个人简介

B.S. Biochemistry, Brigham Young University (1993) Ph.D. Biochemistry, University of Wisconsin-Madison (1998) Postdoctoral Research, Princeton University (1998-2000)

研究领域

Inorganic Chemistry

BIOINORGANIC CHEMISTRY Biological systems require trace amounts of metal ions to sustain life. Metal ions are required at the active sites of many enzymes and are essential to catalyze some of the most energetically demanding reactions in biology. Unfortunately, these highly reactive metal ions also catalyze deleterious reactions for biological systems if the metal ion is permitted to be free in solution. For this purpose biology has evolved elaborate systems to bind and sequester metal ions in non-reactive environments to prevent these dangerous reactions from occurring. A class of proteins referred to as Metallo-chaperone proteins is responsible for binding metal ions when they enter the cell and transport the metal ions to the appropriate location and finally these metallo-chaperones are involved in inserting the metal into the protein that requires metal for catalytic activity. The Watt lab is studying diseases that appear to have disrupted metallo-chaperone systems. Chronic Kidney Disease and Alzheimer’s disease are two diseases that fit into this category. Specifically, iron metabolism appears to have been disrupted leading to free iron. When iron is free in biological systems it catalyzes the formation of superoxide, peroxide and hydroxyl radicals (collectively known as reactive oxygen species or ROS). ROS can cleave DNA, damage proteins and damage lipids. Our research efforts have been focused on metabolites that build up in these diseases. We have performed analysis on how these metabolites disrupt iron loading into ferritin, the iron storage protein or transferrin, the major iron transport protein in the bloodstream. In Chronic Kidney Disease, serum phosphate levels increase because the kidneys are not properly filtering phosphate from the bloodstream. Increased levels of phosphate inhibit iron loading into ferritin by forming insoluble complexes with iron causing free iron to form in the bloodstream that eventually catalyze the formation of ROS. We are now focusing on other metabolites to determine if they also disrupt normal iron loading or release of iron from ferritin. A related project, discovered from the above work focuses on preparing novel materials inside ferritin. Ferritin is a spherical protein with a hollow interior. Ferritin can store up to 4500 iron atoms in its interior and forms mineral particles between 6-8 nm. The size and metal binding ability of ferritin makes it ideal as a bio-nano-reactor to prepare metal nanoparticles of a specific size. We are developing synthetic procedures to make nanomaterials inside ferritin. To date we have prepared iron-molybdate, iron-vanadate and iron-arsenate minerals. We have also prepared iron-platinum, iron-palladium and iron-gold particles. Future work will continue these synthetic procedures and characterize the materials we make for potential nano-magnets, catalysts or quantum dots. We are also working on linking the ferritins to form arrays of the materials we form. Additional research area: Biochemistry

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Shin, K.M., Watt, R.K., Watt, G.D., Choi, S.H., Kim, H.H., Kim, S.I., Kim, S. J., Electrochimica Acta, 2010, 55, 3486-3490. Characterization of ferritin core on redox reactions as a nanocomposite for electron transfer. Hilton, R.J., Keyes, J.D., Watt, R.K., SPIE, 2010, 7646, 764607, 1-10. Photoreduction of Au(III) to form Au(0) nanoparticles using ferritin as a photocatalyst. Hilton, R.J., Keyes, J.D., Watt, R.K., SPIE, 2010, 7646, 76460J, 1-8. Maximizing the efficiency of ferritin as a photocatalyst for applications in an artificial photosynthesis system Zhang, B., Watt, R. K., Galvez, N., Dominguez-Vera, J. M., Watt, G. D., Rate of Iron Transfer through the Horse Spleen Ferritin Shell Determined by Formation of Prussian Blue and Fe-Desferrioxamine in the Ferritin Cavity. Biophysical Chemistry (2006) 120, (2) 96-105. Tyryshkin, A. M., Watt, R. K., Baranov, S. V., Dasgupta, J., Hendrich, M. P., Dismukes, G. C., Spectroscopic evidence for Ca2+ involvement in the assembly of the Mn4Ca cluster in the photosynthetic water-oxidizing complex. Biochemistry (2006) 45, (43) 12876-12889.