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.X-ray absorption spectroscopy (XAS) will be used to investigate a series of copper-zinc superoxide dismutase (CuZnSOD) mutants. These mutants all exhibit a decrease in SOD activity and also show perturbations in the EPR and UV-vis spectra of the oxidized enzymes. Cu(II) K-edge XAS will allow for further characterization of the electronic and geometric structure of the oxidized enzyme. Cu(I) K-edge XAS will allow for characterization of the reduced enzyme, which will aid in understanding any alteration in the mechanism in these mutants. Zn K-edge XAS will be used to determine if any changes have occurred at the structural Zn site. These results will be compared to XAS studies on the WT enzyme and may provide important insight into mutant SOD1 enzyme toxicity in amyotrophic lateral sclerosis (ALS).

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-29
Application #
7721808
Study Section
Special Emphasis Panel (ZRG1-BPC-E (40))
Project Start
2008-03-01
Project End
2009-02-28
Budget Start
2008-03-01
Budget End
2009-02-28
Support Year
29
Fiscal Year
2008
Total Cost
$962
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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