CMS Faculty

Michael W. W. Adams

Michael W. W. Adams

Georgia Power Professor of Biotechnology
Distinguished Research Professor of Biochemistry & Molecular Biology
Co-Director, Center for Metalloenzyme Studies

The Adams group has a general interest in anaerobic microorganisms, particularly archaea and particularly those growing near and above 100°C, the so-called hyperthermophiles. The archaeon Pyrococcus furiosus and the bacterium Thermotoga maritima are being used as model systems. Projects involve the physiology, metabolism, enzymology, bioinorganic chemistry, and functional and structural genomics of these organisms.

Harry A. Dailey

Harry A. Dailey

Professor of Microbiology and Biochemistry & Molecular Biology
Director of Biomedical and Health Sciences Institute

The Dailey group focuses on the mechanism and regulation of heme biosynthesis in both eukaryotes and prokaryotes. Recent projects and collaborations have examined heme metabolism in a number of model systems including C. elegans (and related human pathogenic nematodes), zebrafish, mice and mammalian cell culture, as well as identifying and characterizing new biosynthetic pathways in bacteria.

Shanta Dhar

Shanta Dhar

Assistant Professor of Chemistry

The Dhar group conducts research at the interface of chemistry and biology with particular emphasis on nanocarrier mediated delivery of metal-based drugs for their potential applications in various diseases and in the development of nano-vaccines. Current research is focused on the development of organelle targeted-nanoparticle-metal complex constructs and nanoparticle assisted targeted delivery for possible applications in cancer, cardiovascular and neurodegenerative diseases. A specific goal is to combine conventional methods of cancer treatment with immunotherapy in a single nanoparticle platform.

Jorge C. Escalante-Semerena

Jorge C. Escalante-Semerena

UGA Foundation Distinguished Professor of Microbiology

The Escalante-Semerena group investigates different aspects of the biosynthesis of coenzyme B12 in archaea and bacteria. Coenzyme B12 (CoB12) is a cobalt-containing tetrapyrrole that is essential to many organisms, including humans. The research has discovered new enzymes and pathways, and has resulted in collaborations with crystallographers and transition-metal spectroscopists to gain insights into the formation of the unique Co-C bond in CoB12. Current research focuses on the assembly of the lower ligand base under oxic and anoxic conditions, the nucleotide loop, as well as the use of CoB12 in cell physiology.

Todd C. Harrop

Todd C. Harrop

Associate Professor of Chemistry

The Harrop group works in the area of synthetic bioinorganic chemistry with emphasis on the design, synthesis, and reactivity of first-row transition metal complexes that model crucial metal-catalyzed reactions in biology that involve reactive oxygen or reactive nitrogen species (ROS and RNS, respectively). This interest has stemmed from the discovery of a new and unusual superoxide dismutase enzyme utilizing nickel as a cofactor (NiSOD) and the rising physiological relevance/medicinal application of the RNS nitroxyl (HNO or NO-). Another active area of interest is the design and construction of fluorescent chemosensors for the selective detection of inorganic arsenic in biological and environmental samples.

Michael K. Johnson

Michael K. Johnson

Distinguished Research Professor of Chemistry
Co-Director, Center for Metalloenzyme Studies

The Johnson group uses biophysical spectroscopic approaches to address the mechanism of assembly or incorporation of biological metal centers and structure/function relationships in metalloenzymes. Spectroscopic methods, including UV-visible-NIR absorption, CD and VTMCD, Mössbauer, EPR, resonance Raman and FTIR spectroscopies, have been used to investigate structure/function relationships involving heme, non-heme Fe, Ni, Co, Mo, and W centers in metalloenzymes. The current primary focus involves elucidation of the mechanism of assembly and repair of biological Fe-S clusters and understanding the diverse roles of Fe-S centers in catalysis, small molecule sensing and regulation.

William N. Lanzilotta

William N. Lanzilotta

Associate Professor of Biochemistry & Molecular Biology

The Lanzilotta group uses crystallographic, biochemical and molecular biology approaches to elucidate the mechanism of metalloenzymes involved with radical reactions, heme biosynthesis and acquisition, and heme sensing and regulatory functions. Current research focuses on the terminal reactions in heme biosynthesis and sensing and the function of the active-site and additional [4Fe-4S] clusters in the ubiquitous radical-SAM enzyme superfamily.

Robert J. Maier

Robert J. Maier

Professor of Microbiology
GRA Ramsey Eminent Scholar of Microbial Physiology

The Maier group is interested in the roles of metals in key enzymes involved in pathogenesis by Helicobacter and Salmonella. This especially includes the roles of nickel for urease and hydrogenase maturation/activation, the mechanisms used by the pathogens to sequester and store nickel, and the roles of the final metal sink enzymes (i.e. hydrogenase or urease) in conferring virulence to pathogens.

