published - Apr 2006 |
Bibliographical note
Funding Information:Acknowledgements I am grateful for the hard work and dedication of all of my current and former coworkers at the University of Minnesota, whose names are cited in the references. I also thank my collaborators, in particular E.I. Solomon (advanced spectroscopy), E. Rybak-Akimova and A. Zuberbühler (cryogenic stopped-flow kinetics), and C. Cramer (theory) for their extensive contributions and insights. The Cu bioinorganic chemistry research performed in my group is supported by the NIH (GM47365).
Keywords
- Copper proteins
- Dioxygen
- Nitric oxide
- Sulfide
- Thiolate