Giovanni Gadda
Distinguished University Professor, Chair of Chemistry Biology, Chemistry- Education
B.Sc. (1989): University of Milan, Italy
Ph.D. (1995) : University of Milan, Italy
Postdoctoral Research Associate (1995-2000) : Texas A&M University
- Specializations
Biochemistry
- Biography
Research Interests:
The research interest of my group is in the general area of the mechanistic enzymology of redox enzymes, with a specific interest in flavin-dependent enzymes. The long-term objectives are to understand how enzymes can influence the energetics of reaction intermediates and transition states. These aspects are being studied by steady state kinetics and rapid reaction techniques using pH, viscosity and kinetic isotope effects, as well as mutagenesis, X-ray crystallography and computational approaches.
Several enzymes are currently being investigated. These include:
• Pseudomonas aeruginosa Nitronate monooxygenase
• Cyberlindnera saturnus nitronate monooxygenase
• Neurospora crassa nitronate monooxygenase
• Homo sapiens glycolate oxidase
• Pseudomonas aeruginosa D-arginine dehydrogenase
• Arthrobacter globiformis choline oxidase
• Aspergillus fumigatus choline oxidase
• Trametes ochracea pyranose 2-oxidase
• Halomonas elongata choline dehydrogenase
• Escherichia coli choline dehydrogenase
• Homo sapiens choline dehydrogenaseAwards & Honors:
• Chair (elected), Gordon Research Conference on Enzymes, Coenzymes and Metabolic Pathways, 2015
• Vice Chair (elected), Gordon Research Conference on Enzymes, Coenzymes and Metabolic Pathways, 2014
• International Organizing Committee for the 18th International Symposium on Flavins and Flavoproteins, Thailand
• Organizer, Fifth Southeast Enzyme Conference, 2014
• Guest Editor for Archives of Biochemistry and Biophysics, 2014
• Organizer, Fourth Southeast Enzyme Conference, 2013
• Organizer, Third Southeast Enzyme Conference, 2012
• Organizer, Second Southeast Enzyme Conference, 2011
• Organizing Committee, Third International Conference on Cofactors, 2011
• Organizing Committee, 17th International Symposium on Flavins and Flavoproteins, 2011
• Elected Alternate Councilor of the Division of Biological Chemistry of the ACS, 2011-2013
• Founder, Organizer and Program Chair, First Southeast Enzyme Conference, 2010
• Herty 2011 Medal Award Selection Committee, ACS-GA Section, 2010
• Guest Editor for Archives of Biochemistry and Biophysics, 2009
• Herty 2010 Medal Award Selection Committee, ACS-GA Section, 2009
• Herty 2009 Medal Award Selection Committee, ACS-GA Section, 2008
• Organizing Committee, “Second Interdisciplinary Conference on Vitamins, Coenzymes and Biofactors”, 2008
• Co-organizer, “Strategies in Enzymatic Oxidation Catalysis” Symposium at 234th ACS National Meeting, 2007
• GSU Outstanding Faculty Achievement Award, 2007
• NSF-CAREER, 2006-2011Editorial Boards:
Archives of Biochemistry and Biophysics (2005-present)
ISRN Biochemistry (2012-2013)
International Review of Biophysical Chemistry (2009-2013)
Biochemistry Insights (2008-2013)
Enzyme Research (2009-2013)
Open Enzyme Inhibition Journal (2008-2013)
- Publications
Twenty most recent publications (out of 84):
- Quaye, O., Nguyen, T., Gannavaram, S., Pennati, A., and Gadda, G. (2010) Rescuing of the hydride transfer reaction in the Glu312Asp variant of choline oxidase by a substrate analogue, Arch. Biochem. Biophys., 499, 1-5.
- Finnegan, S., Yuan, H., Wang, Y.F., Orville, A.M., Weber, I., and Gadda, G. (2010) Structural and Kinetic Studies on the Ser101Ala Variant of Choline Oxidase: Catalysis by Compromise, Arch. Biochem. Biophys., 510, 207-213.
- u, G., Yuan, H., Li, C., Lu, C., Gadda, G., and Weber, I. (2010) Conformational Changes and Substrate Recognition in Pseudomonas aeruginosa D-Arginine Dehydrogenase, Biochemistry, 49, 8538-8545.
- Yuan, H., Fu, G., Brooks, P., Weber, I., and Gadda, G. (2010) Steady State Kinetic Mechanism and Reductive Half-Reaction of D-Arginine Dehydrogenase from Pseudomonas aeruginosa, Biochemistry, 49, 9542-9550.
- Pennati, A., and Gadda, G. (2011) Stabilization of an Intermediate in the Oxidative Half Reaction of Human Liver Glycolate Oxidase, Biochemistry, 50, 1-3.
- Yuan, H., and Gadda, G. (2011) Importance of a Serine Proximal to the C(4a)-N(5)Flavin Atoms for Hydride Transfer in Choline Oxidase, Biochemistry, 50, 770-779.
- Fu, G., Yuan, H., Wang, S., Gadda, G., and Weber, I. (2011) Atomic Resolution Structure of an N(5) Flavin Adduct in D-Arginine Dehydrogenase, Biochemistry, 50, 6292-6294.