Amy E. Medlock

Amy E. Medlock

Assistant Professor of Biochemistry & Molecular Biology

The Medlock group is interested in the identification and characterization of porphyrin and heme transporters and understanding the spatial and temporal regulation of heme synthesis in eukaryotes. Revealing the complete picture of total body heme homeostasis is important for understanding the role of heme in organismal growth and development, and may impact the treatment of diseases including anemias, porphyrias, cancers and infectious diseases.

Robert S. Phillips

Robert S. Phillips

Professor of Chemistry

The Phillips group has played a major role in understanding the substrate specificity and stereospecificity of a thermophilic Zn-containing NADP+-dependent alcohol dehydrogenase. This has led to the discovery that mutations in the active site residues near the Zn site can affect both substrate specificity and the stereochemical configuration of substrates. Another primary focus is the use of hydrostatic pressure to determine quantitatively the effects of alkali metal ions on the allosteric properties of tryptophan synthase.

Ramaraja Ramasamy

Ramaraja Ramasamy

Assistant Professor of Engineering
Adjunct Professor of Chemistry

The Ramasamy group addresses one of the fundamental challenges in the field of bio-electrochemistry, namely establishing electrical communication between the electrodes and the reactive biomolecules. This is the bottleneck for achieving high electron transfer kinetics for electrochemical reactions in systems such as enzymatic fuel cells and biosensors. The issue is critically related to the interaction between the metal redox center of the enzyme and electrode, which is largely dependent on the method of immobilization of metalloenzymes on electrode surfaces. The goal of this research program is to address this problem using unique properties of nanostructured materials.

Walter K. Schmidt

Walter K. Schmidt

Associate Professor of Biochemistry & Molecular Biology

The Schmidt group investigates the molecular cell biology and biochemistry of Zn-dependent metalloproteases associated with production of isoprenylated proteins and destruction of amyloidogenic peptides. This work has ties to Alzheimer’s disease, cancer, progeria, and infectious disease.

Anne O. Summers

Anne O. Summers

Professor of Microbiology

Given the long and little regulated use of Hg in industry, cosmetics, and health care and its abundance in coal, humans increasingly experience chronic and acute exposure to Hg worldwide. The Summers group uses genetic, biochemical, biophysical, and ‘omics tools to dissect the mechanistic bases for Hg transformation by bacteria in the primate microbiome and to understand the difference in toxicity of inorganic and organic mercurials.

Jeffery L. Urbauer

Jeffery L. Urbauer

Associate Professor of Chemistry and Biochemistry & Molecular Biology

Calmodulin is a critical cellular Ca2+ signal transducer, activating hundreds of target proteins – enzymes, receptors, signaling proteins, channel proteins – in response to intracellular Ca2+ spikes and Ca2+ binding. The Urbauer group uses NMR spectroscopy to investigate calmodulin interactions with target proteins and small molecules. Currently, these include the plasma membrane Ca2+-ATPase, estrogen receptor alpha, brain adenylyl cyclase and small drug molecules including antiestrogens. Another active area of interest concerns how oxidative stress and the reversible oxidation of methionine residues in calmodulin adjusts its interactions with proteins and other molecules and how these mediate calmodulin-dependent activation.

Bi-Cheng Wang

Bi-Cheng Wang

Professor of Biochemistry & Molecular Biology
GRA Eminent Scholar of Structural Biology
Director of SER-CAT at APS, Argonne National Laboratory

The Wang group has pioneered the use of synchrotron X-ray diffraction studies for high resolution structural structures of biological molecules, including numerous metalloenzymes. Current work involves the development of a novel technique, termed X-Ray Diffraction Near Edge Spectroscopy (XRDNES) which has the potential of assessing the valence states of individual metals in a protein crystal structure. Once fully developed XRDNES should be a valuable tool in studies of metalloproteins.

William B. Whitman

William B. Whitman

Professor of Microbiology

The Whitman group is interested in the adaptations of prokaryotes to their diverse lifestyles, especially those involved in transformations of biogeochemical importance. Many of these adaptations require unusual metalloenzymes whose biochemical and physiological properties are poorly understood.

Jin Xie

Jin Xie

Assistant Professor of Chemistry

The Xie research group focuses on the development and evaluation of metal-, polymer- or protein-based nanoparticles applicable in an imaging and/or therapeutic context. The resulting products, with unique physical properties, targeting profiles, or theranostic attributes, are emerging as a new generation of therapeutic/imaging formulations that hold great promise to improve patient management and treatment outcomes in a wide range of diseases, especially cancer.


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