Insight into metalloenzymes using the synthetic analog approach

CHED 1179

Christopher J. A. Daley, cjdaley@sandiego.edu1, Brendan P. Abolins2, Dustin T. Titus2, Jennifer K. Angelosante2, and David L Tierney, tierney@unm.edu3. (1) Department of Chemistry and Biochemistry, University of San Diego, 5998 Alcala Park, San Diego, CA 92110, (2) Department of Chemistry, Western Washington University, 516 High Street, Bellingham, WA 98225, (3) Department of Chemistry, University of New Mexico, Albuquerque, NM 87131
Nitrile hydratases are of interest as they are used in a wide variety of applications including industrial amide synthesis and the remediation of waste streams. The monometallic Lewis acid active site structure is rare in that it contains two metal-amidato bonds from the peptide backbone as well as bonds from three cysteinate sulfurs. Of note, two of the cysteinate sulfurs have been differentially post-translationally modified (oxidized), which seems to be necessary for activity. The native metal choice, low spin iron(III) or cobalt(III), is atypical owing to the redox chemistry generally observed in systems with high oxidation state metals bonded to thiolates. We used the synthetic analogue approach to study the structure and function of the active site. Our progress on the synthesis and characterization of dissymmetric analogue complexes of cobalt(III) and iron(III) will be presented.
 

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