Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM035752-11
Application #
2178056
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1986-01-01
Project End
1998-12-31
Budget Start
1996-01-01
Budget End
1996-12-31
Support Year
11
Fiscal Year
1996
Total Cost
Indirect Cost

  Institution

Name
University of Wisconsin Madison
Department
Biochemistry
Type
Other Domestic Higher Education
DUNS #
161202122
City
Madison
State
WI
Country
United States
Zip Code
53715

  Publications

Tang, Kuo-Hsiang; Mansoorabadi, Steven O; Reed, George H et al. (2009) Radical triplets and suicide inhibition in reactions of 4-thia-D- and 4-thia-L-lysine with lysine 5,6-aminomutase. Biochemistry 48:8151-60
Carmieli, Raanan; Larsen, Todd M; Reed, George H et al. (2007) The catalytic Mn2+ sites in the enolase-inhibitor complex: crystallography, single-crystal EPR, and DFT calculations. J Am Chem Soc 129:4240-52
Sims, Paul A; Menefee, Ann L; Larsen, Todd M et al. (2006) Structure and catalytic properties of an engineered heterodimer of enolase composed of one active and one inactive subunit. J Mol Biol 355:422-31
Poyner, Russell R; Anderson, Mark A; Bandarian, Vahe et al. (2006) Probing nitrogen-sensitive steps in the free-radical-mediated deamination of amino alcohols by ethanolamine ammonia-lyase. J Am Chem Soc 128:7120-1
Mansoorabadi, Steven O; Seravalli, Javier; Furdui, Cristina et al. (2006) EPR spectroscopic and computational characterization of the hydroxyethylidene-thiamine pyrophosphate radical intermediate of pyruvate:ferredoxin oxidoreductase. Biochemistry 45:7122-31
Mansoorabadi, Steven O; Padmakumar, Rugmini; Fazliddinova, Nisso et al. (2005) Characterization of a succinyl-CoA radical-cob(II)alamin spin triplet intermediate in the reaction catalyzed by adenosylcobalamin-dependent methylmalonyl-CoA mutase. Biochemistry 44:3153-8
Reed, George H; Mansoorabadi, Steven O (2003) The positions of radical intermediates in the active sites of adenosylcobalamin-dependent enzymes. Curr Opin Struct Biol 13:716-21
Sims, Paul A; Larsen, Todd M; Poyner, Russell R et al. (2003) Reverse protonation is the key to general acid-base catalysis in enolase. Biochemistry 42:8298-306
Poyner, Russell R; Larsen, Todd M; Wong, Se-Wei et al. (2002) Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase. Arch Biochem Biophys 401:155-63
Frey, Perry A; Chang, Christopher H; Ballinger, Marcus D et al. (2002) Kinetic characterization of transient free radical intermediates in reaction of lysine 2,3-aminomutase by EPR lineshape analysis. Methods Enzymol 354:426-35

Showing the most recent 10 out of 40 publications