This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Siderophores are bacterial products which bind iron and increase the rate of bacterial iron transport. Some iron-binding compounds are also known to function in media containing animal or human serum. Since iron sequestration is a known stimulus of bacterial growth during infections, siderophore synthesis has been linked to bacterial virulence. Pseudomonas aeruginosa produces two siderophores under iron-limiting conditions with different chelating properties, pyoverdine (PVD) and pyochelin (PCH). In order to elucidate the nature of the iron siderophore ligands in the two P. Aeruginosa siderophores, we are undertaking low temperature 9.5 GHz EPR studies which are particularly sensitive to the details of the iron ligand structure. This service project complements requests from other center users who wish to use center resources for studies of iron-protein interactions.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR016292-10
Application #
8172145
Study Section
Special Emphasis Panel (ZRG1-BCMB-K (40))
Project Start
2010-09-01
Project End
2011-08-31
Budget Start
2010-09-01
Budget End
2011-08-31
Support Year
10
Fiscal Year
2010
Total Cost
$872
Indirect Cost
Name
Cornell University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
872612445
City
Ithaca
State
NY
Country
United States
Zip Code
14850
Jain, Rinku; Vanamee, Eva S; Dzikovski, Boris G et al. (2014) An iron-sulfur cluster in the polymerase domain of yeast DNA polymerase ?. J Mol Biol 426:301-8
Pratt, Ashley J; Shin, David S; Merz, Gregory E et al. (2014) Aggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypes. Proc Natl Acad Sci U S A 111:E4568-76
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