Research Interests

As a structural biochemist I am interested in the general area of structural bioenergetics to understand the molecular basis of energy transduction processes. My laboratory has studied complex metalloproteins and integral membrane proteins, using crystallographic approaches to establish structure and function relationships, particularly for electron-transfer-based energy transduction pathways involving both water-soluble and membrane proteins. Our interest in metalloproteins has centered on proteins that incorporate unusual molybdenum- and tungsten-containing centers, including the iron-molybdenum cofactor of nitrogenase and the more widespread molybdenum cofactor that participate in many of the basic reactions of the biological nitrogen and sulfur cycles. From a structural bioenergetics perspective the nitrogenase structure is also of interest since nitrogenase couples nucleotide hydrolysis to redox chemistry and exhibits striking parallels to nucleotide-dependent signal transduction systems. The membrane protein studies have concenrated on energy transduction processes associated with photosynthesis, respiration, and mechanosensation through structural analysis of the photosynthetic reaction center, fumarate reductase, and a gated mechanosensitive channel.

Membership Type


Election Year


Primary Section

Section 29: Biophysics and Computational Biology

Secondary Section

Section 21: Biochemistry