Models of nitrogen/sulfur containing copper enzymes through synthetic bioinorganic chemistry

CHED 1195

Boram Lee, boram.lee@kysu.edu1, Kayla N. Green, kgreen@mail.chem.tamu.edu2, David A. Rockcliffe, david.rockcliffe@kysu.edu1, and Marcetta Y. Darensbourg, marcetta@mail.chem.tamu.edu2. (1) Division of Mathematics and Sciences, Kentucky State University, 400 E. Main St, Frankfort, KY 40601, (2) Department of Chemistry, Texas A&M University, College Station, TX 77843
Copper is found in many enzymes that perform electron transfer, hydroxylation, oxygenation and oxidation processes. In an attempt to understand the structure/function relationships in copper metalloproteins we are preparing small molecule analogs of the copper binding environment for metalloproteins with nitrogen and sulfur donor groups. We have prepared three complexes with copper in an N2S2 coordination environment: [(CH3CH2)4N]2Cu(II)(ema) (ema = N, N'-ethylenebis(2-mercaptoacetamide); [(CH3CH2)4N]2Cu(II)(emi). 2H2O, (emi = N,N'-ethylenebis(2-(benzylthio)isobutyramide) and Cu(ema)propyl. In addition we prepared Cu(II)-CGC copper-peptide complexes both free and attached to a Rink resin. The results of UV-visible and EPR spectroscopy indicate that the complexes are monomeric with a copper binding environment containing both nitrogen and sulfur donors. Recorded EPR spectra imply that copper(II) has a square planar coordination environment. The poster discusses the preparation and characterization of the copper(II) complexes and compares the structures of the Cu(II)(ema) and Cu(II)(emi) complexes with that of the Cu(II)-(CGC) complexes.
 

Undergraduate Research Poster Session: Inorganic Chemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster

Division of Chemical Education

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008