- Tang, S., Wong, H.C., Wang, Z.M., Hyuang, Y., Zou, J., Zhuo, Y., Pennati, A., Gadda, G., Delbono, O., and Yang, J.J. (2011) Design and Application of a Class of Sensors to Monitor Ca2+ Dynamics in High Ca2+ Concentration Cellular Compartments, Proc. Nat. Acad. Sci., 108, 16265-70.
- Yuan, H., Xin, Y., Hamelberg, D., and Gadda, G. (2011) Insights on the Mechanism of Amine Oxidation Catalyzed by D-Arginine Dehydrogenase Through pH and Kinetic Isotope Effects, J. Am. Chem. Soc., 133, 18957-18965.
- Francis, K., Nishino, S.F., Spain, J.C., and Gadda, G. (2012) A Novel Activity for Fungal Nitronate Monooxygenase: Detoxification of the Metabolic Inhibitor Propionate- 3-Nitronate, Arch. Biochem. Biophys., 521, 84-89.
- Gadda, G. (2012) Oxygen Activation in Flavoprotein Oxidases: the Importance of Being Positive, Biochemistry, 51, 2662-2669.
- Gannavaram, S., and Gadda, G. (2013) Relative Timing of Hydrogen and Proton Transfers in the Reaction of Flavin Oxidation Catalyzed by Choline Oxidase, Biochemistry 52, 1221-1226.
- Smitherman, C., and Gadda, G. (2013) Evidence for a Transient Peroxynitro Acid in the Reaction Catalyzed by Nitronate Monooxygenase with Propionate 3-Nitronate, Biochemistry 52, 2694-2704.
- Lambou, K., Pennati, A., Valsecchi, I., Tada, R., Sherman, S., Sato, H., Beau, R., Gadda, G., and Latgé, J.P. (2013) Pathway of Glycine Betaine Biosynthesis in Aspergillus fumigatus, Eukaryot. Cell 12, 853-863.
- Gadda, G., and Fitzpatrick, P.F. (2013) Solvent Isotope and Viscosity Effects on Steady- State Kinetics of the Flavoprotein Nitroalkane Oxidase, FEBS Lett. 587, 2785-2789.
- Francis, K., Smitherman, C., Nishino, S.F., Spain, J.C.,, and Gadda, G. (2013) The Biochemistry of the Metabolic Poison Propionate 3-Nitronate and its Conjugate Acid, 3- Nitropropionate, IUBMB Life 65, 759-768.
- Salvi, F., and Gadda, G. (2013) Human Choline Dehydrogenase: Medical Promises and Biochemical Challenges, Arch. Biochem. Biophys. 537, 243-252.
- Ouattara, M., Pennati, A., Delvin, D.J., Huang, Y.S., Gadda, G., and Eichenbaum, Z., (2013) Kinetics of Heme Transfer by the Shr NEAT Domains of Group A Streptococcus, Arch. Biochem. Biophys. 538, 71-79.
- Anton, B.P., Chang, Y.C., Brown, P., Choi, H.P., Faller, L.L., Guleria, J., Hu, Z., Klitgord, N., Levy-Moonshine, A., Maksad, A., Mazumdar, V., McGettrick, M., Osmani, L., Pokrzywa, R., Rachlin, J., Swaminathan, R., Allen, B., Housman, G., Monahan, C., Rochussen, K., Tao, K., Bhagwat, A.S., Brenner, S.E., Columbus, L., de Crécy-Lagard, V., Ferguson, D., Fomenkov, A., Gadda, G., Morgan, R.D., Osterman, A.L., Rodionov, D.A., Rodionova, I.A., Rudd, K.E., Söll, D., Spain, J., Xu, S.Y., Bateman, A., Blumenthal, R.M., Bollinger, J.M., Chang, W.S., Ferrer, M., Friedberg, I., Galperin, M.Y., Gobeill, J., Haft, D., Hunt, J., Karp, P., Klimke, W., Krebs, C., Macelis, D., Madupu, R., Martin, M.J., Miller, J.H., O'Donovan, C., Palsson, B., Ruch, P., Setterdahl, A., Sutton, G., Tate, J., Yakunin, A., Tchigvintsev, D., Plata, G., Hu, J., Greiner, R., Horn, D., Sjölander, K., Salzberg, S.L., Vitkup, D., Letovsky, S., Segrè, D., DeLisi, C., Roberts, R.J., Steffen, M., Kasif, S. (2013) The COMBREX Project: Design, Methodology, and Initial Results, PLosS Biol. 11, e1001638.
- Salvi, F., Wang, Y.-F., Weber, I.T., and Gadda, G. (2014) Crystal Structure of Choline Oxidase in Complex with the Reaction Product Glycine Betaine, Acta Cryst. D 70, 405- 413.
- Romero, E., and Gadda, G. (2014) Alcohol Oxidation by Flavoenzymes, Biomolecular Concepts 5, 299-318
- Smitherman, C., Rungsrisuriyachai, K., Germann, M., and Gadda, G. (2015) Identification of the Catalytic Base for
Alcohol Oxidation in Choline Oxidase, Biochemistry, 54, 413-421