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

William B. Tolman

Research output: Contribution to journalShort surveypeer-review

65 Scopus citations

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 languageEnglish (US)
Pages (from-to)261-271
Number of pages11
JournalJournal of Biological Inorganic Chemistry
Volume11
Issue number3
DOIs
StatePublished - Apr 1 2006

Keywords

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

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