Biology Department Seminar

An area of investigation by the Basic Biosciences group at NREL is the genetics and biochemistry of H2-metabolism in the green alga Chlamydomonas reinhardtii. Recently we identified in this organism the proteins that function in the biosynthesis of the unique catalytic FeS-cluster, known as the H-cluster, of [FeFe]-hydrogenases. This discovery has led to the development of a recombinant, biosynthetic system for the production of [FeFe]-hydrogenases from both algal and bacterial organisms. Current areas of investigation and collaboration include; 1) enzyme structure and function, 2) 3D-structure determination, 3) biophysical characterization of the catalytic H-cluster, and 4) photobiochemical cell integration to develop models for bio-hybrid H2-production systems. In addition, a collaboration with NREL-CSC and The Beckman Institute at the University of Illinois-Urbana Champaign has led to the development of theoretical methods to study the relationship between [FeFe]-hydrogenase structure and the diffusion properties that are fundamental to H2 catalysis and O2 inactivation. The overall research aims are to better understand how [FeFe]-hydrogenases have evolved to be highly efficient catalysts (kcat ~6000 sec-1), to dissect the mechanisms of O2 inactivation, and to use this knowledge to engineer more robust enzyme-variants for biotechnological applications.