This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. The overall aim of this research program is to determine how [NiFe]-hydrogenase enzymes are made in bacteria. These enzymes are found in many microorganisms, including Escherchia coli (E. coli) and the pathogenic bacteria 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 active site that contains nickel and iron bound to the protein in addition to several non-protein ligands. It is known that the biosynthesis of hydrogenases requires the coordinated activity of multiple helper proteins to deliver all of the components and assemble the metallocenter correctly. However, very little is known about the mechanisms of action of the individual proteins, how they interrelate with each other, how metal is transferred, 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.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-32
Application #
8362354
Study Section
Special Emphasis Panel (ZRG1-BCMB-P (40))
Project Start
2011-03-01
Project End
2012-02-29
Budget Start
2011-03-01
Budget End
2012-02-29
Support Year
32
Fiscal Year
2011
Total Cost
$279
Indirect Cost
Name
Stanford University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
009214214
City
Stanford
State
CA
Country
United States
Zip Code
94305
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