Inorganic chemistry is concerned with the properties and behavior of inorganic compounds. This field covers all chemical compounds except the myriad organic compounds (carbon-based compounds, usually containing C-H bonds), which are the subjects of organic chemistry. The distinction between the two disciplines is far from absolute, and there is much overlap, most importantly in the sub-discipline of organometallic chemistry. Inorganic chemistry research in the Department spans the continuum from small molecule systems to metalloproteins, from the investigation of the reactivity properties of synthetic complexes to the use of metal-based reagents for probing protein-DNA interactions.
John Caradonna – Bioinorganic chemistry
The Caradonna Group is interested in the biological chemistry of non-heme iron. Approaches include the investigation of synthetic reactivity models, biophysical and mechanistic studies of natural metalloenzymes, and the rational design of metalloproteins. The Caradonna Group is investigating the chemistry of phenylalanine hydroxylase (PAH), a non-heme iron pterin-dependent monooxygenase that catalyzes the conversion of phenylalanine to tyrosine. Defects in PAH, which cause classic phenylketonuria (PKU), increase serum phenylalanine concentrations and result in abnormal accumulation of phenylalanine-based metabolic products. These products cause defective myelination of the central nervous system and result in postnatal brain damage and severe mental retardation. PKU is the most common inborn error in amino acid metabolism of clinical importance (1 in 50 individuals carry the disease trait, with an average incidence of 1 in 10,000 for Caucasians). The non-heme iron PAH-active site is of additional interest because it performs the same spectrum of chemical transformations as cytochrome P450 without benefit of a heme prosthetic group. The Group utilizes a variety of enzyme mechanistic, molecular biological, and biophysical techniques to investigate the mechanism of both wild type enzyme and selected mutants that induce PKU in humans.
Linda Doerrer – Synthetic inorganic chemistry
The Doerrer Group specializes in synthetic inorganic chemistry and is an equal-opportunity element utilizer. Currently it is pursuing two main avenues of research. The first is the use of highly fluorinated aryloxide and alkoxide ligands for the stabilization of high oxidation states in first-row transition metals. Spectroscopic work strongly suggests that these ligands generate a stronger field environment than chloride and might be fluoride mimics. They have prepared many phenolate anions of the form [M(OAr)n]m- and are investigating their reactivity with strong oxidizing agents. The second area of research is in metallophilicity, which is the attraction of electron rich metal centers e.g. Au(I), Pt(II), for each other. They are investigating the use of this relatively weaker attractive force in combination with electrostatics to form chain of metal atoms that can be prepared with odd numbers of spins and investigated as low-dimensional conductors.
Sean Elliott – Bioinorganic chemistry and Metallobiochemistry
The Elliott Group uses Protein film voltammetry (PFV) to explore the electron transfer pathways and redox-dependent catalytic chemistry of complex metalloproteins such as sulfite reductase and multicopper oxidases. They also develop proteomic tools to enable probing the ‘metallome’ — a complete read-out of the metal-binding components of biological pathways. These experiments provide insights into the role of metal ions in biological chemistry.