Center for Metalloenzyme Studies

One-third of all known enzymes are metalloenzymes, the unique class of enzymes in which discrete active centers are formed when metal ions or metal-containing cofactors are incorporated into proteins. These enzymes are involved in vital biological processes as respiration, photosynthesis, nitrogen fixation, and oxygen, carbon, sulfur and nitrogen metabolism. In addition metal centers also play crucial roles in regulating gene expression and enzymatic activity. The University of Georgia, recognizing the need for an understanding of these processes, has created the Center for Metalloenzyme Studies (CMS), under the co-direction of Professors Michael K. Johnson (Chemistry) and Michael W. W. Adams (Biochemistry and Molecular Biology).

The CMS currently involves about sixteen faculty members from the Departments of Biochemistry and Molecular Biology, Chemistry, Microbiology, and Genetics, with a combined external research funding base of over $3.5 million. These diverse research groups provide an atmosphere for graduate research unparalleled in this field. This multidisciplinary training environment has been formally recognized by a Research Training Group award to the CMS from the National Science Foundation on The Role of Transition Metals in Biology. This award provides graduate traineeships for students pursuing multi-disciplinary projects in chemistry and biology. It also supports an annual nationally recognized Inorganic Biochemistry Summer Workshop which brings in expert instructors from all over the country to train graduate students and postdoctoral researchers in the techniques and frontier research areas of inorganic biochemistry. A thriving seminar program (the Metalloenzyme Colloquium) gives graduate students the chance to meet and talk with world-renowned scientists doing research on metalloenzymes and related systems.

Graduate students in the CMS have access to a wide variety of important biophysical techniques, and they are able to take advantage of faculty expertise in a wide variety of biological systems as well as in genetic manipulations; collaborations have developed in which recombinant DNA technology and site-directed mutagenesis are being applied as tools for addressing structural and functional questions in a number of metalloenzyme and metalloprotein systems.

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