Dr Corinna Hess
(email at firstname.lastname@example.org)
PhD, California Institute of Technology, 2002
BS, University of Chicago, 1996
Research in my lab is in the area of bioinorganic chemistry; the central theme of my projects is the development of both inorganic and biological catalysts for small molecule and C-H activation reactions. An important aim of the research program is the discovery of 'green' catalytic systems. Work in my lab entails inorganic synthetic methodology, spectroscopy, as well as biochemical and molecular biology techniques.
The two specific projects are described below.
Ligand-Centred Mixed Valence Complexes for Renewable Energy
The development of an artificial photosynthesis system offers a promising alternate fuel cell prospect, but requires efficient catalysts for both oxygen formation and hydrogen production. Research in my lab centres on the development of inorganic catalysts that are capable of carrying out the associated multi-electron redox processes. The strategy for the design of such systems involves the synthesis of bimetallic two-electron mixed valence compounds, via a novel approach that uses redox active ligands. The redox non-innocent organic ligands, in conjunction with the metal centres, provide electron storage sites for multi-electron transformations. Hydrogen production is a chief target of these unique compounds. The mixed-valence compounds thus are highly relevant to renewable energy processes and fuel cell technologies.
In addition to synthetic work, computational and spectroscopic methods are integral to the characterisation of the mixed-valence complexes.
The Design of Artificial Enzymes for Biocatalysis
Another area of research in my lab focuses on the design of artificial enzyme biocatalysts. Towards this goal, synthetic inorganic motifs will be incorporated into protein scaffolds, thereby expanding on the scope of nature's reactivities.The novel approach to enzyme design exploits the reactive properties of late transition metal ions, as well as the beneficial properties of a peptide scaffold. A central target of this research is the construction of non-native metalloenzymes that can be employed for C-H activation reactions. This reaction represents one of the most obstinate chemical transformations that confront synthetic chemists; yet, C-H bond activation is the key element for hydrocarbon functionalisation to generate valuable industrial products.Artificial enzymes offer a new avenue for coordination chemistry and a distinctive approach in the development of environmentally friendly, 'green' catalysts for production processes.
The project is at the intersection of biological and inorganic chemistry. Development of the bioinorganic systems will entail structural analysis, inorganic spectroscopy and reactivity studies in addition to biochemical methods.
Students interested in PhD projects are welcome to contact me at any time.
Undergraduates, at all levels, interested in obtaining research experience also are encouraged to enquire about available opportunities.
Banerjee, P., Company, A., Weyhermüller, T., Bill, E., Hess, C. R.* "Zn and Fe Complexes Containing a Redox Active Macrocyclic Biquinazoline Ligand." Inorg. Chem., 2009, 48, 2944.
Hess, C. R., Weyhermüller, T., Bill, E., Wieghardt, K. "[Fe(TIM)]2: An Fe-Fe Dimer Containing an Unsupported Metal-Metal Bond and Redox Active N4-Macrocyclic Ligands." Angew. Chem. Intl. Ed. 2009, 48, 3703.
Hess, C. R., Welford, R. W. D., Klinman, J. P. "Chemistry of Oxygen Activation by Enzymes." pp 529-540, in Wiley Encyclopedia of Chemical Biology, 2009, Vol. 3, T. P. Beghley (Ed.), Hoboken: John Wiley & Sons.
Hess, C. R., Wu, Z., Ng, A., Gray, E. E., McGuirl, M. A., Klinman, J. P. "Hydroxylase Activity of Met471Cys Tyramine b-Monooxygenase." J. Am. Chem. Soc., 2008, 130, 11939.