The group of Prof. Fridovich has been studying the enzymology and the physiological role of SODs as well as the mechanism of superoxide radical-induced cell damage for more than 20 years. Having the opportunity to work under his guidance I expect to become familiar with the most advanced concepts for the mechanism of superoxide toxicity. This includes the possibility for direct action of superoxide on cell constituents. I'll be able to use quite new methodological approaches such as investigations on mutants lacking protecting enzymes. Furthermore, I'll have free access to the forefront research facilities and, what is the most important, could be able to exchange ideas for new promising aspects of the biochemistry of free radicals.

Agency
National Institute of Health (NIH)
Institute
Fogarty International Center (FIC)
Type
International Research Fellowships (FIC) (F05)
Project #
5F05TW004975-02
Application #
2293051
Study Section
International and Cooperative Projects 1 Study Section (ICP)
Project Start
1994-09-27
Project End
Budget Start
1994-09-27
Budget End
1995-09-26
Support Year
2
Fiscal Year
1994
Total Cost
Indirect Cost
Name
Duke University
Department
Biochemistry
Type
Schools of Medicine
DUNS #
071723621
City
Durham
State
NC
Country
United States
Zip Code
27705
Benov, L T; Beyer Jr, W F; Stevens, R D et al. (1996) Purification and characterization of the Cu,Zn SOD from Escherichia coli. Free Radic Biol Med 21:117-21
Benov, L; Fridovich, I (1995) A superoxide dismutase mimic protects sodA sodB Escherichia coli against aerobic heating and stationary-phase death. Arch Biochem Biophys 322:291-4
Benov, L; Fridovich, I (1995) Superoxide dismutase protects against aerobic heat shock in Escherichia coli. J Bacteriol 177:3344-6
Benov, L; Chang, L Y; Day, B et al. (1995) Copper, zinc superoxide dismutase in Escherichia coli: periplasmic localization. Arch Biochem Biophys 319:508-11
Benov, L T; Fridovich, I (1994) Escherichia coli expresses a copper- and zinc-containing superoxide dismutase. J Biol Chem 269:25310-4