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.
"A Nickel Phosphine Complex as a Fast and Efficient Hydrogen Production Catalyst," L. Gan, T. L. Groy, P. Tarakeshwar, S. K. S. Mazinani, J. Shearer, V. Mujica, and A. K. Jones, J. Am. Chem. Soc. In Press (2015)
"A Bioelectrochemical Approach to Characterize Extracellular Electron Transfer by Synechocystis sp. PCC6803," A. Cereda, A. Hitchcock, M. D. Symes, L. Cronin, T. S. Bibby, A. K. Jones, PLOS One DOI: 10.1371/journal.pone.0091484 (2014)
"Catalytic Hydrogen Evolution by Fe(II) Carbonyls Featuring a Dithiolate and a Chelating Phosphine," S. Roy, S. K. S. Mazinani, T. L. Groy, L. Gan, P. Tarakeshwar, V. Mujica, A. K. Jones, Inorg. Chem. 53(17) 8919-8929 (2014)
"Biomimetic model for [FeFe]-hydrogenase: Asymmetrically disubstituted diiron complex with a redox-active 2,2'-bipyridyl ligand," S. Roy, T. Groy, A. K. Jones, Dalton Trans. DOI:10.1039/C2DT32457A (2013)
"Metalloenzymes: Cutting out the middleman," S. Roy and A. K. Jones, Nature Chemical Biology 9 603-605 (2013)
"Sequential Oxidations of the Thiolates and the Cobalt Metallocenter in a Synthetic Metallopeptide: Implications for the Biosynthesis of Nitrile Hydratase," A. Dutta, M. Flores, S. Roy, J. Schmitt, G. A. Hamilton, H. E. Hartnett, J. Shearer, A. K. Jones, Inorg. Chem. 52 5236-5245 (2013)
"Transparent gold as a platform for unmediated protein spectroelectrochemistry: investigation of cytochrome c and azurin," I. Ashur, O. Schulz, C. McIntosh, I. Pinkas, R. Ros, A. K. Jones, Langmuir 28 5861-5871 (2012)
"Immobilization of azurin with retention of native electrochemical properties at alkylsilane self-assembled monolayer modified indium tin oxide," I. Ashur, A. K. Jones, Electrochimica Acta 10.1016/j.electacta.2012.08.044 (2012)
"Construction of Heterometallic Clusters in a Small Peptide Scaffold as [NiFe]-Hydrogenase Models: Development of a Synthetic Methodology," A. Dutta, G. A. Hamilton, H. E. Hartnett, A. K. Jones, Inorganic Chemistry http://dx.doi.org/10.1021/ic2026818 (2012)
"Artificial [FeFe] hydrogenase: On resin modification of an amino acid to anchor a diiron-hexacarbonyl cluster in a peptide framework.," S. Roy, S. Shinde, G. A. Hamilton, H. E. Hartnett, A. K. Jones*, Eur. J. Inorg. Chem. 7 1050-1055 (2011)
"The [NiFe]-hydrogenase of the cyanobacterium Synechocystis sp. PCC 6803 is working bidirectionally. ," C. L. McIntosh, F. Germer, R. Schulz, J. Appel, A. K. Jones, J. Am. Chem. Soc. 133(29) 11308-11319 (2011)
"Spectroelectrochemistry of cytochrome c and azurin immobilized in nanoporous antimony tin oxide," P. Kwan, D. Schmitt, A. M. Volosin, C. L. McIntosh, D.-K. Seo, A. K. Jones, Chemical Communications 47 12367-12369 (2011)
"Crystallization and preliminary X-ray crystallographic analysis of the [NiFe] hydrogenase maturation factor HypF1 from Ralstonia eutropha H16," G. Winter, S. Dokel, N. Krauss, A. K. Jones, W. Hohne, B. Friedrich, Acta Cryst. F 66 452-455 (2010)
"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)