Spectroscopy & characterization of Metalloenzymes & Biomimetic complexes
Metalloproteins are essential for the basic processes of life, including DNA synthesis, metabolism, photosynthesis, detoxification, and the chemical transformations of nitrogen, oxygen, and carbon molecules required for life. Many diseases are due to metal imbalances or inactivity of critical metalloenzymes. Metalloenzymes are nature’s amazing catalytic centers, transforming the most stable chemical bonds in nature, and thus are important factors for health, agriculture, and the environment.
Our focus is an atomic level understanding of catalytic function. We achieved this through isolation and spectroscopic characterization of intermediates of reaction cycles of enzymes and biomimetic complexes. The metals of interest are probed with a combination of EPR, ENDOR, Mössbauer spectroscopies, or SQUID magnetization. We have developed new spectroscopic instrumentation, computer simulation software, and quantitative methodologies specifically suited to probe metalloproteins and metal complexes.
PhD 1988, University of Illinois
Carnegie Mellon University
Department of Chemistry
4400 Fifth Avenue
Pittsburgh, PA 15213
Phone: (412) 268-1058
Fax: (412) 268-1061