Project 171203

The aim of this research is to determine how [NiFe]-hydrogenase enzymes are made in bacteria. These enzymes are found in many microorganisms, including the pathogenic bacteria Escherichia coli and Helicobacter pylori, and they are key components in the metabolic pathways that either make hydrogen gas or use it as an energy source. The enzyme has a complicated catalytic center that contains nickel and iron as well as other components. It is known that the biosynthesis of hydrogenase enzymes requires the coordinated activity of multiple helper proteins to deliver all of the correct components and assemble the metallocenter correctly. However, very little is known about how this molecular factory works. This research is designed to elucidate the molecular details of hydrogenase biosynthesis, with an initial focus on the proteins that insert the nickel into the enzyme center. An understanding of this multi-step process is essential in order to realize the potential of hydrogenase enzymes for biotechnology and consumable energy applications, or to evaluate the component proteins as antibiotic targets. Furthermore, this study will contribute to our knowledge about intracellular transition metal homeostasis, a fundamental aspect of life.

elucidating the molecular details of [NiFe]-hydrogenase biosynthesis in bacteria