Non-heme active sites are found in a variety of mono- and binuclear iron proteins involved in a wide range of biological functions. Containing metal ion sites of unusual ligation and geometry, these proteins often exhibit unique spectral features quite different from those of small molecule transition metal complexes. It has been Dr. Solomon's goal to understand active site spectral features in terms of geometric and electronic structure and to define their contributions to reactivity. He now plans to further characterize the electronic structure of binuclear non-heme iron proteins including hemerythrin, ribonucleotide reductase, acid phosphatase and methane monooxygenase through the use of variable temperature and variable field magnetic circular dichroism, circular dichroism and adsorption spectroscopy techniques.
