This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Recent work has revealed the existence of a novel class of Zn enzymes, in which the Zn appears to function to activate a coordinated thiolate toward nucleophilic attack on an alkyl donor. Work to date has characterized the Zn sites in Ada, in cobalamin-dependent and cobalamin-independent methionine synthase, and in epoxide carboxylase. Additional studies are proposed on the last three of these enzymes, on cobalamide:coenzyme M methyl transferase and farnesyl protein transferase, and on related Zn model compounds. These studies will use both Zn and ligand (S and Se) edge and EXAFS measurements to characterize the structure and function of the Zn sites in these enzy
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