Dr. Michelle Hamm

Associate Professor of Chemistry
D-302 Gottwald Center for the Sciences
Office: (804) 287-6327
Fax: (804) 287-1897

http://facultystaff.richmond.edu/~mhamm/

Teaching:
Organic Chemistry
Biochemistry

Research:
I use synthetic and physical organic chemistry to address specific biological questions. Currently, my work focuses on 8-oxo-2'-deoxyguanosine (OdG), an abundant DNA lesion that can cause genome mutation and is thought to play a major role in several diseases, including cancer. My group is synthesizing analogs of OdG and incorporating them into short strands of DNA. These analogs have great potential as biochemical tools with which to study the contacts that take place between OdG lesions and other biopolymers. For example, we will use these molecules to study how various nucleotides and enzymes, including polymerases and glycosylases, interact with OdG at the molecular level. These studies will help reveal not only how these lesions lead to DNA mutations, but also how the mutations are prevented and/or removed by DNA repair enzymes. Furthermore, since it has been hypothesized that mutations produced by OdG may trigger the associated diseases, these studies may also provide insight into the link between disease and OdG.

Education:
Ph.D. - University of Chicago

Selected Publications:
Hamm, M.L.; Gill, T.J.*; Nicolson, S.C.*; Summers, M.R.* Substrate Specificity of Fpg (MutM) and hOGG1, Two Repair Glycosylases J. Amer. Chem. Soc. (2007) 129, 7724 – 7725.
 
Hamm, M.L.; Billig, K.* Oligonucleotide Incorporation and Base Pair Stability of
7-Methyl-8-oxo-2’-deoxyguanosine. Org. Biomol. Chem. (2006) 4, 4068-4070.
 
Hamm, M.L.; Rajguru, S.*; Downs, A.M.*; Cholera, R.* Base Pair Stability of 8-Chloro and 8-Iodo-2’-deoxyguanosine Opposite 2’-Deoxycytidine: Implications regarding the Bioactivity of 8-Oxo-2’-deoxyguanosine. J. Amer. Chem. Soc. (2005) 127, 12220-12221.
 
Hamm, M.L.; Cholera, R.*; Hoey, C.L.*; Gill, T.J.* Oligonucleotide Incorporation of 8-Thio-2’-deoxyguanosine Org. Lett. (2004) 6, 3817-3820.

Alecseyev Y., Hamm, M.L., and Essigmann J.M. Aflatoxin B1 Formamidopyrimidine Adducts are Preferentially Repaired by the Nucleotide Excision Repair Pathway in vivo.  Carcinogenesis (2004) 25, 1045-1051.
 
Smela, M.E., Hamm, M.L., Henderson, P.T., Harris, C.M., Harris, T.M., and Essigmann, J.M. The Aflatoxin B1 Formamidopyrimidine Adduct Plays a Major Role in Causing the Types of Mutations Observed in Human Hepatocellular Carcinoma. Proc. Natl. Acacd. Sci. USA (2002) 99, 6655-6660.