Inorganic Chemistry Division

Laboratory for Bioinorganic Chemistry

Research Interests

1. Structure and function of copper-containing nitrite reductase.
2. Preparation and functional studies of active site models for the copper-containing active site of nitrite reductase.
3. Structure and function of copper-containing nitrous oxide reductase.
4. Structural biological studies of calcium-containing methanol dehydrogenase and its associated electron transfer proteins.

Metal ions play important roles in maintaining the structure and function of biological systems. Our current work focuses on (1) studies of the structure and functions of metals in proteins (Cu, Ni, Fe, Ca, etc.) by various spectroscopies, recombinant DNA methods, and X-ray crystal structure analysis; and (2) synthesis and structural and functional characterization of transition metal complexes as models for the active sites of metalloproteins. Most metalloproteins studied in our laboratory are isolated from denitrifying bacteria, which play an important role in the terrestrial nitrogen cycle. Denitrification is an anaerobic respiratory pathway by which denitrifying bacteria sequentially reduce nitrate, via nitrite, nitrogen monoxide, and nitrous oxide, to dinitrogen.