Using synthetic chemistry to understand copper protein active sites: A personal perspective

William B. Tolman

Research output: Contribution to journalShort surveypeer-review

69 Scopus citations


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 languageEnglish (US)
Pages (from-to)261-271
Number of pages11
JournalJournal of Biological Inorganic Chemistry
Issue number3
StatePublished - 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).


  • Copper proteins
  • Dioxygen
  • Nitric oxide
  • Sulfide
  • Thiolate


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