|
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
"Synthetic hydrogenases: Incorporation of an iron carbonyl thiolate into a designed peptide," A. K. Jones, B. R. Lichtenstein, A. Dutta, G. Gordon, P. L. Dutton, J. Am. Chem. Soc. 129, 14844 (2007).
"A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina," K. L. Pankhurst, C. G. Mowat, E. L. Rothery, J. M. Hudson, A. K. Jones, C. S. Miles, M. D. Walkinshaw, F. A. Armstrong, G. A. Reid, and S. K. Chapman, J. Biol. Chem 281, 20589 (2006).
"Functional modules of Aerotolerant [NiFe]-Hydrogenases in Ralstonia eutropha H16," T. Burgdorf, O. Lenz, T. Buhrke, E. van der Linden, A. K. Jones, S. Albracht, and B. Friedrich, . Mol. Microbiol. Biotechnol 10, 181-196 (2005).
"Hydrogenase active site biosynthesis: Identification of Hyp protein complexes in Ralstonia eutropha," A.K. Jones, O. Lenz, A. Strack, T. Buhrke, and B. Friedrich, Biochemistry 43(42), 13467-13477 (2004).
"Enzyme electrokinetics: electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase," A. K. Jones, S. E. Lamle, H. R. Pershad, K. A. Vincent, S. P. J. Albracht, and F. A. Armstrong, J. Am. Chem. Soc 125(28), 8505-14 (2003).
"Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst," A. K. Jones, E. Sillery, S. P. J. Albracht, and F. A. Armstrong, Chem Commun 8, 866-7 (2002).
"Interruption and Time
Resolution of Catalysis by a Flavoenzyme Using Fast Scan Protein Film Voltammetry
," A. K. Jones, R. Camba, G. A. Reid, S. K. Chapman, and F. A. Armstrong, J. Am. Chem. Soc. 122, 6494 (1999).
|
