Using Synthetic Chemistry to Understand Copper Protein Active Sites: a Personal Perspective.
From: Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, 207 Pleasant Street SE, Minneapolis, MN 55455, USA. tolman@chem.umn.edu
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
- Publish Date: Apr 2006
- ISSN: 0949-8257
- Volume: 11
- Issue: 3
- Pages: 261-71
- Medium: Print
- Language: English
- Citation (JAMA): Tolman William B, et al. Using Synthetic Chemistry to Understand Copper Protein Active Sites: a Personal Perspective.. J. Biol. Inorg. Chem. Apr 2006;11:261-71
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 sulfido-bridged “CuZ” site in nitrous oxide reductase, and the processes of dioxygen binding and activation by mono- and dicopper centers in oxidases and oxygenases.
Mesh Headings (Keywords): Binding Sites, Catalytic Domain, Copper, Enzymes, Models, Molecular, Proteins
Check for Full Text / PubMed Unique Identifier (PMID): 16447049
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