Effects of solvation on the chemistry of amino acid complexes of copper

MEDI 431

David A. Gallagher, dgallagher@cachesoftware.com, CAChe Group, Fujitsu America Inc, 15244 NW Greenbrier Parkway, Beaverton, OR 97006-5733 and Londa Borer, borer@csus.edu, Department of Chemistry, California State University Sacramento, 6000 J Street, Sacramento, CA 95819.
Copper (II) is an essential part of enzymes such as catecholoxidases and tyrosinases. Hence, there is considerable interest in the chemistry of copper with proteins and amino acids.

A conveniently simple model system, copper diglycinate, exists as both cis and trans isomers. While the cis isomer forms in aqueous solution, it is easily converted to the trans form on heating in the solid state. Some authors have suggested that although the trans isomer is more thermodynamically stable, the cis isomer is the kinetic product in aqueous solution. However, quantum chemistry studies reveal a different explanation.

Models of potential reaction pathways from simple intramolecular isomerization to water-catalyzed isomerization in solution, are compared with experimental observations and offer new insights into the coordination chemistry of copper with amino acids.


Poster Session
7:00 PM-9:00 PM, Wednesday, 31 August 2005 Washington DC Convention Center -- Hall A, Poster

Division of Medicinal Chemistry

The 230th ACS National Meeting, in Washington, DC, Aug 28-Sept 1, 2005