Hausinger, Robert P.
University Distinguished Professor
B.S., 1977, University of Wisconsin
Ph.D., 1982, University of Minnesota
Postdoctoral studies: 1982-1984, Massachusetts Institute of Technology
Department of Microbiology and Molecular Genetics
6193 Biomedical Physical Sciences
Michigan State University
East Lansing, MI 48824
Phone: (517) 884-5404
My laboratory investigates microbial physiology and enzymology related to transition metals. In particular, we study mechanisms of catalysis by metalloenzymes and characterize the biosynthesis of protein metallocenters. We use an array of experimental techniques and approaches that includes gene cloning, site-directed mutagenesis, enzyme kinetics, metal ion binding assays, active site peptide studies, biophysical spectroscopic methods, and cellular assays for toxicity, DNA repair, and other processes.
One major emphasis in my laboratory focuses on characterization of lactate racemase, the most recently discovered nickel-containing enzyme. We demonstrated the enzyme contains a tethered niacin-derived pincer complex featuring a nickel-carbon bond (Science) this is the first example of a pincer complex in biology, contrasting with the extensive literature on synthetic pincer complexes by inorganic chemists. We continue to examine the mechanism and biosynthesis (requiring three helper proteins) of this unique cofactor, and are interested in its potential function in other enzymes.
A second area of emphasis centers on several ferrous ion and 2-oxoglutarate dependent hydroxylases (reviewed in a recent book). Prior efforts in this area included work with the fungal enzyme XanA that metabolizes xanthine, the protozoal enzyme JMP1 required for synthesis of base J in trypanosomes, the bacterial enzyme AlkB that repairs DNA damage, and mammalian AlkB homologs that react with AP sites in DNA. We continue our studies of the sulfonate-metabolizing TauD, the paradigm of this enzyme family, using a variety of spectroscopic and other approaches. In addition, current efforts focus on the characterization of bacterial enzymes that generate ethylene or metabolize glutaric acid.