 Dan Buttry accepted the position of Professor of the Department of Chemistry & Biochemistry, and started from spring 2008.
Professor Buttry earned a B. A. with highest distinction in chemistry, magna cum laude, in 1979 at the University of Colorado in Colorado Springs. He subsequently attended the California Institute of Technology in Pasadena, receiving a Ph. D. degree in Electrochemistry in 1983. After graduating, he accepted a position as a Member of the Research Staff at IBM’s San Jose Research Lab (now the Almaden Research Lab). In 1985, he moved to the University of Wyoming as an assistant professor, where his research effort was initially focused on applications of the quartz crystal microbalance in electrochemistry and chemical sensor research and development. He became a professor in 1992 and served as head of the department from 1999-2002. His research interests have broadened to include new materials for battery and fuel cell applications, interfacial chemistry in corrosion, and electrochemical behavior of nanoscale materials and nanocomposites. His group has been supported by many agencies and companies, including the National Science Foundation, the Office of Naval Research, the Air Force Office of Scientific Research and the Department of Energy. |
 Yan Liu started in fall 2007 as a assistant professor of the Department of Chemistry and Biochemistry
Dr. Liu has been an assistant research professor of ASU Department of Chemistry and Biochemistry and Biodesign institute since 2004.She graduated from Columbia University with a PhD in chemistry in 2000, and held postdoctoral associate positions at Rockefeller University 2000-2001 and Duke University 2001-2004 before coming to ASU.
Her research program is highly interdisciplinary which combines Chemistry, Biology, Physics and Material Science. Our goal is to develop nanoparticle based multi-component and multi-functional nanostructures using self-assembly and DNA directed self-assembly, to characterize their unique optical properties, and explore their applications in bio-imaging, biosensing, etc.
The nanoparticles used include gold or silver nanoparticles, quantum dots, and magnetic nanoparticles. Surface modification of the nanoparticles by various bioconjugation methods will be explored to generate stable nanoparticles with desirable surface funtionalities. Self-assembly of DNA nanostructures form patterned DNA arrays, and the directed assembly of nanoparticles by the DNA templates generate uniquely functional nanodevices. Taking advantage of the precise spatial control of DNA nanostructures, and tunable size-or distance dependence of the properties of nanoparticles, multi-component structures with unique properties can be created. The various tools we use to characterize the nanoparticle based multi-compoent structures, include the microscopic imaging techniques of optical microscope, AFM, SEM or TEM, and spectral analysis tools, such as UV-Vis, fluorometer, surface Raman spectroscopy, etc.
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 Anne Katherine Jones
D.Phil - Oxford University, 2002
NIH-NRSA Postdoctoral Research Fellow: The Johnson Research Foundation, University of Pennsylvania
Research and Teaching Interests:
The goal of my group is to understand how redox enzymes work and to reproduce their activities in synthetic peptide systems. Why redox enzymes? In addition to their biological roles in energy conversion, chemical transformation, signal transduction, and transport, redox enzymes play important industrial roles in sensors, drugs, green energy production, catalysis, bioremediation of pollutants, and nanotechnology. These proteins are at the interface of biochemistry, inorganic chemistry, physical chemistry and engineering. However, despite their ubiquity, their complex structures have obscured most investigations into mechanism and structure/function relationships. My laboratory will explore the roles of biological materials in tuning the chemistry of both naturally occurring and synthetic redox active prosthetic groups.
Questions to be addressed include:
1. What are the catalytic mechanisms of redox enzymes?
2. How redox enzymes can be re-engineered for use in devices such as fuel cells and biosensors?
3. How multiple redox cofactors in oxidoreductase complexes interact to produce desired chemistry and prevent side reactions?
4. How de novo redox enzymes can be designed to interface with electronic and biological components for technological and medical applications?
Techniques employed in my laboratory will include molecular biology, protein purification, enzymology, direct protein electrochemistry, computer simulations, de novo protein design, FTIR spectroscopy, circular dichroism, solid state peptide synthesis, HPLC, and chemical synthesis.
Representative Publications
T. Burgdorf, O. Lenz, T. Buhrke, E. van der Linden, A. K. Jones, S. Albracht, and B. Friedrich. Functional modules of Aerotolerant [NiFe]-Hydrogenases in Ralstonia eutropha H16, J. Mol. Microbiol. Biotechnol., 2005, 10, 181-196.
A.K. Jones, O. Lenz, A. Strack, T. Buhrke, and B. Friedrich. Hydrogenase active site biosynthesis: Identification of Hyp protein complexes in Ralstonia eutropha. Biochemistry 2004, 43(42), 13467-13477.
A. K. Jones, S. E. Lamle, H. R. Pershad, K. A. Vincent, S. P. J. Albracht, and F. A. Armstrong. Enzyme electrokinetics: electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase. J. Am. Chem. Soc. 2003; 125(28), 8505-14.
A. K. Jones, E. Sillery, S. P. J. Albracht, and F. A. Armstrong. Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst. Chem Commun, 2002; (8):866-7.
A. K. Jones, R. Camba, G. A. Reid, S. K. Chapman, and F. A. Armstrong. Interruption and Time
Resolution of Catalysis by a Flavoenzyme Using Fast Scan Protein Film Voltammetry. J. Am. Chem. Soc., 1999; 122(27): 6494-6495.
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Kevin E. Redding started in spring 2008 as an associate professor. 
