Document Detail

Using synthetic chemistry to understand copper protein active sites: a personal perspective.
MedLine Citation:
PMID:  16447049     Owner:  NLM     Status:  MEDLINE    
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.
William B Tolman
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Review     Date:  2006-01-27
Journal Detail:
Title:  Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry     Volume:  11     ISSN:  0949-8257     ISO Abbreviation:  J. Biol. Inorg. Chem.     Publication Date:  2006 Apr 
Date Detail:
Created Date:  2006-04-04     Completed Date:  2006-06-28     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  9616326     Medline TA:  J Biol Inorg Chem     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  261-71     Citation Subset:  IM    
Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, 207 Pleasant Street SE, Minneapolis, MN 55455, USA.
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MeSH Terms
Binding Sites
Catalytic Domain
Copper / chemistry*
Enzymes / chemistry,  metabolism
Models, Molecular
Proteins / chemistry*
Grant Support
Reg. No./Substance:
0/Enzymes; 0/Proteins; 7440-50-8/Copper

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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