This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.Our research is focused on determining how [NiFe]-hydrogenase enzymes are synthesized in bacteria such as Escherichia coli. It is known that this process involves the coordinated activity of a number of helper proteins to deliver all the correct components and assemble the hydrogenase metallocenter correctly (1). However, very little is known about the mechanisms of action of the specific components, how they interrelate or interact with each other, or how metal selectivity is achieved. 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.
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